SC31B_MOUSE
ID SC31B_MOUSE Reviewed; 1158 AA.
AC Q3TZ89; Q811L4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein transport protein Sec31B;
DE AltName: Full=SEC31-like protein 2;
DE AltName: Full=SEC31-related protein B;
GN Name=Sec31b; Synonyms=Gm341, Sec31l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 791-1158 (ISOFORMS 1/2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q9NQW1}.
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 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9NQW1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQW1}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q9NQW1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9NQW1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9NQW1}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NQW1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9NQW1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TZ89-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TZ89-2; Sequence=VSP_026764;
CC -!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex,
CC leading to regulate the size of COPII coats.
CC {ECO:0000250|UniProtKB:Q9NQW1}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; AK158017; BAE34320.1; -; mRNA.
DR EMBL; AC151478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042701; AAH42701.1; -; mRNA.
DR CCDS; CCDS37997.1; -. [Q3TZ89-1]
DR RefSeq; NP_001028515.1; NM_001033343.1. [Q3TZ89-1]
DR AlphaFoldDB; Q3TZ89; -.
DR SMR; Q3TZ89; -.
DR BioGRID; 232221; 1.
DR STRING; 10090.ENSMUSP00000064900; -.
DR iPTMnet; Q3TZ89; -.
DR PhosphoSitePlus; Q3TZ89; -.
DR SwissPalm; Q3TZ89; -.
DR jPOST; Q3TZ89; -.
DR MaxQB; Q3TZ89; -.
DR PaxDb; Q3TZ89; -.
DR PeptideAtlas; Q3TZ89; -.
DR PRIDE; Q3TZ89; -.
DR ProteomicsDB; 255466; -. [Q3TZ89-1]
DR ProteomicsDB; 255467; -. [Q3TZ89-2]
DR Antibodypedia; 49267; 87 antibodies from 19 providers.
DR Ensembl; ENSMUST00000063632; ENSMUSP00000064900; ENSMUSG00000051984. [Q3TZ89-1]
DR Ensembl; ENSMUST00000111985; ENSMUSP00000107616; ENSMUSG00000051984. [Q3TZ89-2]
DR GeneID; 240667; -.
DR KEGG; mmu:240667; -.
DR UCSC; uc008hpu.1; mouse. [Q3TZ89-1]
DR CTD; 25956; -.
DR MGI; MGI:2685187; Sec31b.
DR VEuPathDB; HostDB:ENSMUSG00000051984; -.
DR eggNOG; KOG0307; Eukaryota.
DR GeneTree; ENSGT00390000003175; -.
DR HOGENOM; CLU_003033_1_0_1; -.
DR InParanoid; Q3TZ89; -.
DR OMA; AQWAFGG; -.
DR OrthoDB; 100998at2759; -.
DR PhylomeDB; Q3TZ89; -.
DR TreeFam; TF313842; -.
DR BioGRID-ORCS; 240667; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q3TZ89; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3TZ89; protein.
DR Bgee; ENSMUSG00000051984; Expressed in hindlimb stylopod muscle and 49 other tissues.
DR ExpressionAtlas; Q3TZ89; baseline and differential.
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; ISO: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; 2.
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..1158
FT /note="Protein transport protein Sec31B"
FT /id="PRO_0000295154"
FT REPEAT 4..47
FT /note="WD 1"
FT REPEAT 65..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 376..407
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 485..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026764"
FT CONFLICT 275
FT /note="L -> P (in Ref. 1; BAE34320)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="M -> I (in Ref. 1; BAE34320)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="K -> R (in Ref. 1; BAE34320)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="R -> G (in Ref. 1; BAE34320)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="A -> E (in Ref. 1; BAE34320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046
FT /note="T -> A (in Ref. 1; BAE34320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1158 AA; 125633 MW; 86EE5CD7F518691B CRC64;
MKLKELEKPA VQAWSPARQY PVYLATGTSA QQLDASFSTN ATLEIFEIDF RDPSLDLKHK
GILSVSSRFH KLIWGSFGSG LLENSGVIAG GGDNGTLTLY NVTHVLSSGK EPLIAQKQKH
TGAVRALDFN PFQGNLLASG ASDSEIFIWD LNHLSVPMTP GPKSQNPPED IKALSWNLQV
QHILASAHPS GKAVVWDLRK NEPIIKVSSH SSRMNCSGLA WNPDIATQLV LCSEDDQLPV
IQLWDLRFAS SPLKVLESHS RGILSMSWNQ ADAELLLSTA KDSQIFCWNL SSSEVVYKLP
TQSSWCFDVQ WCPQSPPVFS AVSFDGWISL CSVMGRSWEA QHMRQADKVP EQVAQASLIP
PLKKPPKWMR RPAGGSFAFG GKLVTFGLPS IPVQPVAQAC SRPVFISQVI TESEVLTRSV
VLQEALGSGN LLNYCQSKVQ QASLPCEKIL WQFLKVTLEQ DSRPKFLGLL GYSREELQKK
VDTCLKSDSK SQESPQLEAV DLKSDRAHSP CAQASKHTAK EASESSAFFD ELIPQNMTPW
EIPTTEDTDG LLSQALLLGE LRSAVELCLK EERFADAIIL AQAGDAELLK WTQERYLAKR
RTKTSSLLAC VVKKNWKDLV CACRLKNWRE ALALLLTYSG PEKFPELCDM LGTRMEQEGG
RALTSEARLC YVCSGSVERL VESWAKFQQA SSPMALQELM EQVTVLSRSL ELLQGSNKMS
PGPATTHRLT QYANLLAAQG SLATAMSFLP SDCIQPGVQQ LRDRLFHAQG SAVLGQQAPA
FPFPRVAVGA ALHSKETSSY RRGLQPPQQV PAPSVRPRTT AQPSSVMPFS PSQPSPSQGS
SDHRVLRPQA ILPGHFVPGV RPALSPPQLS GGQSVPAVNP AGFCGAWPLP GPTPVMASPD
FMQPGSTHLP ETPRLLPLPP VGPPGPNPLS SQLPASPVTF SVAPPPGGPR APCSSALPSS
GILATCPGPQ DSWKVSPASQ GNLQRKKLPE TFMPPAPITA PLRSLGPEPQ QALLPQPLVS
SATLPPPGAP RECSLQQLQP LPPERTEKEL PPEHQCVKDS FEALLQRCSL TATDLKTKRK
LEEAARRLEC LYEKLCEGTL SPHVLAGLHE VARCVDAGSF EQGLAVHAQV AGCSSFSEVS
SFMPMLKAVL TIAHKLQG
