BAP31_MOUSE
ID BAP31_MOUSE Reviewed; 245 AA.
AC Q61335; A2ALM8; Q9D0E9; Q9D8G7;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=B-cell receptor-associated protein 31;
DE Short=BCR-associated protein 31;
DE Short=Bap31;
DE AltName: Full=p28;
GN Name=Bcap31; Synonyms=Bap31;
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 [MRNA], PROTEIN SEQUENCE OF 2-11, INTERACTION WITH
RP BCAP29 AND IGD, AND TISSUE SPECIFICITY.
RC TISSUE=Plasmacytoma;
RX PubMed=8612576; DOI=10.1002/j.1460-2075.1996.tb00497.x;
RA Adachi T., Schamel W.W.A., Kim K.-M., Watanabe T., Becker B., Nielsen P.J.,
RA Reth M.;
RT "The specificity of association of the IgD molecule with the accessory
RT proteins BAP31/BAP29 lies in the IgD transmembrane sequence.";
RL EMBO J. 15:1534-1541(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Small intestine;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [6]
RP PROTEIN SEQUENCE OF 150-157; 168-180; 205-213; 214-220; 221-231 AND
RP 232-242, AND INTERACTION WITH BCAP29 AND IGD.
RX PubMed=8070407; DOI=10.1002/j.1460-2075.1994.tb06690.x;
RA Kim K.-M., Adachi T., Nielsen P.J., Terashima M., Lamers M.C., Koehler G.,
RA Reth M.;
RT "Two new proteins preferentially associated with membrane immunoglobulin
RT D.";
RL EMBO J. 13:3793-3800(1994).
RN [7]
RP FUNCTION, AND INTERACTION WITH VAMP3.
RX PubMed=9396746; DOI=10.1083/jcb.139.6.1397;
RA Annaert W.G., Becker B., Kistner U., Reth M., Jahn R.;
RT "Export of cellubrevin from the endoplasmic reticulum is controlled by
RT BAP31.";
RL J. Cell Biol. 139:1397-1410(1997).
RN [8]
RP FUNCTION.
RX PubMed=15187134; DOI=10.4049/jimmunol.172.12.7548;
RA Paquet M.E., Cohen-Doyle M., Shore G.C., Williams D.B.;
RT "Bap29/31 influences the intracellular traffic of MHC class I molecules.";
RL J. Immunol. 172:7548-7555(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Functions as a chaperone protein (PubMed:9396746). Is one of
CC the most abundant endoplasmic reticulum (ER) proteins (PubMed:9396746).
CC Plays a role in the export of secreted proteins in the ER, the
CC recognition of abnormally folded protein and their targeting to the ER
CC associated-degradation (ERAD) (PubMed:9396746). Also serves as a cargo
CC receptor for the export of transmembrane proteins (PubMed:15187134).
CC Plays a role in the assembly of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I) by stimulating the translocation
CC of NDUFS4 and NDUFB11 from the cytosol to the mitochondria via
CC interaction with TOMM40 (By similarity). In response to ER stress,
CC delocalizes from the ER-mitochondria contact sites and binds BCL2 (By
CC similarity). May be involved in CASP8-mediated apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:P51572,
CC ECO:0000269|PubMed:15187134, ECO:0000269|PubMed:9396746}.
CC -!- SUBUNIT: Homodimer and heterodimer with BCAP29 (PubMed:8612576). Binds
CC CASP8 (isoform 9) as a complex containing BCAP31, BCAP29, BCL2 and/or
CC BCL2L1 (By similarity). Forms a complex (via C-terminus) with TOMM40
CC which mediates the translocation of components of the mitochondrial
CC membrane respiratory chain NADH dehydrogenase (Complex I) from the
CC cytosol to the mitochondria; within the complex BCAP31 interacts
CC directly with unprocessed and processed NDUFS4 and NDUFB11. Interacts
CC with VDAC1 (By similarity). Interacts with VAMP3, VAMP1 and membrane
CC IgD immunoglobulins (PubMed:9396746). Interacts with HACD2 (By
CC similarity). {ECO:0000250|UniProtKB:P51572, ECO:0000269|PubMed:8612576,
CC ECO:0000269|PubMed:9396746}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P51572}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250|UniProtKB:P51572}; Multi-pass membrane protein
CC {ECO:0000255}. Note=May shuttle between the ER and the intermediate
CC compartment/cis-Golgi complex. Associates with the mitochondria-
CC associated endoplasmic reticulum membrane via interaction with TOMM40.
CC {ECO:0000250|UniProtKB:P51572}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8612576}.
CC -!- PTM: Cleaved by CASP8 and other caspases. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family. {ECO:0000305}.
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DR EMBL; X81816; CAA57414.1; -; mRNA.
DR EMBL; AK008043; BAB25427.1; -; mRNA.
DR EMBL; AK011500; BAB27660.1; -; mRNA.
DR EMBL; AL805924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466650; EDL29886.1; -; Genomic_DNA.
DR EMBL; BC002106; AAH02106.1; -; mRNA.
DR CCDS; CCDS30209.1; -.
DR PIR; S71116; S71116.
DR RefSeq; NP_001300627.1; NM_001313698.1.
DR RefSeq; NP_036190.2; NM_012060.5.
DR RefSeq; XP_006528111.1; XM_006528048.2.
DR RefSeq; XP_011245902.1; XM_011247600.2.
DR AlphaFoldDB; Q61335; -.
DR SMR; Q61335; -.
DR BioGRID; 205116; 3.
DR IntAct; Q61335; 3.
DR MINT; Q61335; -.
DR STRING; 10090.ENSMUSP00000002091; -.
DR iPTMnet; Q61335; -.
DR PhosphoSitePlus; Q61335; -.
DR SwissPalm; Q61335; -.
DR EPD; Q61335; -.
DR jPOST; Q61335; -.
DR MaxQB; Q61335; -.
DR PaxDb; Q61335; -.
DR PRIDE; Q61335; -.
DR ProteomicsDB; 277111; -.
DR TopDownProteomics; Q61335; -.
DR Antibodypedia; 590; 509 antibodies from 45 providers.
DR DNASU; 27061; -.
DR Ensembl; ENSMUST00000002091; ENSMUSP00000002091; ENSMUSG00000002015.
DR GeneID; 27061; -.
DR KEGG; mmu:27061; -.
DR UCSC; uc009tmj.1; mouse.
DR CTD; 10134; -.
DR MGI; MGI:1350933; Bcap31.
DR VEuPathDB; HostDB:ENSMUSG00000002015; -.
DR eggNOG; KOG1962; Eukaryota.
DR GeneTree; ENSGT00390000011863; -.
DR HOGENOM; CLU_070975_1_0_1; -.
DR InParanoid; Q61335; -.
DR OMA; NQASIYF; -.
DR OrthoDB; 1514108at2759; -.
DR PhylomeDB; Q61335; -.
DR TreeFam; TF315310; -.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-75153; Apoptotic execution phase.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 27061; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Bcap31; mouse.
DR PRO; PR:Q61335; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q61335; protein.
DR Bgee; ENSMUSG00000002015; Expressed in paneth cell and 259 other tissues.
DR Genevisible; Q61335; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042288; F:MHC class I protein binding; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:MGI.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; ISO:MGI.
DR GO; GO:1904154; P:positive regulation of retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IGI:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEP:BHF-UCL.
DR InterPro; IPR008417; BAP29/BAP31.
DR InterPro; IPR040463; BAP29/BAP31_N.
DR InterPro; IPR041672; Bap31/Bap29_C.
DR PANTHER; PTHR12701; PTHR12701; 1.
DR Pfam; PF05529; Bap31; 1.
DR Pfam; PF18035; Bap31_Bap29_C; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Coiled coil; Direct protein sequencing; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51572"
FT CHAIN 2..245
FT /note="B-cell receptor-associated protein 31"
FT /id="PRO_0000142892"
FT TOPO_DOM 2..6
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..102
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 165..236
FT /evidence="ECO:0000250"
FT MOTIF 242..245
FT /note="Di-lysine motif"
FT SITE 164..165
FT /note="Cleavage; by caspase-8"
FT /evidence="ECO:0000255"
FT CONFLICT 28
FT /note="S -> Y (in Ref. 2; BAB25427)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="F -> L (in Ref. 1; CAA57414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27957 MW; A8C53B7A04E06C97 CRC64;
MSLQWTTVAT FLYAEVFAVL LLCIPFISPK RWQKVFKSRL VELVVTYGNT FFVVLIVILV
LLVIDAVREI LKYDDVTEKV NLQNNPGAME HFHMKLFRAQ RNLYIAGFSL LLSFLLRRLV
TLISQQATLL ASNEAFKKQA ESASEAAKKY MEENDQLKKG AAEDGDKLDI GNTEMKLEEN
KSLKNDLRKL KDELASTKKK LEKAENEALA MQKQSEGLTK EYDRLLEEHA KLQASVRGPS
VKKEE
