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Conserved domains on  [gi|4874275|gb|AAD31340|]
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Similar to gb|L26291 clathrin-associated protein unc-101 from Caenorhabditis elegans and is a member of the PF|00928 Adapter complexes medium subunit family [Arabidopsis thaliana]

Protein Classification

AP-1 complex subunit mu( domain architecture ID 13000723)

AP-1 complex subunit mu is a subunit of the clathrin-associated adaptor protein complex 1 that plays a role in protein sorting at the trans-Golgi network and early endosomes (TGN/EE)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AP-1_Mu1_Cterm cd09250
C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex ...
156-426 1.68e-177

C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1 subunit, which includes two closely related homologs, mu1A (encoded by ap1m1) and mu1B (encoded by ap1m2). Mu1A is ubiquitously expressed, but mu1B is expressed exclusively in polarized epithelial cells. AP-1 has been implicated in bi-directional transport between the trans-Golgi network (TGN) and endosomes. It plays an essential role in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Epithelial cell-specific AP-1 is also involved in sorting to the basolateral surface of polarized epithelial cells. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


:

Pssm-ID: 271158  Cd Length: 272  Bit Score: 495.97  E-value: 1.68e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  156 TNSVSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLEAQGRAIKGKAID 235
Cdd:cd09250   1 TNAVSWRPEGIKYKKNEVFLDVIESVNLLVDLNGQVLRSEIVGAIKMRSYLSGMPELKLGLNDKVLFEATGRSSKGKAVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  236 LEDIKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEMLVKARSQFKDRSYATSVEI 315
Cdd:cd09250  81 LEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLSTQVKPLIWVEPTVERHSRSRVEIMVKAKTQFKRRSTANNVEI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  316 ELPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEEATP-ERKAPIRVKFEIPKFIVSG 394
Cdd:cd09250 161 RIPVPPDADSPRFKCSAGSVVYAPEKDALLWKIKSFPGGKEFSMRAEFGLPSIESEEEQGtEKKAPIQVKFEIPYFTVSG 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 4874275  395 IQVRYLKIIEKSGYQAHPWVRYITMAGEYELR 426
Cdd:cd09250 241 LQVRYLKIIEKSGYQALPWVRYITQSGDYYIR 272
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
6-145 3.46e-82

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


:

Pssm-ID: 341439  Cd Length: 139  Bit Score: 248.62  E-value: 3.46e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    6 SALFLLDIKGRVLVWRDYRGDVTAAQAERFFTKLIETEGDSqSNDPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLLF 85
Cdd:cd14835   1 SAIFILDLKGKVLISRNYRGDVPMSVIEKFMPLLMEKEEEG-NLTPILTDGGVTYIYIKHNNLYLLAVTKKNANAAMVLS 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275   86 FLHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEFIKTDAYRM 145
Cdd:cd14835  80 FLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMMDFGYPQTTESKILQEYITQESHKL 139
 
Name Accession Description Interval E-value
AP-1_Mu1_Cterm cd09250
C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex ...
156-426 1.68e-177

C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1 subunit, which includes two closely related homologs, mu1A (encoded by ap1m1) and mu1B (encoded by ap1m2). Mu1A is ubiquitously expressed, but mu1B is expressed exclusively in polarized epithelial cells. AP-1 has been implicated in bi-directional transport between the trans-Golgi network (TGN) and endosomes. It plays an essential role in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Epithelial cell-specific AP-1 is also involved in sorting to the basolateral surface of polarized epithelial cells. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271158  Cd Length: 272  Bit Score: 495.97  E-value: 1.68e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  156 TNSVSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLEAQGRAIKGKAID 235
Cdd:cd09250   1 TNAVSWRPEGIKYKKNEVFLDVIESVNLLVDLNGQVLRSEIVGAIKMRSYLSGMPELKLGLNDKVLFEATGRSSKGKAVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  236 LEDIKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEMLVKARSQFKDRSYATSVEI 315
Cdd:cd09250  81 LEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLSTQVKPLIWVEPTVERHSRSRVEIMVKAKTQFKRRSTANNVEI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  316 ELPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEEATP-ERKAPIRVKFEIPKFIVSG 394
Cdd:cd09250 161 RIPVPPDADSPRFKCSAGSVVYAPEKDALLWKIKSFPGGKEFSMRAEFGLPSIESEEEQGtEKKAPIQVKFEIPYFTVSG 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 4874275  395 IQVRYLKIIEKSGYQAHPWVRYITMAGEYELR 426
Cdd:cd09250 241 LQVRYLKIIEKSGYQALPWVRYITQSGDYYIR 272
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
159-427 2.01e-113

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 333.12  E-value: 2.01e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    159 VSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLeaqgraikgkaIDLED 238
Cdd:pfam00928   1 VPWRPPGIKYKKNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDKLLL-----------IELDD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    239 IKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLST-QVKPLIWVEAHIERHSR-SRVEMLVKARSQFKDRSYATSVEIE 316
Cdd:pfam00928  70 VSFHQCVNLDKFESERVISFIPPDGEFELMRYRLSTnEVKLPFTVKPIVSVSGDeGRVEIEVKLRSDFPKKLTAENVVIS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    317 LPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEEATPERKAPIRVKFEIPKFIVSGIQ 396
Cdd:pfam00928 150 IPVPKEASSPVLRVSDGKAKYDPEENALEWSIKKIPGGNESSLSGELELSVESSSDDEFPSDPPISVEFSIPMFTASGLK 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 4874275    397 VRYLKIIEKSgYQAHPWVRYITMAGEYELRL 427
Cdd:pfam00928 230 VRYLKVEEEN-YKPYKWVRYVTQSGSYSIRI 259
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
6-145 3.46e-82

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341439  Cd Length: 139  Bit Score: 248.62  E-value: 3.46e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    6 SALFLLDIKGRVLVWRDYRGDVTAAQAERFFTKLIETEGDSqSNDPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLLF 85
Cdd:cd14835   1 SAIFILDLKGKVLISRNYRGDVPMSVIEKFMPLLMEKEEEG-NLTPILTDGGVTYIYIKHNNLYLLAVTKKNANAAMVLS 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275   86 FLHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEFIKTDAYRM 145
Cdd:cd14835  80 FLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMMDFGYPQTTESKILQEYITQESHKL 139
 
Name Accession Description Interval E-value
AP-1_Mu1_Cterm cd09250
C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex ...
156-426 1.68e-177

C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1 subunit, which includes two closely related homologs, mu1A (encoded by ap1m1) and mu1B (encoded by ap1m2). Mu1A is ubiquitously expressed, but mu1B is expressed exclusively in polarized epithelial cells. AP-1 has been implicated in bi-directional transport between the trans-Golgi network (TGN) and endosomes. It plays an essential role in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Epithelial cell-specific AP-1 is also involved in sorting to the basolateral surface of polarized epithelial cells. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271158  Cd Length: 272  Bit Score: 495.97  E-value: 1.68e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  156 TNSVSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLEAQGRAIKGKAID 235
Cdd:cd09250   1 TNAVSWRPEGIKYKKNEVFLDVIESVNLLVDLNGQVLRSEIVGAIKMRSYLSGMPELKLGLNDKVLFEATGRSSKGKAVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  236 LEDIKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEMLVKARSQFKDRSYATSVEI 315
Cdd:cd09250  81 LEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLSTQVKPLIWVEPTVERHSRSRVEIMVKAKTQFKRRSTANNVEI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  316 ELPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEEATP-ERKAPIRVKFEIPKFIVSG 394
Cdd:cd09250 161 RIPVPPDADSPRFKCSAGSVVYAPEKDALLWKIKSFPGGKEFSMRAEFGLPSIESEEEQGtEKKAPIQVKFEIPYFTVSG 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 4874275  395 IQVRYLKIIEKSGYQAHPWVRYITMAGEYELR 426
Cdd:cd09250 241 LQVRYLKIIEKSGYQALPWVRYITQSGDYYIR 272
AP-1_Mu1A_Cterm cd09258
C-terminal domain of medium Mu1A subunit in ubiquitously expressed clathrin-associated adaptor ...
155-426 7.70e-153

C-terminal domain of medium Mu1A subunit in ubiquitously expressed clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1A subunit encoded by ap1m1 gene, which is ubiquitously expressed in all mammalian tissues and cells. AP-1 has been implicated in bidirectional transport between the trans-Golgi network (TGN) and endosomes. It is involved in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). The ubiquitous AP-1 is recruited to the TGN membrane, as well as to immature secretory granules. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1A subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271166  Cd Length: 270  Bit Score: 433.54  E-value: 7.70e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  155 VTNSVSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLEAQGRAiKGKAI 234
Cdd:cd09258   1 VTNAVSWRSEGIKYRKNEVFLDVIESVNLLVSANGNVLRSEIVGSIKMRVYLSGMPELRLGLNDKVLFENTGRG-KSKSV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  235 DLEDIKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEMLVKARSQFKDRSYATSVE 314
Cdd:cd09258  80 ELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIERHSHSRVEYMIKAKSQFKRRSTANNVE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  315 IELPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEEatPERKAPIRVKFEIPKFIVSG 394
Cdd:cd09258 160 IHIPVPNDADSPKFKTTVGSVKYVPENSEIVWSIKSFPGGKEYLMRAHFGLPSVESEE--KEGRPPISVKFEIPYFTTSG 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 4874275  395 IQVRYLKIIEKSGYQAHPWVRYITMAGEYELR 426
Cdd:cd09258 238 IQVRYLKIIEKSGYQALPWVRYITQNGDYQLR 269
AP-1_Mu1B_Cterm cd09259
C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated ...
156-426 5.35e-146

C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1B subunit encoded by ap1m2 gene exclusively expressed in polarized epithelial cells. Epithelial cell-specific AP-1 is used to sort proteins to the basolateral plasma membrane, which involves the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). The phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic reside-binding. Besides, AP-1 mu1B subunit mediates the basolateral recycling of low-density lipoprotein receptor (LDLR) and transferrin receptor (TfR) from the sorting endosomes, where the basolateral sorting signal does not belong to the tyrosine-based signals. Thus, the binding site in mu1B subunit of AP-1 for the signals of LDLR and TfR might be distinct from that for YXXPhi signals.


Pssm-ID: 271167  Cd Length: 268  Bit Score: 416.34  E-value: 5.35e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  156 TNSVSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLEAQGRAiKGKAID 235
Cdd:cd09259   1 TNAVSWRSEGIKYKKNEVFIDVIESVNVLVNANGSVLSSEIVGCIKLKVFLSGMPELRLGLNDRVLFELTGRD-KNKTVE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  236 LEDIKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEMLVKARSQFKDRSYATSVEI 315
Cdd:cd09259  80 LEDVKFHQCVRLSRFENDRTISFIPPDGDFELMSYRLNTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  316 ELPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEEAtpERKAPIRVKFEIPKFIVSGI 395
Cdd:cd09259 160 RVPVPSDADSPKFKTSVGSAKYVPEKNVVVWSIKSFPGGKEYLMRAHFGLPSVENEEL--EGKPPITVKFEIPYFTVSGI 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 4874275  396 QVRYLKIIEKSGYQAHPWVRYITMAGEYELR 426
Cdd:cd09259 238 QVRYMKIIEKSGYQALPWVRYITQSGDYQLR 268
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
159-427 2.01e-113

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 333.12  E-value: 2.01e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    159 VSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLeaqgraikgkaIDLED 238
Cdd:pfam00928   1 VPWRPPGIKYKKNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDKLLL-----------IELDD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    239 IKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLST-QVKPLIWVEAHIERHSR-SRVEMLVKARSQFKDRSYATSVEIE 316
Cdd:pfam00928  70 VSFHQCVNLDKFESERVISFIPPDGEFELMRYRLSTnEVKLPFTVKPIVSVSGDeGRVEIEVKLRSDFPKKLTAENVVIS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    317 LPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEEATPERKAPIRVKFEIPKFIVSGIQ 396
Cdd:pfam00928 150 IPVPKEASSPVLRVSDGKAKYDPEENALEWSIKKIPGGNESSLSGELELSVESSSDDEFPSDPPISVEFSIPMFTASGLK 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 4874275    397 VRYLKIIEKSgYQAHPWVRYITMAGEYELRL 427
Cdd:pfam00928 230 VRYLKVEEEN-YKPYKWVRYVTQSGSYSIRI 259
AP-2_Mu2_Cterm cd09251
C-terminal domain of medium Mu2 subunit in ubiquitously expressed clathrin-associated adaptor ...
168-426 1.54e-111

C-terminal domain of medium Mu2 subunit in ubiquitously expressed clathrin-associated adaptor protein (AP) complex AP-2; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, -2, -3, and -4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 2 (AP-2) medium mu2 subunit. Mu2 is ubiquitously expressed in mammals. In higher eukaryotes, AP-2 plays a critical role in clathrin-mediated endocytosis from the plasma membrane in different cells. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-2. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-2 mu2 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding. Since the Y-X-X-Phi binding site is buried in the core structure of AP-2, a phosphorylation induced conformational change is required when the cargo molecules binds to AP-2. In addition, the C-terminal domain of mu2 subunit has been shown to bind other molecules. For instance, it can bind phosphoinositides, in particular PI[4,5]P2, which might be involved in the recognition process of the tyrosine-based signals. It can also interact with synaptotagmins, a family of important modulators of calcium-dependent neurosecretion within the synaptic vesicle (SV) membrane. Since many of the other endocytic adaptors responsible for biogenesis of synaptic vesicles exist, in the absence of AP-2, clathrin-mediated endocytosis can still occur. However, the cells may not survive in the complete absence of clathrin as well as AP-2.


Pssm-ID: 271159  Cd Length: 263  Bit Score: 328.40  E-value: 1.54e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  168 FKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLEAQGR-----AIKGKAIDLEDIKFH 242
Cdd:cd09251   1 YRKNEVFLDVVESVNLLMSPQGQVLRADVDGVIVMKTYLSGMPECKFGLNDKLVLESEGKeksgsKSGKGSVELDDCTFH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  243 QCVRLARFENDRTISFIPPDGSFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEMLVKARSQFKDRSYATSVEIELPVPTD 322
Cdd:cd09251  81 QCVRLSKFDSERSISFIPPDGEFELMRYRVTENINLPFRVIPLVKEVGRTKLEYKVKIKSNFPPKLLATNVVVRIPVPKN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  323 AYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSiAAEEATPERKAPIRVKFEIPKFIVSGIQVRYLKI 402
Cdd:cd09251 161 TAKVTINVSKGKAKYDPEENAIVWKIKKFAGMTESTLSAEVELLS-TTSKKKKWSRPPISMDFEVPMFTASGLRVRYLKV 239
                       250       260
                ....*....|....*....|....
gi 4874275  403 IEKSGYQAHPWVRYITMAGEYELR 426
Cdd:cd09251 240 FEKSNYKTVKWVRYITRAGSYEIR 263
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
6-145 3.46e-82

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341439  Cd Length: 139  Bit Score: 248.62  E-value: 3.46e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    6 SALFLLDIKGRVLVWRDYRGDVTAAQAERFFTKLIETEGDSqSNDPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLLF 85
Cdd:cd14835   1 SAIFILDLKGKVLISRNYRGDVPMSVIEKFMPLLMEKEEEG-NLTPILTDGGVTYIYIKHNNLYLLAVTKKNANAAMVLS 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275   86 FLHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEFIKTDAYRM 145
Cdd:cd14835  80 FLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMMDFGYPQTTESKILQEYITQESHKL 139
AP_MHD_Cterm cd07954
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
172-426 1.85e-80

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271157  Cd Length: 245  Bit Score: 248.47  E-value: 1.85e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  172 EVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILleaqgraikgkAIDLEDIKFHQCVRLARFE 251
Cdd:cd07954   1 EVFLDVVEKVNLLISKDGSLLNSEVQGEIALKSFLSGMPEIRLGLNNPDV-----------GIKLDDVSFHPCVRLKRFE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  252 NDRTISFIPPDGSFDLMTYRLSTQ-VKPLIWVEAHIERHSrSRVEMLVKARSQFKDRSYATSVEIELPVPTDAYNPDVRT 330
Cdd:cd07954  70 SERVISFIPPDGEFELMSYRTVEPwSILPITIFPVVSEEG-SQLEVVITLKLSESLQLTAENVEVHIPLPSGVTSLKSKP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  331 SLGSAAYAPEKDALVWKI-QYFYGNKEHTLKADFHLPSIAAEEatPERKAPIRVKFEIPKFIVSGIQVRYLKIIEKS--G 407
Cdd:cd07954 149 SDGQAKFDPEKNALVWRIkRIPVGGKEQSLSAHVELGSLAHEC--PEEAPPVSVSFEIPETTGSGIQVRSLQVFDEKnpG 226
                       250
                ....*....|....*....
gi 4874275  408 YQAHPWVRYITMAGEYELR 426
Cdd:cd07954 227 HDPIKWVRYITHTGKYVAR 245
AP-4_Mu4_Cterm cd09253
C-terminal domain of medium Mu4 subunit in adaptor protein (AP) complex AP-4; AP complexes ...
169-427 3.32e-79

C-terminal domain of medium Mu4 subunit in adaptor protein (AP) complex AP-4; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 4 (AP-4) medium mu4 subunit. AP-4 plays a role in signal-mediated trafficking of integral membrane proteins in mammalian cells. Unlike other AP complexes, AP-4 is found only in mammals and plants. It is believed to be part of a nonclathrin coat, since it might function independently of clathrin, a scaffolding protein participating in the formation of coated vesicles. Recruitment of AP-4 to the trans-Golgi network (TGN) membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1) or a related protein. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. One of the most important sorting signals binding to mu subunits of AP complexes are tyrosine-based endocytotic signals, which are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. However, AP-4 does not bind most canonical tyrosine-based signals except for two naturally occurring ones from the lysosomal membrane proteins CD63 and LAMP-2a. It binds YX [FYL][FL]E motif, where X can be any residue, from the cytosolic tails of amyloid precursor protein (APP) family members in a distinct way.


Pssm-ID: 271161  Cd Length: 271  Bit Score: 245.94  E-value: 3.32e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  169 KKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILLEAQGRAIKGKAIDLEDIKFHQCVRLA 248
Cdd:cd09253   9 KRNEIFVDVLERLSVVFNANGQVLNSEIDGSIQMKSYLPGNPELRLALNEDLVIGKRENRAYYSAVVLDDCNFHESVDLE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  249 RFENDRTISFIPPDGSFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEMLVKARSQFKDRSYATSVEIELPVPTDAYNPDV 328
Cdd:cd09253  89 EFESDRTLSLTPPDGEFTLMNYRISGEFKPPFRVFPSVEETSPYKLELVLKLRADFPPKSTATNVVVRIPLPKGTTSVSC 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  329 RTSLG----SAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSiAAEEATPERKAPIRVKFEIPKFIVSGIQVRYLKIIE 404
Cdd:cd09253 169 ELGSGasgqSAEYKEKEKLVLWNIKKFPGGTELTLRAKITLSS-PVSSSVRKEIGPISLSFEIPMYNVSGLQVRYLRILE 247
                       250       260
                ....*....|....*....|....
gi 4874275  405 K-SGYQAHPWVRYITMAGEYELRL 427
Cdd:cd09253 248 RsSSYNPHRWVRYVTQSSSYVCRI 271
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
159-426 1.69e-54

C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271160  Cd Length: 251  Bit Score: 181.63  E-value: 1.69e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  159 VSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDrilleaqgraikgkAIDLED 238
Cdd:cd09252   1 VPWRRAGVKYTNNEIYFDVVEEIDAIVDKSGKPVSGEVRGEIDCNSRLSGMPDLLLSFNN--------------PRLLDD 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  239 IKFHQCVRLARFENDRTISFIPPDGSFDLMTYR--LSTQVKPLIWVEAHIE-RHSRSRVEMLVKARSqfkdrSYATSVE- 314
Cdd:cd09252  67 PSFHPCVRYSRWESERVLSFIPPDGKFTLMSYRvdLNSLVSLPVYVKPQISfSGSSGRFEITVGSRQ-----NLGKSIEn 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  315 --IELPVPTDAYNPDVRTSLGSAAYAPEKDALVWKIQyFYGNKEH-TLKADFhlpSIAAEEATPERKAPIRVKFEIPKFI 391
Cdd:cd09252 142 vvVEIPLPKGVKSLRLTASHGSFSFDSSTKTLVWNIG-KLTPGKTpTLRGSV---SLSSGLEAPSESPSISVQFKIPGYT 217
                       250       260       270
                ....*....|....*....|....*....|....*
gi 4874275  392 VSGIQVRYLKIIEkSGYQAHPWVRYITMAGEYELR 426
Cdd:cd09252 218 PSGLKVDSLDIYN-EKYKPFKGVKYITKAGKYQVR 251
AP2_Mu_N cd14836
AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ...
6-145 3.85e-42

AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341440  Cd Length: 140  Bit Score: 145.36  E-value: 3.85e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    6 SALFLLDIKGRVLVWRDYRGDVTAAQAERFFTKLIETEGDSQSndPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLLF 85
Cdd:cd14836   3 SALFIYNLKGDVLISRTYRDDVKRSVADAFRVQVINAKEQVRS--PVLTIGSTSFFHVRHGNLYLVAVTRSNVNAAMVFE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275   86 FLHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEFIKTDAYRM 145
Cdd:cd14836  81 FLYKLVQLFKSYFGKFNEDSIKNNFVLIYELLDEILDFGYPQNTEPEALKTYITQEGVKS 140
AP_Mu_N cd14828
AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the ...
6-139 1.05e-40

AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341432  Cd Length: 136  Bit Score: 141.57  E-value: 1.05e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    6 SALFLLDIKGRVLVWRDYRGDVTA-AQAERFFTKLIETEGDSQSndPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLL 84
Cdd:cd14828   1 SCLYILDENLEPLISRNYRADINLqSVVQDFFKAYKKLNPEERP--PIISSNGWNFIYIKRDDLYFVSVTQTNVNLMSVL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4874275   85 FFLHRVVDVFKHYF--EELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEFIK 139
Cdd:cd14828  79 VFLDQFYDLLKDYFgvKKLDKNSIIDNFVLIYELIDESIDFGIIQLTDYNILKDYIK 135
AP-3_Mu3A_Cterm cd09260
C-terminal domain of medium Mu3A subunit in ubiquitously expressed adaptor protein (AP) ...
159-426 6.01e-37

C-terminal domain of medium Mu3A subunit in ubiquitously expressed adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3A subunit encoded by ap3m1gene. Mu3A is ubiquitously expressed in all mammalian tissues and cells. It appears to be localized to the trans-Golgi network (TGN) and/or endosomes and participates in trafficking to the vacuole/lysosome in yeast, flies, and mammals. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of ubiquitous AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3A subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 211371  Cd Length: 254  Bit Score: 135.62  E-value: 6.01e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  159 VSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLG-LNDRILleaqgraikgkaidlE 237
Cdd:cd09260   1 IPWRRAGVKYTNNEAYFDVVEEIDAIIDKSGSTVFAEIQGVIDACIKLSGMPDLSLSfMNPRLL---------------D 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  238 DIKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLSTQ--VKPLIWVEAHI---ERHSRSRVEMLVKARSQFKDRSYATS 312
Cdd:cd09260  66 DVSFHPCIRFKRWESERVLSFIPPDGNFRLISYRVSSQnlVAIPVYVKHNIsfkENSSCGRFDITIGPKQNMGKTIEGIT 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  313 VEIELpvPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFHLPSIAAEeatPERKAPIRVKFEIPKFIV 392
Cdd:cd09260 146 VTVHM--PKVVLNMNLTPTQGSYTFDPVTKVLAWDVGKITPQKLPSLKGLVNLQSGAPK---PEENPSLNIQFKIQQLAI 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 4874275  393 SGIQVRYLKIIEKSgYQAHPWVRYITMAGEYELR 426
Cdd:cd09260 221 SGLKVNRLDMYGEK-YKPFKGVKYITKAGKFQVR 253
AP4_Mu_N cd14838
AP-4 complex subunit mu N-terminal domain; AP-4 complex mu subunit is part of the ...
6-142 9.34e-36

AP-4 complex subunit mu N-terminal domain; AP-4 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341442  Cd Length: 137  Bit Score: 128.43  E-value: 9.34e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    6 SALFLLDIKGRVLVWRDYRGDVTAAQAERFFTKLIETEGDSQsndPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLLF 85
Cdd:cd14838   1 SQFFILSPRGDTIIFRDYRGDVPKGSPEIFYRKVKFWKGDAP---PVFNVDGVNYLHVKRNGLYFVATTRFNVSPSYVLE 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4874275   86 FLHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEFIKTDA 142
Cdd:cd14838  78 LLNRIAKLIKDYCGVLNEESIRKNFVLIYELLDEILDFGYPQTTSTEQLKSFVYNEP 134
AP-3_Mu3B_Cterm cd09261
C-terminal domain of medium Mu3B subunit in neuron-specific adaptor protein (AP) complex AP-3; ...
159-426 8.10e-35

C-terminal domain of medium Mu3B subunit in neuron-specific adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3B subunit encoded by ap3m2 gene. Mu3B is specifically expressed in neurons and neuroendocrine cells. Neuron-specific AP-3 appears to be involved in synaptic vesicle biogenesis from endosomes in neurons and plays an important role in synaptic transmission in the central nervous system. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of neuron-specific AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 211372  Cd Length: 254  Bit Score: 129.78  E-value: 8.10e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  159 VSWRSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLG-LNDRILleaqgraikgkaidlE 237
Cdd:cd09261   1 VPWRRTGVKYTNNEAYFDVIEEIDAIIDKSGSTITAEIQGVIDACVKLTGMPDLTLSfMNPRLL---------------D 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  238 DIKFHQCVRLARFENDRTISFIPPDGSFDLMTYRLSTQ--VKPLIWVEAHI---ERHSRSRVEMLVKARSQFKDRSYATS 312
Cdd:cd09261  66 DVSFHPCVRFKRWESERILSFIPPDGNFRLLSYHVSAQnlVAIPVYVKHNIsfrEGSSLGRFEITLGPKQTMGKTVEGVT 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  313 VEIELpvPTDAYNPDVRTSLGSAAYAPEKDALVWKIQYFYGNKEHTLKADFhlpSIAAEEATPERKAPIRVKFEIPKFIV 392
Cdd:cd09261 146 VTSQM--PKGVLNMSLTPSQGTYTFDPVTKLLSWDVGKINPQKLPSLKGSM---SLQAGASKPDENPTINLQFKIQQLAI 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 4874275  393 SGIQVRYLKIIEKSgYQAHPWVRYITMAGEYELR 426
Cdd:cd09261 221 SGLKVNRLDMYGEK-YKPFKGIKYMTKAGKFQVR 253
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
7-139 9.44e-31

AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341441  Cd Length: 139  Bit Score: 114.92  E-value: 9.44e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    7 ALFLLDIKGRVLVWRDYRGDVTAAQAERFFTKLiETEGDSQSNDPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLLFF 86
Cdd:cd14837   2 SLFILNKSGEVILEKHWRGRIPRSVLDPFNEAL-TKPSRPEDVPPVIYTPPYYLFHILRNNLYFLAVVTSEVPPLLVIEF 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4874275   87 LHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEFIK 139
Cdd:cd14837  81 LHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNGFPLTTEPNALKELVP 133
AP-like_stonins_MHD cd09255
Mu homology domain (MHD) of adaptor-like proteins (AP-like), stonins; A small family of ...
162-416 8.21e-28

Mu homology domain (MHD) of adaptor-like proteins (AP-like), stonins; A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonins, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonins is unable to recognize tyrosine-based endocytic sorting signals. To data, little is known about the localization and function of stonin 1. Stonin 2, also known as stoned B, acts as an AP-2-dependent synaptotagmin-specific sorting adaptors for SV endocytosis. Stoned A is not a stonin. It is structurally unrelated to the adaptins and does not appear to have mammalian homologs. It is not included in this family.


Pssm-ID: 271163 [Multi-domain]  Cd Length: 315  Bit Score: 112.12  E-value: 8.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  162 RSEGLKFKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDrilLEAQGRAIKG---------- 231
Cdd:cd09255   2 RDRGITYREDEITVDVTDEFHGKVTKTGEIKKLGVTVQIHILSFVTGDPECVLGLND---LEVEGREVVRrqdimpsstd 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  232 KAIDLEDIKFHQCVRLARFENDRTISFIPPDG-SFDLMTYR-------LSTQVKPLIWV-EAHIERHSRSRVEMLVKARS 302
Cdd:cd09255  79 QWIKLHNCEFHSCVDVEEFEQSRSIKFHPLDAcRFELMRFRtrynkknLPLTLKSVVSVkGAHVELRADVRMSGYHSRNP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  303 QFKdrsYA-TSVEIELPVPtDAYNPDVRT---------------------------------SLGSAAYAPEKDALVWKI 348
Cdd:cd09255 159 LAQ---VPcENIMIRFPVP-ESWVPAFRTekrfrekslkskknkkasggstaeslsepvievSVGSAKYEHAYRAVVWRI 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4874275  349 QYFYG-----NKEHTLKADFHLPSiaaEEATPERKAP-IRVKFEIPKFIVSGIQVRYLKIIEKSgyQAHPWVRY 416
Cdd:cd09255 235 DRLPDknsaaDTPHTFSCRLDLAS---DLEIPSSTYPhAEVEFTMPSTTASKTTVRSISVSNKN--IPEKWVRY 303
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
6-137 1.61e-26

Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341427  Cd Length: 131  Bit Score: 103.37  E-value: 1.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275    6 SALFLLDIKGRVLVWRDYRGDVTAAQAERFFTKLIETE-GDSQSndPVAYDNGVTYMFVQHSNIYLMIASRQNCNAASLL 84
Cdd:cd14823   1 KAILVLDNDGKRLFAKYYDDTYPSVKEQKAFEKNIFNKkHRTDS--EIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4874275   85 FFLHRVVDVFKHYFEELEEESLRDNFVVVYELLDEMMDFGYPQFTEARILSEF 137
Cdd:cd14823  79 EVLNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVHF 131
AP_stonin-2_MHD cd09263
Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-2; A small family of ...
165-416 3.50e-17

Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-2; A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are the only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonin 2, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonin-2 is unable to recognize tyrosine-based endocytic sorting signals. It acts as an AP-2-dependent synaptotagmin-specific sorting adaptor for SV endocytosis.


Pssm-ID: 271169  Cd Length: 318  Bit Score: 81.99  E-value: 3.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  165 GLKFKKNEVFLDVIESVN-ILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDrilLEAQGRAI----------KGKA 233
Cdd:cd09263   5 GLNYTEEEITVDVRDEFYgILSKGDSRILQHLVLTRINMLSFLSGLAECRLGLND---ILIKGNEIvsrqdimpttTTKW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  234 IDLEDIKFHQCVRLARFENDRTISFIPPDG-SFDLMTYRLSTQVKPLIWVEAHIERHSRSRVEM---LVKARSQFKDRSY 309
Cdd:cd09263  82 IKLRDCRFHECVDEDEFNNSRAILFNPLDAcRFELMRFRTVFAEKTLPFTLRTAASVNGAEVEVqswLVMSTGFSSNRDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  310 AT-----SVEIELPVP--------------------------------TDAYNPDVRTSLGSAAYAPEKDALVWKIQYFY 352
Cdd:cd09263 162 LTqvpceNVMIRYPVPeewvknfrresvlgekslkakvnkgasfgstsTSGSEPVMRVTLGTAKYEHAFNSIVWRINRLP 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4874275  353 GNKE-----HTLKADFHLPSiaAEEATPERKAPIRVKFEIPKFIVSGIQVRYLKIIEKSGYQAhpWVRY 416
Cdd:cd09263 242 DKNSasghpHCFFCHLELGS--DREVPSTFECHVEVEFDMPTTSASKAAVRSISVEDKTDVRK--WVNY 306
AP_stonin-1_MHD cd09262
Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-1 (also called Stoned ...
168-416 6.00e-16

Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-1 (also called Stoned B-like factor); A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are the only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonin 1, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonin-1 is unable to recognize tyrosine-based endocytic sorting signals. To data, little is known about the localization and function of stonin-1.


Pssm-ID: 271168  Cd Length: 314  Bit Score: 78.06  E-value: 6.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  168 FKKNEVFLDVIESVNILVNSNGQIVRSDVVGALKMRTYLSGMPECKLGLNDRILL---EAQGRAIKGKA-IDLEDIKFHQ 243
Cdd:cd09262   8 YEEQELSLEIVDNFWGKVTKEGKVVESAVITQIYCLCFVNGPGECFLTLNDLELLkrdESYGEKEAGKKwIEILDCHFHK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  244 CVRLARFENDRTISFIPPDG-SFDLMTYR-------LSTQVKPLIWVE-AHIERHSRSRVEMLVKARSQFKDRSYATSVE 314
Cdd:cd09262  88 CVNEQEFEQSRIIKFSPLDAcRAELMRFKtayngtqLPFSVKATVVVQgAYVELQAFLNMASTALSFGVSDSHPLCENVV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  315 IELPVPTD--------------------------------AYNPDVRTSLGSAAYAPEKDALVWKIQYFYG-----NKEH 357
Cdd:cd09262 168 IRFPVPAQwikalwtmnlqrqkslkakmnrraclgalretESRPVIQVSVGTAKYESAYSAVVWKIDRLPDknsslDHPH 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4874275  358 TLKADFHLPSiaaEEATPERKAP-IRVKFEIPKFIVSGIQVRYLKIIEKSGYQAH--PWVRY 416
Cdd:cd09262 248 SLSYKLELGS---DQEIPSDWYPfATVQFEVMDTCASQTEVKSLGTESDMQPQKHvtQWARY 306
AP_MuD_MHD cd09256
Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, ...
195-397 3.84e-11

Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, MuD (also known as MUDENG); This family corresponds to the MHD found in a protein encoded by MuD (also known as Adapter-related protein complex 5 subunit mu-1), which is distantly related to the C-terminal domain of the mu2 subunit of AP complexes that participates in clathrin-mediated endocytosis. MuD is evolutionary conserved from mammals to amphibians. It is able to induce cell death by itself and plays an important role in cell death in various tissues.


Pssm-ID: 271164  Cd Length: 276  Bit Score: 63.17  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  195 DVVGALKMRTYLSGMPECKLGLndrILLEAQgraikgkaiDLEDIKFHQCVR------LARFENdRTISFIPPDGSFDLM 268
Cdd:cd09256  37 SVFGEVRCKAELEGLPEVTVSL---SVPANS---------PLQAIIVHPCVQspesgmLAFSGP-YKIRFSPPLGNFVLC 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4874275  269 TYRLSTQVKPLI---WVEAHIERHsrsrVEMLVKARSQFKDRSYATSVEIELPVPTDAY--NPDVRTSLGSAAYAPEKDA 343
Cdd:cd09256 104 RYQSQSVPVPPIlgfYQMKGDEKH----VKFLIQLKLHESVKNSFEYCEVHIPFPNRGLikHVSATPSNGQLEVSKEKRR 179
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4874275  344 LVWKI-QYFYGNKEHTLKADFHLPSIAAEEATPE------RKAPIRVKFEIPKFIVSGIQV 397
Cdd:cd09256 180 LVWNIgQKFPKSLEATLSGTVNFGSESNRRADPEdpfcvgLNAYVKLFFKISDYTLSGCSI 240
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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