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   27-MAR-2024, entry version 176.
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,
RC   Pancreas, 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). Interacts with DNM1L; may form part of a larger protein
CC       complex at the endoplasmic reticulum-mitochondrial interface during
CC       mitochondrial fission (By similarity). {ECO:0000250|UniProtKB:P51572,
CC       ECO:0000269|PubMed:8612576, 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; 5.
DR   IntAct; Q61335; 3.
DR   MINT; Q61335; -.
DR   STRING; 10090.ENSMUSP00000002091; -.
DR   GlyGen; Q61335; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61335; -.
DR   MetOSite; Q61335; -.
DR   PhosphoSitePlus; Q61335; -.
DR   SwissPalm; Q61335; -.
DR   EPD; Q61335; -.
DR   jPOST; Q61335; -.
DR   MaxQB; Q61335; -.
DR   PaxDb; 10090-ENSMUSP00000002091; -.
DR   ProteomicsDB; 277111; -.
DR   Pumba; Q61335; -.
DR   TopDownProteomics; Q61335; -.
DR   Antibodypedia; 590; 550 antibodies from 45 providers.
DR   DNASU; 27061; -.
DR   Ensembl; ENSMUST00000002091.6; ENSMUSP00000002091.6; ENSMUSG00000002015.6.
DR   GeneID; 27061; -.
DR   KEGG; mmu:27061; -.
DR   UCSC; uc009tmj.1; mouse.
DR   AGR; MGI:1350933; -.
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; AGREIWK; -.
DR   OrthoDB; 2882163at2759; -.
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 80 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 263 other cell types or tissues.
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: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:0005886; C:plasma membrane; 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:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; 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   Gene3D; 1.20.5.110; -; 1.
DR   InterPro; IPR008417; BAP29/BAP31.
DR   InterPro; IPR040463; BAP29/BAP31_N.
DR   InterPro; IPR041672; Bap31/Bap29_C.
DR   PANTHER; PTHR12701:SF15; B-CELL RECEPTOR-ASSOCIATED PROTEIN 31; 1.
DR   PANTHER; PTHR12701; BCR-ASSOCIATED PROTEIN, BAP; 1.
DR   Pfam; PF05529; Bap31; 1.
DR   Pfam; PF18035; Bap31_Bap29_C; 1.
DR   Genevisible; Q61335; MM.
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
//