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Conserved domains on  [gi|966981989|ref|XP_014968192|]
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ancient ubiquitous protein 1 isoform X2 [Macaca mulatta]

Protein Classification

lipid droplet-regulating VLDL assembly factor AUP1( domain architecture ID 10353897)

lipid droplet-regulating VLDL assembly factor AUP1 (ancient ubiquitous protein 1) plays a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome

CATH:  1.10.8.10
Gene Symbol:  AUP1
Gene Ontology:  GO:0043130|GO:0016020
SCOP:  4003786

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CUE_AUP1 cd14420
CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a ...
352-396 4.71e-22

CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. It also binds to the membrane-proximal KVGFFKR motif of the cytoplasmic tail of the integrin alphaCTs that plays a crucial role in the inside-out signaling of alpha(IIb)beta(3). AUP1 is found in both the ER and in lipid droplets. It contains two conserved cytoplasmic domains, an acyltransferase domain, a CUE domain and an E2 ubiquitin conjugase G2 (Ube2g2)-binding domain (G2BR). The acyltransferase domain transfers fatty acids onto phospholipids and CUE domain participates in ubiquitin binding or in recruitment of ubiquitin-conjugating enzymes to the site of dislocation.


:

Pssm-ID: 270603  Cd Length: 45  Bit Score: 88.43  E-value: 4.71e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 966981989 352 QLATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEGAVAF 396
Cdd:cd14420    1 RLARMAQQVKEVLPHVPLHVIRRDLEKTRNVDTTITNILEGRVKF 45
LPLAT super family cl17185
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
122-320 5.09e-16

Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).


The actual alignment was detected with superfamily member cd07991:

Pssm-ID: 473073 [Multi-domain]  Cd Length: 211  Bit Score: 76.49  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966981989 122 VRTMCAVLGL-VARQEDSGLRDHSVRVLISNHVTPFDHNIVnllttcstpLLNSPPSFVC-WSRGFM------------- 186
Cdd:cd07991    1 ARVLLFAFGFyVIKVHGKPDPPEAPRIIVANHTSFIDPLIL---------FSDLFPSIVAkKELGKLpfigtilralgci 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966981989 187 -----EMDGRGELVESLKRFCASTRLPPTPLLLfpeEEATNGREGLLRFSSWPFSIQDVVQPLTLQVQRPLV--SVTVSD 259
Cdd:cd07991   72 fvdrsEPKDRKKVVEEIKERATDPNWPPILIFP---EGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVdaFWNSSG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966981989 260 ASWVSELLWSLFVPFTVYQVRWLRPVHR-QLGEANEEFALRVQQLVAKELGQTGTRLTPADK 320
Cdd:cd07991  149 YSSLMYLFRLLTQPANVLEVEFLPVYTPsEEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
 
Name Accession Description Interval E-value
CUE_AUP1 cd14420
CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a ...
352-396 4.71e-22

CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. It also binds to the membrane-proximal KVGFFKR motif of the cytoplasmic tail of the integrin alphaCTs that plays a crucial role in the inside-out signaling of alpha(IIb)beta(3). AUP1 is found in both the ER and in lipid droplets. It contains two conserved cytoplasmic domains, an acyltransferase domain, a CUE domain and an E2 ubiquitin conjugase G2 (Ube2g2)-binding domain (G2BR). The acyltransferase domain transfers fatty acids onto phospholipids and CUE domain participates in ubiquitin binding or in recruitment of ubiquitin-conjugating enzymes to the site of dislocation.


Pssm-ID: 270603  Cd Length: 45  Bit Score: 88.43  E-value: 4.71e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 966981989 352 QLATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEGAVAF 396
Cdd:cd14420    1 RLARMAQQVKEVLPHVPLHVIRRDLEKTRNVDTTITNILEGRVKF 45
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
122-320 5.09e-16

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 76.49  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966981989 122 VRTMCAVLGL-VARQEDSGLRDHSVRVLISNHVTPFDHNIVnllttcstpLLNSPPSFVC-WSRGFM------------- 186
Cdd:cd07991    1 ARVLLFAFGFyVIKVHGKPDPPEAPRIIVANHTSFIDPLIL---------FSDLFPSIVAkKELGKLpfigtilralgci 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966981989 187 -----EMDGRGELVESLKRFCASTRLPPTPLLLfpeEEATNGREGLLRFSSWPFSIQDVVQPLTLQVQRPLV--SVTVSD 259
Cdd:cd07991   72 fvdrsEPKDRKKVVEEIKERATDPNWPPILIFP---EGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVdaFWNSSG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966981989 260 ASWVSELLWSLFVPFTVYQVRWLRPVHR-QLGEANEEFALRVQQLVAKELGQTGTRLTPADK 320
Cdd:cd07991  149 YSSLMYLFRLLTQPANVLEVEFLPVYTPsEEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
CUE smart00546
Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also ...
352-392 1.57e-07

Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2. Ponting (Biochem. J.) "Proteins of the Endoplasmic reticulum" (in press)


Pssm-ID: 214715  Cd Length: 43  Bit Score: 47.49  E-value: 1.57e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 966981989   352 QLATLAQRVKEVLPHVPLGVIQRDL-AKTGCVDLTITNLLEG 392
Cdd:smart00546   1 ENDEALHDLKEMFPNLDEEVIEAVLeANTGNVEATINNLLEG 42
CUE pfam02845
CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE ...
358-392 9.78e-07

CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE domains are related to pfam00627 and this has been confirmed by the structure of the domain. CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2.


Pssm-ID: 427018  Cd Length: 42  Bit Score: 45.16  E-value: 9.78e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 966981989  358 QRVKEVLPHVPLGVIQRDL-AKTGCVDLTITNLLEG 392
Cdd:pfam02845   6 ETLKEMFPDLDEEVIRAVLeASNGNVEAAINALLEG 41
PLN02588 PLN02588
glycerol-3-phosphate acyltransferase
219-320 1.35e-03

glycerol-3-phosphate acyltransferase


Pssm-ID: 215320 [Multi-domain]  Cd Length: 525  Bit Score: 41.12  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966981989 219 EATNGREG-LLRFSSWPFSIQDVVQPLTLQVQRPLVSVTVSDASWVSELLWSLFVPFTVYQVRWLRPVHRQL-------- 289
Cdd:PLN02588 400 EGTTCREPyLLRFSPLFSEVCDVIVPVAIDSHVTFFYGTTASGLKAFDPIFFLLNPFPSYTVQLLDPVSGSSsstcqdpd 479
                         90       100       110
                 ....*....|....*....|....*....|..
gi 966981989 290 -GEANEEFALRVQQLVAKELGQTGTRLTPADK 320
Cdd:PLN02588 480 nGKLKFEVANHVQHEIGNALGFECTNLTRRDK 511
 
Name Accession Description Interval E-value
CUE_AUP1 cd14420
CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a ...
352-396 4.71e-22

CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. It also binds to the membrane-proximal KVGFFKR motif of the cytoplasmic tail of the integrin alphaCTs that plays a crucial role in the inside-out signaling of alpha(IIb)beta(3). AUP1 is found in both the ER and in lipid droplets. It contains two conserved cytoplasmic domains, an acyltransferase domain, a CUE domain and an E2 ubiquitin conjugase G2 (Ube2g2)-binding domain (G2BR). The acyltransferase domain transfers fatty acids onto phospholipids and CUE domain participates in ubiquitin binding or in recruitment of ubiquitin-conjugating enzymes to the site of dislocation.


Pssm-ID: 270603  Cd Length: 45  Bit Score: 88.43  E-value: 4.71e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 966981989 352 QLATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEGAVAF 396
Cdd:cd14420    1 RLARMAQQVKEVLPHVPLHVIRRDLEKTRNVDTTITNILEGRVKF 45
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
122-320 5.09e-16

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 76.49  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966981989 122 VRTMCAVLGL-VARQEDSGLRDHSVRVLISNHVTPFDHNIVnllttcstpLLNSPPSFVC-WSRGFM------------- 186
Cdd:cd07991    1 ARVLLFAFGFyVIKVHGKPDPPEAPRIIVANHTSFIDPLIL---------FSDLFPSIVAkKELGKLpfigtilralgci 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966981989 187 -----EMDGRGELVESLKRFCASTRLPPTPLLLfpeEEATNGREGLLRFSSWPFSIQDVVQPLTLQVQRPLV--SVTVSD 259
Cdd:cd07991   72 fvdrsEPKDRKKVVEEIKERATDPNWPPILIFP---EGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVdaFWNSSG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966981989 260 ASWVSELLWSLFVPFTVYQVRWLRPVHR-QLGEANEEFALRVQQLVAKELGQTGTRLTPADK 320
Cdd:cd07991  149 YSSLMYLFRLLTQPANVLEVEFLPVYTPsEEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
CUE_AUP1_AMFR_like cd14376
CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor ...
355-390 3.03e-12

CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor (AMFR) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. AMFR is an internalizing cell surface glycoprotein that is localized in both plasma membrane caveolae and the ER, and involves in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. Cue1p is an N-terminally membrane-anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). This family also includes plant E3 ubiquitin protein ligases RIN2, RIN3, and similar proteins. Comparing with other CUE domain-containing proteins, some family members from higher eukaryotes do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains.


Pssm-ID: 270559  Cd Length: 37  Bit Score: 60.57  E-value: 3.03e-12
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 966981989 355 TLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLL 390
Cdd:cd14376    2 EMVEQVQEVFPHIPREAIRRDLQRTNSVDLTINNIL 37
CUE_AMFR cd14421
CUE domain found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR is an ...
355-392 1.78e-08

CUE domain found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR is an internalizing cell surface glycoprotein that is localized in both plasma membrane caveolae and the endoplasmic reticulum (ER), and involves in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. It is also called ER-protein gp78 that has been identified as a RING finger-dependent ubiquitin protein ligase (E3) implicated in degradation from the ER. AMFR contains an N-terminal RING-finger domain and a C-terminal CUE domain.


Pssm-ID: 270604  Cd Length: 41  Bit Score: 50.34  E-value: 1.78e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 966981989 355 TLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEG 392
Cdd:cd14421    2 AMAHQVQEMFPQVPLSVILADLRLTRSVEVTIENILEG 39
CUE smart00546
Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also ...
352-392 1.57e-07

Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2. Ponting (Biochem. J.) "Proteins of the Endoplasmic reticulum" (in press)


Pssm-ID: 214715  Cd Length: 43  Bit Score: 47.49  E-value: 1.57e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 966981989   352 QLATLAQRVKEVLPHVPLGVIQRDL-AKTGCVDLTITNLLEG 392
Cdd:smart00546   1 ENDEALHDLKEMFPNLDEEVIEAVLeANTGNVEATINNLLEG 42
CUE pfam02845
CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE ...
358-392 9.78e-07

CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE domains are related to pfam00627 and this has been confirmed by the structure of the domain. CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2.


Pssm-ID: 427018  Cd Length: 42  Bit Score: 45.16  E-value: 9.78e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 966981989  358 QRVKEVLPHVPLGVIQRDL-AKTGCVDLTITNLLEG 392
Cdd:pfam02845   6 ETLKEMFPDLDEEVIRAVLeASNGNVEAAINALLEG 41
CUE_RIN3_plant cd14422
CUE domain found in plant E3 ubiquitin protein ligases RIN2, RIN3 and similar proteins; RIN2 ...
353-390 2.32e-06

CUE domain found in plant E3 ubiquitin protein ligases RIN2, RIN3 and similar proteins; RIN2 and RIN3 are two closely related RPM1-interacting proteins conserved in higher eukaryotes. They are orthologs of the mammalian autocrine motility factor receptor (AMFR), a cytokine receptor localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). RIN2 and RIN3 have been identified as membrane-bound RING-finger type ubiquitin ligases with six apparent transmembrane domains, a RING-finger domain and a CUE domain. They act as positive regulators of RPM1- and RPS2-dependent hypersensitive response (HR).


Pssm-ID: 270605  Cd Length: 38  Bit Score: 44.21  E-value: 2.32e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 966981989 353 LATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLL 390
Cdd:cd14422    1 ILAMVGMVREVLPHVPDEIIFQDLQRTNSVTATVNNLL 38
PLN02588 PLN02588
glycerol-3-phosphate acyltransferase
219-320 1.35e-03

glycerol-3-phosphate acyltransferase


Pssm-ID: 215320 [Multi-domain]  Cd Length: 525  Bit Score: 41.12  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966981989 219 EATNGREG-LLRFSSWPFSIQDVVQPLTLQVQRPLVSVTVSDASWVSELLWSLFVPFTVYQVRWLRPVHRQL-------- 289
Cdd:PLN02588 400 EGTTCREPyLLRFSPLFSEVCDVIVPVAIDSHVTFFYGTTASGLKAFDPIFFLLNPFPSYTVQLLDPVSGSSsstcqdpd 479
                         90       100       110
                 ....*....|....*....|....*....|..
gi 966981989 290 -GEANEEFALRVQQLVAKELGQTGTRLTPADK 320
Cdd:PLN02588 480 nGKLKFEVANHVQHEIGNALGFECTNLTRRDK 511
 
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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