SC31A_DANRE
ID SC31A_DANRE Reviewed; 1254 AA.
AC Q7SYD5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein transport protein Sec31A;
DE AltName: Full=SEC31-like protein 1;
DE AltName: Full=SEC31-related protein A;
GN Name=sec31a; Synonyms=sec31l1, sec31p;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:O94979, ECO:0000250|UniProtKB:Q9Z2Q1}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:O94979, ECO:0000250|UniProtKB:Q9Z2Q1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z2Q1}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q9Z2Q1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Z2Q1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Z2Q1}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z2Q1}; Peripheral membrane protein
CC {ECO:0000250}. Note=Associates with membranes in a GTP-dependent
CC manner. Localizes to endoplasmic reticulum exit sites (ERES), also
CC known as transitional endoplasmic reticulum (tER).
CC {ECO:0000250|UniProtKB:Q3UPL0, ECO:0000250|UniProtKB:Q9Z2Q1}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; BC054909; AAH54909.1; -; mRNA.
DR AlphaFoldDB; Q7SYD5; -.
DR SMR; Q7SYD5; -.
DR STRING; 7955.ENSDARP00000104171; -.
DR PaxDb; Q7SYD5; -.
DR ZFIN; ZDB-GENE-020919-2; sec31a.
DR eggNOG; KOG0307; Eukaryota.
DR InParanoid; Q7SYD5; -.
DR PhylomeDB; Q7SYD5; -.
DR Reactome; R-DRE-204005; COPII-mediated vesicle transport.
DR Reactome; R-DRE-2132295; MHC class II antigen presentation.
DR Reactome; R-DRE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q7SYD5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0055123; P:digestive system development; IMP:ZFIN.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:ZFIN.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IMP:ZFIN.
DR Gene3D; 2.130.10.10; -; 1.
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 SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport;
KW WD repeat.
FT CHAIN 1..1254
FT /note="Protein transport protein Sec31A"
FT /id="PRO_0000295152"
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..341
FT /note="WD 7"
FT REPEAT 397..428
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 364..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1254 AA; 135709 MW; A659CA335136E727 CRC64;
MKLKEINRTA IQAWSPAQQH PIYLAAGTSA QQLDATFSTN ASLEIFELDL ADSALAMKSC
GSFSSPHRYH KLVWGPHGIE NQGLPSGVLI AGGENGNIIL YDASKIIAGD SEVIISQSEK
HTGAVRALDV NSFQSNLVAS GGNESEIYIW DLNNFSSPMT PGPKTQPQED ISCVAWNKQV
QHILASASPS GKASVWDLRK NDLIIKVSDH SNRMHCSGLA WNPEVATQLV LASEDDRMPV
IQMWDLRFAT SPLKVLENHT RGILAIAWSV ADPELLLSCG KDNRILCWNP NTAEVLYELP
TSTQWCFDIQ WCPRNPAVLS AAAFDGHISI YSIMGGSNDN ANNLQADQLS SSFGNVDPFG
TGKTLPPLQL PQQTSPQSTI TPLKKPPKWI RRPVGASFAF GGKLVTLDNI KPTAQQPQQT
AAHVVHISQV VTETDFIHRS NQLQTTLNAG NFLEYCQNKI ETVQNEFERT VWSFLKVNFE
EDARLKYLEL LGYEKEELAL KIASALEGNC KPKEADMDKE EVLAEEEAES DLDDIPVNEE
EPVVEETSNT EVPPAPASDA INLKVSQDID GLITQALLTG DYEAAVNLCL HDNRMADGII
LAIAGGPELL AKTQRKYFSK TESKISKLIS AVVMKDWLDI LETCDLQNWK EALAAVMTYA
KPEEFSALCG LLGSRLESSE DVELQAQACL CYICAGTVEQ LVSFWTKTQD SCSPLSLQEL
VEKVVVLQRA VEKAQGAVPA DMGALLAEKM NQYASLLASQ GSLQTAISYL PTNTEQVSVQ
QLRERLSRAL GQHQHLQQPA AAVTGIQKMH QRRPAAVPMQ TYTQPQPPQV PAQPAAPAVP
PQYYQQGRSA TTVTSWSNQT PTALPSVPRQ LVPSSDPQGD STPPAFGLQS PAMASVPAST
PFMYSQQYQN YPPVQQFTPS AGTPGIYQPL PYASSAGAPL PPPPSSSSSA AVYPPQFMLS
ASSQASAPPQ SFCPPPAVSS GGCFQHGGPG SPTSYLPPPG ARAPGTQHEP ALIPASQRTD
GFYQETAWGL EGPQNGWNDP PALSRAAKKK KVPQHFTPPA PITAPIMAPL GDPQAPAGMQ
TLQPQQQVPD QSAGPATFTP IQQQPLGPRN PSMPQGNMEG APGAPIGDVI KPLQAIPTEK
ITKKPIPEEH MVLKTTFEGL IQKCLTAASD PQTKRKLDDA HKRLELLYDK LREQTLSPAI
IGGLHNMAQS IECRSYADGL NIHTHIVSNS NFSETSAFMP VLKVVLTQAN KLGV
