SC31B_HUMAN
ID SC31B_HUMAN Reviewed; 1179 AA.
AC Q9NQW1; B7ZM75; Q6MZS3; Q86UF0; Q9Y4Q8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein transport protein Sec31B;
DE AltName: Full=SEC31-like protein 2;
DE AltName: Full=SEC31-related protein B;
DE AltName: Full=SEC31B-1;
GN Name=SEC31B; Synonyms=SEC31L2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 4),
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP SEC13 AND SEC31A.
RC TISSUE=Testis;
RX PubMed=16495487; DOI=10.1242/jcs.02751;
RA Stankewich M.C., Stabach P.R., Morrow J.S.;
RT "Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that
RT associate with the COPII coat.";
RL J. Cell Sci. 119:958-969(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 265-1179 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND VARIANTS
RP ALA-89; PHE-129 AND ALA-332.
RC TISSUE=Testis;
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 [5]
RP TISSUE SPECIFICITY.
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 [6]
RP UBIQUITINATION.
RX PubMed=22358839; DOI=10.1038/nature10822;
RA Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R.,
RA Rape M.;
RT "Ubiquitin-dependent regulation of COPII coat size and function.";
RL Nature 482:495-500(2012).
CC -!- FUNCTION: As a component of the coat protein complex II (COPII), may
CC function in vesicle budding and cargo export from the endoplasmic
CC reticulum. {ECO:0000269|PubMed:16495487}.
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 Interacts with SEC31A. {ECO:0000250, ECO:0000269|PubMed:16495487}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16495487}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000269|PubMed:16495487}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16495487}; Cytoplasmic side
CC {ECO:0000269|PubMed:16495487}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16495487}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16495487}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=SEC31B-F;
CC IsoId=Q9NQW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQW1-2; Sequence=VSP_026759, VSP_026760, VSP_026761;
CC Name=3;
CC IsoId=Q9NQW1-3; Sequence=VSP_026757, VSP_026758;
CC Name=4; Synonyms=SEC31B-t;
CC IsoId=Q9NQW1-4; Sequence=VSP_026762, VSP_026763;
CC Name=5;
CC IsoId=Q9NQW1-5; Sequence=VSP_026759;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels with specific
CC expression in thymus and testis. Expressed in testis by Sertoli cells,
CC Leydig cells and spermatogonia and in cerebellum more prominently by
CC Purkinje and granular cells (at protein level).
CC {ECO:0000269|PubMed:10788476, ECO:0000269|PubMed:16495487}.
CC -!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex,
CC leading to regulate the size of COPII coats.
CC {ECO:0000269|PubMed:22358839}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; AF274863; AAF78243.1; -; mRNA.
DR EMBL; AL080141; CAB45735.1; -; mRNA.
DR EMBL; BX640914; CAE45955.1; -; mRNA.
DR EMBL; AL133352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034946; AAH34946.1; -; mRNA.
DR EMBL; BC044569; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC144313; AAI44314.1; -; mRNA.
DR CCDS; CCDS7495.1; -. [Q9NQW1-1]
DR PIR; T12526; T12526.
DR RefSeq; NP_056305.1; NM_015490.3. [Q9NQW1-1]
DR AlphaFoldDB; Q9NQW1; -.
DR SMR; Q9NQW1; -.
DR BioGRID; 117447; 19.
DR IntAct; Q9NQW1; 13.
DR MINT; Q9NQW1; -.
DR STRING; 9606.ENSP00000359370; -.
DR iPTMnet; Q9NQW1; -.
DR PhosphoSitePlus; Q9NQW1; -.
DR BioMuta; SEC31B; -.
DR DMDM; 74762753; -.
DR jPOST; Q9NQW1; -.
DR MassIVE; Q9NQW1; -.
DR PaxDb; Q9NQW1; -.
DR PeptideAtlas; Q9NQW1; -.
DR PRIDE; Q9NQW1; -.
DR ProteomicsDB; 82201; -. [Q9NQW1-1]
DR ProteomicsDB; 82202; -. [Q9NQW1-2]
DR ProteomicsDB; 82204; -. [Q9NQW1-4]
DR ProteomicsDB; 82205; -. [Q9NQW1-5]
DR Antibodypedia; 49267; 87 antibodies from 19 providers.
DR DNASU; 25956; -.
DR Ensembl; ENST00000370345.8; ENSP00000359370.3; ENSG00000075826.17. [Q9NQW1-1]
DR Ensembl; ENST00000462434.5; ENSP00000474124.1; ENSG00000075826.17. [Q9NQW1-2]
DR GeneID; 25956; -.
DR KEGG; hsa:25956; -.
DR MANE-Select; ENST00000370345.8; ENSP00000359370.3; NM_015490.4; NP_056305.1.
DR UCSC; uc001krc.2; human. [Q9NQW1-1]
DR CTD; 25956; -.
DR GeneCards; SEC31B; -.
DR HGNC; HGNC:23197; SEC31B.
DR HPA; ENSG00000075826; Low tissue specificity.
DR MIM; 610258; gene.
DR neXtProt; NX_Q9NQW1; -.
DR OpenTargets; ENSG00000075826; -.
DR PharmGKB; PA162402792; -.
DR VEuPathDB; HostDB:ENSG00000075826; -.
DR eggNOG; KOG0307; Eukaryota.
DR GeneTree; ENSGT00390000003175; -.
DR HOGENOM; CLU_003033_1_0_1; -.
DR InParanoid; Q9NQW1; -.
DR OMA; AQWAFGG; -.
DR OrthoDB; 100998at2759; -.
DR PhylomeDB; Q9NQW1; -.
DR TreeFam; TF313842; -.
DR PathwayCommons; Q9NQW1; -.
DR SignaLink; Q9NQW1; -.
DR SIGNOR; Q9NQW1; -.
DR BioGRID-ORCS; 25956; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; SEC31B; human.
DR GenomeRNAi; 25956; -.
DR Pharos; Q9NQW1; Tdark.
DR PRO; PR:Q9NQW1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NQW1; protein.
DR Bgee; ENSG00000075826; Expressed in right hemisphere of cerebellum and 116 other tissues.
DR ExpressionAtlas; Q9NQW1; baseline and differential.
DR Genevisible; Q9NQW1; HS.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030120; C:vesicle coat; IDA:MGI.
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:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 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; Membrane; Protein transport;
KW Reference proteome; Repeat; Transport; Ubl conjugation; WD repeat.
FT CHAIN 1..1179
FT /note="Protein transport protein Sec31B"
FT /id="PRO_0000295153"
FT REPEAT 17..56
FT /note="WD 1"
FT REPEAT 67..110
FT /note="WD 2"
FT REPEAT 119..159
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 391..422
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 812..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 69..85
FT /note="FHKLVWGSFGSGLLESS -> ATSWLQGPAILKSSLGI (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026757"
FT VAR_SEQ 86..1179
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026758"
FT VAR_SEQ 165
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026759"
FT VAR_SEQ 349
FT /note="I -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026760"
FT VAR_SEQ 350..1179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026761"
FT VAR_SEQ 470..482
FT /note="KVTLEQDSRMKFL -> KPARDSSGARR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_026762"
FT VAR_SEQ 483..1179
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_026763"
FT VARIANT 89
FT /note="V -> A (in dbSNP:rs3763695)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033228"
FT VARIANT 100
FT /note="Y -> C (in dbSNP:rs7074707)"
FT /id="VAR_033229"
FT VARIANT 129
FT /note="L -> F (in dbSNP:rs3793706)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033230"
FT VARIANT 332
FT /note="S -> A (in dbSNP:rs2295774)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033231"
FT VARIANT 372
FT /note="P -> S (in dbSNP:rs2295772)"
FT /id="VAR_033232"
FT VARIANT 433
FT /note="R -> Q (in dbSNP:rs2295771)"
FT /id="VAR_053415"
FT VARIANT 478
FT /note="R -> T (in dbSNP:rs11819496)"
FT /id="VAR_053416"
FT VARIANT 527
FT /note="S -> R (in dbSNP:rs17113157)"
FT /id="VAR_033233"
FT VARIANT 1169
FT /note="A -> S (in dbSNP:rs2298075)"
FT /id="VAR_033234"
FT CONFLICT 805
FT /note="A -> V (in Ref. 2; CAB45735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1179 AA; 128697 MW; 88C591B060643A5D CRC64;
MKLKELERPA VQAWSPASQY PLYLATGTSA QQLDSSFSTN GTLEIFEVDF RDPSLDLKHR
GVLSALSRFH KLVWGSFGSG LLESSGVIVG GGDNGMLILY NVTHILSSGK EPVIAQKQKH
TGAVRALDLN PFQGNLLASG ASDSEIFIWD LNNLNVPMTL GSKSQQPPED IKALSWNRQA
QHILSSAHPS GKAVVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDIATQLV LCSEDDRLPV
IQLWDLRFAS SPLKVLESHS RGILSVSWSQ ADAELLLTSA KDSQILCRNL GSSEVVYKLP
TQSSWCFDVQ WCPRDPSVFS AASFNGWISL YSVMGRSWEV QHMRQADKIS SSFSKGQPLP
PLQVPEQVAQ APLIPPLKKP PKWIRRPTGV SFAFGGKLVT FGLPSTPAHL VPQPCPRLVF
ISQVTTESEF LMRSAELQEA LGSGNLLNYC QNKSQQALLQ SEKMLWQFLK VTLEQDSRMK
FLKLLGYSKD ELQKKVATWL KSDVGLGESP QPKGNDLNSD RQQAFCSQAS KHTTKEASAS
SAFFDELVPQ NMTPWEIPIT KDIDGLLSQA LLLGELGPAV ELCLKEERFA DAIILAQAGG
TDLLKQTQER YLAKKKTKIS SLLACVVQKN WKDVVCTCSL KNWREALALL LTYSGTEKFP
ELCDMLGTRM EQEGSRALTS EARLCYVCSG SVERLVECWA KCHQALSPMA LQDLMEKVMV
LNRSLEQLRG PHGVSPGPAT TYRVTQYANL LAAQGSLATA MSFLPRDCAQ PPVQQLRDRL
FHAQGSAVLG QQSPPFPFPR IVVGATLHSK ETSSYRLGSQ PSHQVPTPSP RPRVFTPQSS
PAMPLAPSHP SPYQGPRTQN ISDYRAPGPQ AIQPLPLSPG VRPASSQPQL LGGQRVQVPN
PVGFPGTWPL PGSPLPMACP GIMRPGSTSL PETPRLFPLL PLRPLGPGRM VSHTPAPPAS
FPVPYLPGDP GAPCSSVLPT TGILTPHPGP QDSWKEAPAP RGNLQRNKLP ETFMPPAPIT
APVMSLTPEL QGILPSQPPV SSVSHAPPGV PGELSLQLQH LPPEKMERKE LPPEHQSLKS
SFEALLQRCS LSATDLKTKR KLEEAAQRLE YLYEKLCEGT LSPHVVAGLH EVARCVDAGS
FEQGLAVHAQ VAGCSSFSEV SSFMPILKAV LIIAHKLLV
