SC31A_RAT
ID SC31A_RAT Reviewed; 1249 AA.
AC Q9Z2Q1; Q5RKK4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein transport protein Sec31A;
DE AltName: Full=SEC31-like protein 1;
DE AltName: Full=SEC31-related protein A;
DE AltName: Full=Vesicle-associated protein 1;
GN Name=Sec31a; Synonyms=Sec31l1, Vap1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, TISSUE SPECIFICITY, INTERACTION WITH SEC13, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Liver;
RX PubMed=10574704; DOI=10.1242/jcs.112.24.4547;
RA Shugrue C.A., Kolen E.R., Peters H., Czernik A., Kaiser C., Matovcik L.,
RA Hubbard A.L., Gorelick F.;
RT "Identification of the putative mammalian orthologue of Sec31P, a component
RT of the COPII coat.";
RL J. Cell Sci. 112:4547-4556(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC13.
RX PubMed=10788476; DOI=10.1074/jbc.275.18.13597;
RA Tang B.L., Zhang T., Low D.Y.H., Wong E.T., Horstmann H., Hong W.;
RT "Mammalian homologues of yeast sec31p. An ubiquitously expressed form is
RT localized to endoplasmic reticulum (ER) exit sites and is essential for ER-
RT Golgi transport.";
RL J. Biol. Chem. 275:13597-13604(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526; SER-531 AND SER-1192,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. {ECO:0000269|PubMed:10788476}.
CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2
CC tetramer that forms the edge element of the COPII outer coat. The
CC tetramer self-assembles in multiple copies to form the complete
CC polyhedral cage. Interacts (via WD 8) with SEC13 (PubMed:10574704,
CC PubMed:10788476). Interacts with PDCD6; interaction takes place in
CC response to cytosolic calcium increase and leads to bridge together the
CC BCR(KLHL12) complex and SEC31A, leading to monoubiquitination.
CC Interacts with KLHL12 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O94979, ECO:0000269|PubMed:10574704,
CC ECO:0000269|PubMed:10788476}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10574704}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000269|PubMed:10574704}; Peripheral membrane protein; Cytoplasmic
CC side. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10574704};
CC Peripheral membrane protein. Note=Associates with membranes in a GTP-
CC dependent manner (PubMed:10574704). Localizes to endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER) (By similarity). {ECO:0000250|UniProtKB:Q3UPL0,
CC ECO:0000269|PubMed:10574704}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z2Q1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2Q1-2; Sequence=VSP_026754, VSP_026755, VSP_026756;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10574704}.
CC -!- DOMAIN: The ALG-2-binding site motif-2 (ABS-2) contains a PXPGF
CC sequence that binds hydrophobic pocket 3 of PDCD6.
CC {ECO:0000250|UniProtKB:O94979}.
CC -!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex,
CC leading to regulate the size of COPII coats.
CC {ECO:0000250|UniProtKB:O94979}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; AF034582; AAD01990.1; -; mRNA.
DR EMBL; BC085722; AAH85722.1; -; mRNA.
DR PIR; T14150; T14150.
DR RefSeq; NP_148981.1; NM_033021.1.
DR RefSeq; XP_006250751.1; XM_006250689.3. [Q9Z2Q1-2]
DR RefSeq; XP_006250752.1; XM_006250690.2. [Q9Z2Q1-2]
DR AlphaFoldDB; Q9Z2Q1; -.
DR SMR; Q9Z2Q1; -.
DR BioGRID; 250159; 4.
DR IntAct; Q9Z2Q1; 2.
DR STRING; 10116.ENSRNOP00000003072; -.
DR iPTMnet; Q9Z2Q1; -.
DR PhosphoSitePlus; Q9Z2Q1; -.
DR jPOST; Q9Z2Q1; -.
DR PaxDb; Q9Z2Q1; -.
DR PRIDE; Q9Z2Q1; -.
DR GeneID; 93646; -.
DR KEGG; rno:93646; -.
DR CTD; 22872; -.
DR RGD; 620233; Sec31a.
DR VEuPathDB; HostDB:ENSRNOG00000002251; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_1_0_1; -.
DR InParanoid; Q9Z2Q1; -.
DR OrthoDB; 100998at2759; -.
DR PhylomeDB; Q9Z2Q1; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q9Z2Q1; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002251; Expressed in jejunum and 19 other tissues.
DR ExpressionAtlas; Q9Z2Q1; baseline and differential.
DR Genevisible; Q9Z2Q1; RN.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0030120; C:vesicle coat; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:RGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 1.
DR Pfam; PF12931; Sec16_C; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Isopeptide bond; Membrane;
KW Methylation; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport; Ubl conjugation; WD repeat.
FT CHAIN 1..1249
FT /note="Protein transport protein Sec31A"
FT /id="PRO_0000295150"
FT REPEAT 4..47
FT /note="WD 1"
FT REPEAT 64..111
FT /note="WD 2"
FT REPEAT 120..160
FT /note="WD 3"
FT REPEAT 166..206
FT /note="WD 4"
FT REPEAT 209..254
FT /note="WD 5"
FT REPEAT 258..298
FT /note="WD 6"
FT REPEAT 301..342
FT /note="WD 7"
FT REPEAT 397..429
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 161..470
FT /note="Interaction with SEC13"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT REGION 790..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..1142
FT /note="Interaction with PDCD6"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT REGION 842..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 873..879
FT /note="ALG-2-binding site motif-2 (ABS-2),"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT COMPBIAS 885..908
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 423
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3UPL0"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT MOD_RES 1190
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT MOD_RES 1192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT CROSSLNK 1246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT VAR_SEQ 503..541
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026754"
FT VAR_SEQ 834..864
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026755"
FT VAR_SEQ 907..1019
FT /note="PYQPAQQYSLGTGGSAVYRPQQPVAPPASKRYPNAPYVSPVASYSGQPHMYT
FT AQPASSPTSSSAPLPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTPPAASELPASQR
FT TG -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026756"
FT CONFLICT 209
FT /note="D -> N (in Ref. 1; AAD01990)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="R -> W (in Ref. 1; AAD01990)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="Q -> E (in Ref. 1; AAD01990)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="N -> K (in Ref. 1; AAD01990)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="L -> F (in Ref. 1; AAD01990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1249 AA; 135272 MW; 8069E577903231B5 CRC64;
MKLKEIDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC
ATFSSSHRYH KLIWGPHKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQKDK
HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV
QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV
VQMWDLRFAS SPLRVLENHA RGILAIAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP
TNTQWCFDIQ WCPRNPAVLS AASFDGRIRV YSIMGGSIDG LRQKQVDKLS SSFGNLDPFG
TGQPLPPLQI PQQTSQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFENV TGQPQQGAEQ
PRRQPVFISQ VVTEKDFLSR SEQLQHVVQS QGFISYCQKK IDASQTDFEK NVWSFLKVNF
EEDSRGKYLE LLGYRREDLG EKIALALNRV DGSDVALKDS DRVAQSDGEE SPAEEGQLLG
ERIKEEKQEC DFLPSAGGGT FNISVSGDID GLITRALLTG NFESAVDLCL HDNRMADAII
LAIAGGQELL AQTQKKYFAK SQSKITRLIT AVVMKNWKEI VESCDLKNWR EALAAVLTYA
KPDEFSALCD LLGARLESEG DSLLRTQACL CYICAGNVER LVACWTKAQD GSNPLSLQDL
IEKVVILRKA VQLTQALDTN TVGALLAEKM SQYANLLAAQ GSIAAALAFL PDNTNQPDIV
QLRDRLCRAQ GRSVPGQESS RSSYEGQPLP KGGPGPLAGH PQVSRVQSQQ YYPQVRIAPT
VTTWSDRTPT ALPSHPPAAC PSDTQGGNPP PPGFIMHGNV VPNSPAPLPT SPGHMHSQPP
PYPQPQPYQP AQQYSLGTGG SAVYRPQQPV APPASKRYPN APYVSPVASY SGQPHMYTAQ
PASSPTSSSA PLPPPPSSGA SFQHGGPGAP PSSSAYALPP GTTGTPPAAS ELPASQRTGP
QNGWNDPPAL NRVPKKKKLP ENFMPPVPIT SPIMNPGGDP QPQGLQQQPS ASGPRSSHAS
FPQPHLAGGQ PFHGIQQPLA QTGMPPSFSK PNTEGAPGAP IGNTIQHVQA LPTEKITKKP
IPDEHLILKT TFEDLIQRCL SSATDPQTKR KLDDASKRLE CLYDKLRDQT LSPTIISGLH
SIARSIETRN YSEGLTVHTH IVSTSNFSET SAFMPVLKVV LSQASKLGV
