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Conserved domains on  [gi|1622955350|ref|XP_028707320|]
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sorting nexin-6 isoform X1 [Macaca mulatta]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 10246358)

PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to sorting nexins that are involved in regulating membrane traffic and protein sorting in the endosomal system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
161-378 3.00e-140

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153346  Cd Length: 218  Bit Score: 397.87  E-value: 3.00e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 161 DFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICK 240
Cdd:cd07662     1 DFFKNVVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTLGTQDSTDICK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 241 FFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQ 320
Cdd:cd07662    81 FFLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETTQQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622955350 321 LCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLN 378
Cdd:cd07662   161 LCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQSCLAVLN 218
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
42-145 8.44e-61

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


The actual alignment was detected with superfamily member cd07292:

Pssm-ID: 470617  Cd Length: 141  Bit Score: 192.62  E-value: 8.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350  42 AALQVDISDALSERDKVKFTVHTK-------------------------------------IPPAPPRPDFDASREKLQK 84
Cdd:cd07292     1 AALQVDISDALSERDKVKFTVHTKsslpnfkqnefsvvrqheefiwlhdsfvenedyagyiIPPAPPRPDFDASREKLQK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622955350  85 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 145
Cdd:cd07292    81 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 141
 
Name Accession Description Interval E-value
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
161-378 3.00e-140

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153346  Cd Length: 218  Bit Score: 397.87  E-value: 3.00e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 161 DFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICK 240
Cdd:cd07662     1 DFFKNVVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTLGTQDSTDICK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 241 FFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQ 320
Cdd:cd07662    81 FFLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETTQQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622955350 321 LCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLN 378
Cdd:cd07662   161 LCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQSCLAVLN 218
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
42-145 8.44e-61

The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.


Pssm-ID: 132825  Cd Length: 141  Bit Score: 192.62  E-value: 8.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350  42 AALQVDISDALSERDKVKFTVHTK-------------------------------------IPPAPPRPDFDASREKLQK 84
Cdd:cd07292     1 AALQVDISDALSERDKVKFTVHTKsslpnfkqnefsvvrqheefiwlhdsfvenedyagyiIPPAPPRPDFDASREKLQK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622955350  85 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 145
Cdd:cd07292    81 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 141
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
178-364 4.89e-11

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 62.30  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 178 VKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGT-QDSTDICKFFLKVSELFDKTRKIE 256
Cdd:pfam09325  19 FNEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASlELSTGLSRALSQLAEVEERIKELL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 257 ARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAK------------------NKDVLQAETS 318
Cdd:pfam09325  99 ERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQlekllranksqndklqqaKKEVEELERR 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622955350 319 QQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAK 364
Cdd:pfam09325 179 VQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQK 224
BAR smart00721
BAR domain;
269-379 6.11e-04

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 40.83  E-value: 6.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350  269 DLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKD-----VLQAETSQQLCCQKFEKISESAKQELIDFKTR 343
Cdd:smart00721 124 PLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKAKKSKEKkkdekLAKAEEELRKAKQEFEESNAQLVEELPQLVAS 203
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622955350  344 RVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLNG 379
Cdd:smart00721 204 RVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
113-145 6.35e-04

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 38.38  E-value: 6.35e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622955350 113 KKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 145
Cdd:pfam00787  52 EKRRKGLEQYLQRLLQHPELRNSEVLLEFLESD 84
 
Name Accession Description Interval E-value
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
161-378 3.00e-140

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153346  Cd Length: 218  Bit Score: 397.87  E-value: 3.00e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 161 DFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICK 240
Cdd:cd07662     1 DFFKNVVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTLGTQDSTDICK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 241 FFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQ 320
Cdd:cd07662    81 FFLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETTQQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622955350 321 LCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLN 378
Cdd:cd07662   161 LCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQSCLAVLN 218
BAR_SNX5_6 cd07621
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, ...
161-378 1.52e-128

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153305  Cd Length: 219  Bit Score: 368.20  E-value: 1.52e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 161 DFFKNMVKSAD-GVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDIC 239
Cdd:cd07621     1 GFLKSISKSADeELLLSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 240 KFFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQ 319
Cdd:cd07621    81 KFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAKDLLYRRLRCLANYENANKNLEKARAKNKDVHAAEAAQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622955350 320 QLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLN 378
Cdd:cd07621   161 QEACEKFESMSESAKQELLDFKTRRVAAFRKNLVELAELEIKHAKAQIQLLKNCLAALK 219
BAR_SNX5 cd07663
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid ...
162-377 1.73e-101

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153347  Cd Length: 218  Bit Score: 299.16  E-value: 1.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 162 FFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICKF 241
Cdd:cd07663     2 FFKNMVKSADEVLFSGVKEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTVIKKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 242 FLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQL 321
Cdd:cd07663    82 LLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAKDLLYRRARALADYENSNKALDKARLKSKDVKQAEAHQQE 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622955350 322 CCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVL 377
Cdd:cd07663   162 CCQKFEKLSESAKQELISFKRRRVAAFRKNLIEMTELEIKHAKNNVSLLQSCIDLF 217
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
42-145 8.44e-61

The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.


Pssm-ID: 132825  Cd Length: 141  Bit Score: 192.62  E-value: 8.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350  42 AALQVDISDALSERDKVKFTVHTK-------------------------------------IPPAPPRPDFDASREKLQK 84
Cdd:cd07292     1 AALQVDISDALSERDKVKFTVHTKsslpnfkqnefsvvrqheefiwlhdsfvenedyagyiIPPAPPRPDFDASREKLQK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622955350  85 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 145
Cdd:cd07292    81 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 141
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
42-145 5.32e-60

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 190.66  E-value: 5.32e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350  42 AALQVDISDALSERDKVKFTVHTK-------------------------------------IPPAPPRPDFDASREKLQK 84
Cdd:cd07291     1 PSLQIDIPDALSERDKVKFTVHTKttlpsfqspdfsvtrqhedfiwlhdalietedyagliIPPAPPKPDFDGPREKMQK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622955350  85 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 145
Cdd:cd07291    81 LGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEYD 141
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
42-145 1.96e-57

The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Members of this subfamily include SNX5, SNX6, and similar proteins. They contain a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p.


Pssm-ID: 132802  Cd Length: 141  Bit Score: 183.79  E-value: 1.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350  42 AALQVDISDALSERDKVKFTVHTK-------------------------------------IPPAPPRPDFDASREKLQK 84
Cdd:cd06892     1 SSLQVDISDALSERDKVKFTVHTKttlptfqkpefsvtrqheefvwlhdtlvenedyagliIPPAPPKPDFDASREKLQK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622955350  85 LGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 145
Cdd:cd06892    81 LGEGEGSMTKEEFEKMKQELEAEYLAIFKKTVAMHEVFLRRLASHPVLRNDANFRVFLEYE 141
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
180-375 3.34e-35

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 128.63  E-value: 3.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 180 DVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDST---DICKFFLKVSELFDKTRKIE 256
Cdd:cd07596     1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEvggELGEALSKLGKAAEELSSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 257 ARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAK------------------NKDVLQAETS 318
Cdd:cd07596    81 EAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQleklkaapgikpakveelEEELEEAESA 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622955350 319 QQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLA 375
Cdd:cd07596   161 LEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLP 217
BAR_SNX_like cd07630
The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are ...
180-374 8.67e-24

The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of uncharacterized proteins with similarity to sorting nexins (SNXs), which are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153314  Cd Length: 198  Bit Score: 97.58  E-value: 8.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 180 DVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQD---STDICKFFLKVSELFDKTRKIE 256
Cdd:cd07630     1 DVDEFFQKERDMNTKLSANMKEAAEKFLKIVNTEQRLANALGHLSSSLQLCVGLDeasVVALNRLCTKLSEALEEAKENI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 257 ARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDvlQAETSQQLCCQKFEKISESAKQE 336
Cdd:cd07630    81 EVVAGNNENTLGLTLDLYSRYSESEKDMLFRRTCKLIEFENASKALEKAKPQKKE--QAEEAKKKAETEFEEISSLAKKE 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622955350 337 LIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCL 374
Cdd:cd07630   159 LERFHRQRVLELQSALVCYAESQIKNAKEAAAVLTKTL 196
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
178-364 4.89e-11

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 62.30  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 178 VKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGT-QDSTDICKFFLKVSELFDKTRKIE 256
Cdd:pfam09325  19 FNEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASlELSTGLSRALSQLAEVEERIKELL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 257 ARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAK------------------NKDVLQAETS 318
Cdd:pfam09325  99 ERQALQDVLTLGETIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQlekllranksqndklqqaKKEVEELERR 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622955350 319 QQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAK 364
Cdd:pfam09325 179 VQQAEKEFEDISELIKKELERFELERVDDFKNSVEIYLESAIESQK 224
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
246-372 3.09e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX1, SNX2, and similar proteins. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153307  Cd Length: 224  Bit Score: 50.74  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 246 SELFDKTRKIEA--RVSADEDL-KLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKAR-AKNK----------- 310
Cdd:cd07623    73 SQLAEVEEKIEQlhGEQADTDFyILAELLKDYIGLIGAIKDVFHERVKVWQNWQNAQQTLTKKReAKAKlelsgrtdkld 152
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622955350 311 ----DVLQAETSQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKgnlQLLQN 372
Cdd:cd07623   153 qaqqEIKEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQQ---QLIKY 215
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
58-143 9.82e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 44.11  E-value: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350  58 VKFTVHTKIPPAPPRP----------DFDASREKLQKLGEG-------EGSMTkeEFTKMKQELeaeylaIFKKTVAMhE 120
Cdd:cd06859    19 VVYRVTTKTNLPDFKKsefsvlrrysDFLWLYERLVEKYPGrivppppEKQAV--GRFKVKFEF------IEKRRAAL-E 89
                          90       100
                  ....*....|....*....|...
gi 1622955350 121 VFLCRVAAHPILRKDLNFHVFLE 143
Cdd:cd06859    90 RFLRRIAAHPVLRKDPDFRLFLE 112
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
182-352 6.00e-05

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153311 [Multi-domain]  Cd Length: 216  Bit Score: 43.83  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 182 DDFFEHERTFLLEYHNRVKdASAKSDRMTRSHKSA-ADDYNRIGSSLYALGTQD-STDICKFFLKVSELFDKTRKIEARV 259
Cdd:cd07627     3 DEWFIEKKQYLDSLESQLK-QLYKSLELVSSQRKElASATEEFAETLEALSSLElSKSLSDLLAALAEVQKRIKESLERQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 260 SADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAK------------------NKDVLQAETSQQL 321
Cdd:cd07627    82 ALQDVLTLGVTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQleklkrqgktqqeklnslLSELEEAERRASE 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955350 322 CCQKFEKISESAKQELIDFKTRRVAAFRKNL 352
Cdd:cd07627   162 LKKEFEEVSELIKSELERFERERVEDFRNSV 192
BAR smart00721
BAR domain;
269-379 6.11e-04

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 40.83  E-value: 6.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350  269 DLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKD-----VLQAETSQQLCCQKFEKISESAKQELIDFKTR 343
Cdd:smart00721 124 PLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKAKKSKEKkkdekLAKAEEELRKAKQEFEESNAQLVEELPQLVAS 203
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622955350  344 RVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLNG 379
Cdd:smart00721 204 RVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
113-145 6.35e-04

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 38.38  E-value: 6.35e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622955350 113 KKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 145
Cdd:pfam00787  52 EKRRKGLEQYLQRLLQHPELRNSEVLLEFLESD 84
BAR_SNX1 cd07665
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid ...
164-357 1.63e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153349 [Multi-domain]  Cd Length: 234  Bit Score: 39.67  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 164 KNMVKSADGVIVSGVK--DVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGT-QDSTDICK 240
Cdd:cd07665     1 KMFNKATDAVSKMTIKmnESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLGSsEDNTALSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 241 FFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQ 320
Cdd:cd07665    81 ALSQLAEVEEKIEQLHQEQANNDFFLLAELLADYIRLLSAVRGAFDQRMKTWQRWQDAQAMLQKKREAEARLLWANKPDK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622955350 321 LCCQK----------------FEKISESAKQELIDFKTRRVAAFRKNLVELAE 357
Cdd:cd07665   161 LQQAKdeiaewesrvtqyerdFERISATVRKEVIRFEKEKSKDFKNHIIKYLE 213
BAR_SNX2 cd07664
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid ...
168-357 6.86e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153348 [Multi-domain]  Cd Length: 234  Bit Score: 37.72  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 168 KSADGVIVSGVK--DVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALG-TQDSTDICKFFLK 244
Cdd:cd07664     5 KAADAVNKMTIKmnESDAWFEEKQQQFENLDQQLRKLHASVESLVCHRKELSANTAAFAKSAAMLGnSEDHTALSRALSQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 245 VSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKAR--------AKNKDVLQA- 315
Cdd:cd07664    85 LAEVEEKIDQLHQDQAFADFYLFSELLGDYIRLIAAVKGVFDQRMKCWQKWQDAQVTLQKKReaeaklqyANKPDKLQQa 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622955350 316 -------ETSQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAE 357
Cdd:cd07664   165 kdeikewEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLE 213
BAR_Amphiphysin_I_II cd07611
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, ...
271-379 7.41e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature. Human autoantibodies to amphiphysin-1 hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Mutations in amphiphysin-2 (BIN1) are associated with autosomal recessive centronuclear myopathy.


Pssm-ID: 153295  Cd Length: 211  Bit Score: 37.61  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955350 271 LKYYLRESQAAKDLLYRRSRSLVDYENAN---KALDKARAKN-KDVLQAETSQQLCCQKFEKISESAKQELIDFKTRRVA 346
Cdd:cd07611    96 LDTYLGQFPDIKNRIAKRSRKLVDYDSARhhlEALQTSKRKDeGRIAKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVG 175
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622955350 347 AFRKNLVELAELELKHAKGNLQLLQNCLAVLNG 379
Cdd:cd07611   176 FYVNTFKNVSSLEAKFHKEISVLCHKLYEVMTK 208
 
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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