ID BAP31_HUMAN Reviewed; 246 AA. AC P51572; B3KQ79; D3DWV5; Q13836; Q96CF0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 211. DE RecName: Full=B-cell receptor-associated protein 31; DE Short=BCR-associated protein 31; DE Short=Bap31; DE AltName: Full=6C6-AG tumor-associated antigen; DE AltName: Full=Protein CDM; DE AltName: Full=p28; GN Name=BCAP31 {ECO:0000312|HGNC:HGNC:16695}; GN Synonyms=BAP31 {ECO:0000303|PubMed:25854864}, DXS1357E; 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). RX PubMed=7806238; DOI=10.1006/geno.1994.1413; RA Mosser J., Sarde C.-O., Vicaire S., Yates J.R., Mandel J.-L.; RT "A new human gene (DXS1357E) with ubiquitous expression, located in Xq28 RT adjacent to the adrenoleukodystrophy gene."; RL Genomics 22:469-471(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8706661; DOI=10.1111/j.1432-1033.1996.0631w.x; RA Li E., Bestagno M., Burrone O.; RT "Molecular cloning and characterization of a transmembrane surface antigen RT in human cells."; RL Eur. J. Biochem. 238:631-638(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=B-cell, and Promyelocytic leukemia; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Stomach, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Pancreas; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-246. RA Eichler E.E., Lu F., Shen Y., Muzny D.M., Gibbs R.A., Nelson D.L.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 2-11, SUBCELLULAR LOCATION, AND INTERACTION WITH BCL2; RP BCL2L1 AND CASP8. RX PubMed=9334338; DOI=10.1083/jcb.139.2.327; RA Ng F.W.H., Nguyen M., Kwan T., Branton P.E., Nicholson D.W., Cromlish J.A., RA Shore G.C.; RT "p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the RT endoplasmic reticulum."; RL J. Cell Biol. 139:327-338(1997). RN [10] RP PROTEIN SEQUENCE OF 80-96 AND 205-214, SUBCELLULAR LOCATION, AND FUNCTION. 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 [11] RP MUTAGENESIS OF ASP-164 AND ASP-238, AND ROLE IN APOPTOSIS. RX PubMed=10958671; DOI=10.1128/mcb.20.18.6731-6740.2000; RA Nguyen M., Breckenridge D.G., Ducret A., Shore G.C.; RT "Caspase-resistant BAP31 inhibits Fas-mediated apoptotic membrane RT fragmentation and release of cytochrome c from mitochondria."; RL Mol. Cell. Biol. 20:6731-6740(2000). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=11042173; DOI=10.1074/jbc.m006143200; RA Bell A.W., Ward M.A., Blackstock W.P., Freeman H.N.M., Choudhary J.S., RA Lewis A.P., Chotai D., Fazel A., Gushue J.N., Paiement J., Palcy S., RA Chevet E., Lafreniere-Roula M., Solari R., Thomas D.Y., Rowley A., RA Bergeron J.J.M.; RT "Proteomics characterization of abundant Golgi membrane proteins."; RL J. Biol. Chem. 276:5152-5165(2001). RN [13] RP TISSUE SPECIFICITY. RX PubMed=11561007; DOI=10.1177/002215540104901005; RA Manley H.A., Lennon V.A.; RT "Endoplasmic reticulum membrane-sorting protein of lymphocytes (BAP31) is RT highly expressed in neurons and discrete endocrine cells."; RL J. Histochem. Cytochem. 49:1235-1243(2001). RN [14] RP INTERACTION WITH CASP8 ISOFORM 9. RX PubMed=11917123; DOI=10.1073/pnas.072088099; RA Breckenridge D.G., Nguyen M., Kuppig S., Reth M., Shore G.C.; RT "The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at RT the endoplasmic reticulum."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4331-4336(2002). RN [15] RP INTERACTION WITH HACD2. RX PubMed=15024066; DOI=10.1128/mcb.24.7.2767-2778.2004; RA Wang B., Pelletier J., Massaad M.J., Herscovics A., Shore G.C.; RT "The yeast split-ubiquitin membrane protein two-hybrid screen identifies RT BAP31 as a regulator of the turnover of endoplasmic reticulum-associated RT protein tyrosine phosphatase-like B."; RL Mol. Cell. Biol. 24:2767-2778(2004). RN [16] RP INVOLVEMENT IN CONTIGUOUS ABCD1/DXS1375E DELETION SYNDROME. RX PubMed=11992258; DOI=10.1086/340849; RA Corzo D., Gibson W., Johnson K., Mitchell G., LePage G., Cox G.F., RA Casey R., Zeiss C., Tyson H., Cutting G.R., Raymond G.V., Smith K.D., RA Watkins P.A., Moser A.B., Moser H.W., Steinberg S.J.; RT "Contiguous deletion of the X-linked adrenoleukodystrophy gene (ABCD1) and RT DXS1357E: a novel neonatal phenotype similar to peroxisomal biogenesis RT disorders."; RL Am. J. Hum. Genet. 70:1520-1531(2002). RN [17] RP FUNCTION. RX PubMed=18287538; DOI=10.1091/mbc.e07-08-0781; RA Wakana Y., Takai S., Nakajima K., Tani K., Yamamoto A., Watson P., RA Stephens D.J., Hauri H.P., Tagaya M.; RT "Bap31 is an itinerant protein that moves between the peripheral RT endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER- RT associated Degradation."; RL Mol. Biol. Cell 19:1825-1836(2008). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP INVOLVEMENT IN DDCH. RX PubMed=24011989; DOI=10.1016/j.ajhg.2013.07.023; RA Cacciagli P., Sutera-Sardo J., Borges-Correia A., Roux J.C., Dorboz I., RA Desvignes J.P., Badens C., Delepine M., Lathrop M., Cau P., Levy N., RA Girard N., Sarda P., Boespflug-Tanguy O., Villard L.; RT "Mutations in BCAP31 cause a severe X-linked phenotype with deafness, RT dystonia, and central hypomyelination and disorganize the Golgi RT apparatus."; RL Am. J. Hum. Genet. 93:579-586(2013). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP INTERACTION WITH DNM1L. RX PubMed=24196833; DOI=10.1091/mbc.e13-09-0525; RA Shen Q., Yamano K., Head B.P., Kawajiri S., Cheung J.T., Wang C., Cho J.H., RA Hattori N., Youle R.J., van der Bliek A.M.; RT "Mutations in Fis1 disrupt orderly disposal of defective mitochondria."; RL Mol. Biol. Cell 25:145-159(2014). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP INTERACTION WITH HRSV SH (MICROBIAL INFECTION). RX PubMed=25854864; DOI=10.1016/j.virol.2015.03.034; RA Li Y., Jain N., Limpanawat S., To J., Quistgaard E.M., Nordlund P., RA Thanabalu T., Torres J.; RT "Interaction between human BAP31 and respiratory syncytial virus small RT hydrophobic (SH) protein."; RL Virology 482:105-110(2015). RN [24] RP FUNCTION, INTERACTION WITH TOMM40; NDUFS4; NDUFB11; VDAC1 AND BCL2, AND RP SUBCELLULAR LOCATION. RX PubMed=31206022; DOI=10.1126/sciadv.aaw1386; RA Namba T.; RT "BAP31 regulates mitochondrial function via interaction with Tom40 within RT ER-mitochondria contact sites."; RL Sci. Adv. 5:eaaw1386-eaaw1386(2019). RN [25] RP SUBCELLULAR LOCATION (MICROBIAL INFECTION). RX PubMed=25631089; DOI=10.1128/jvi.03574-14; RA Bagchi P., Walczak C.P., Tsai B.; RT "The endoplasmic reticulum membrane J protein C18 executes a distinct role RT in promoting simian virus 40 membrane penetration."; RL J. Virol. 89:4058-4068(2015). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 168-233, SUBUNIT, AND COILED-COIL. RX PubMed=23967155; DOI=10.1371/journal.pone.0071111; RA Quistgaard E.M., Low C., Moberg P., Guettou F., Maddi K., Nordlund P.; RT "Structural and biophysical characterization of the cytoplasmic domains of RT human BAP29 and BAP31."; RL PLoS ONE 8:E71111-E71111(2013). CC -!- FUNCTION: Functions as a chaperone protein (PubMed:9396746, CC PubMed:18287538). Is one of the most abundant endoplasmic reticulum CC (ER) proteins (PubMed:9396746, PubMed:18287538). Plays a role in the CC export of secreted proteins in the ER, the recognition of abnormally CC folded protein and their targeting to the ER associated-degradation CC (ERAD) (PubMed:9396746, PubMed:18287538). Also serves as a cargo CC receptor for the export of transmembrane proteins (By similarity). 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 (PubMed:31206022). In response to ER stress, CC delocalizes from the ER-mitochondria contact sites and binds BCL2 CC (PubMed:31206022). May be involved in CASP8-mediated apoptosis CC (PubMed:10958671). {ECO:0000250|UniProtKB:Q61335, CC ECO:0000269|PubMed:10958671, ECO:0000269|PubMed:18287538, CC ECO:0000269|PubMed:31206022, ECO:0000269|PubMed:9396746}. CC -!- SUBUNIT: Homodimer and heterodimer with BCAP29 (PubMed:9334338, CC PubMed:23967155). Binds CASP8 (isoform 9) as a complex containing CC BCAP31, BCAP29, BCL2 and/or BCL2L1 (PubMed:9334338, PubMed:11917123, CC PubMed:31206022). Forms a complex (via C-terminus) with TOMM40 which CC mediates the translocation of components of the mitochondrial membrane CC respiratory chain NADH dehydrogenase (Complex I) from the cytosol to CC the mitochondria; within the complex BCAP31 interacts directly with CC unprocessed and processed NDUFS4 and NDUFB11 (PubMed:31206022). CC Interacts with VDAC1 (PubMed:31206022). Interacts with VAMP3, VAMP1 and CC membrane IgD immunoglobulins (By similarity). Interacts with HACD2 CC (PubMed:15024066). Interacts with DNM1L; may form part of a larger CC protein complex at the endoplasmic reticulum-mitochondrial interface CC during mitochondrial fission (PubMed:24196833). CC {ECO:0000250|UniProtKB:Q61335, ECO:0000269|PubMed:11917123, CC ECO:0000269|PubMed:15024066, ECO:0000269|PubMed:23967155, CC ECO:0000269|PubMed:31206022, ECO:0000269|PubMed:9334338}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with HRSV CC membrane protein SH; this interaction is direct. CC {ECO:0000269|PubMed:25854864}. CC -!- INTERACTION: CC P51572; P05067: APP; NbExp=3; IntAct=EBI-77683, EBI-77613; CC P51572; P10415: BCL2; NbExp=2; IntAct=EBI-77683, EBI-77694; CC P51572; Q14790: CASP8; NbExp=3; IntAct=EBI-77683, EBI-78060; CC P51572; P13569: CFTR; NbExp=9; IntAct=EBI-77683, EBI-349854; CC P51572; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-77683, EBI-398977; CC P51572; Q9Y3D6: FIS1; NbExp=8; IntAct=EBI-77683, EBI-3385283; CC P51572; Q6Y1H2: HACD2; NbExp=4; IntAct=EBI-77683, EBI-530257; CC P51572; P42858: HTT; NbExp=4; IntAct=EBI-77683, EBI-466029; CC P51572; Q92876: KLK6; NbExp=3; IntAct=EBI-77683, EBI-2432309; CC P51572; P60468: SEC61B; NbExp=7; IntAct=EBI-77683, EBI-1788819; CC P51572; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-77683, EBI-6268651; CC P51572; Q15629: TRAM1; NbExp=5; IntAct=EBI-77683, EBI-1788852; CC P51572; Q77YB1: SH (1A); Xeno; NbExp=6; IntAct=EBI-77683, EBI-11358177; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:31206022, ECO:0000269|PubMed:9334338, CC ECO:0000269|PubMed:9396746}; Multi-pass membrane protein {ECO:0000255}. CC Endoplasmic reticulum-Golgi intermediate compartment membrane CC {ECO:0000269|PubMed:11042173, ECO:0000269|PubMed:9396746}; Multi-pass CC membrane protein {ECO:0000255}. Note=May shuttle between the ER and the CC intermediate compartment/cis-Golgi complex (PubMed:9396746). Associates CC with the mitochondria-associated endoplasmic reticulum membrane via CC interaction with TOMM40 (PubMed:31206022). CC {ECO:0000269|PubMed:31206022, ECO:0000269|PubMed:9396746}. CC -!- SUBCELLULAR LOCATION: Note=(Microbial infection) Upon SV40 infection, CC colocalizes with DNAJC18, DNAJB12 and DNAJB14 in punctate structures CC within the endoplasmic reticulum membrane. CC {ECO:0000269|PubMed:25631089}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P51572-1; Sequence=Displayed; CC Name=2; CC IsoId=P51572-2; Sequence=VSP_043116; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in neurons and CC discrete endocrine cells. {ECO:0000269|PubMed:11561007}. CC -!- PTM: Cleaved by CASP8 and other caspases. CC -!- DISEASE: Deafness, dystonia, and cerebral hypomyelination (DDCH) CC [MIM:300475]: An X-linked recessive syndrome characterized by CC sensorineural deafness, intellectual disability, dysmorphic facial CC features, dystonia, pyramidal signs, almost no psychomotor development, CC and hypomyelination on brain imaging. {ECO:0000269|PubMed:24011989}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Note=BCAP31 is deleted in the chromosome Xq28 deletion CC syndrome which involves BCAP31 and the and the promoter region of CC ABCD1. {ECO:0000269|PubMed:11992258}. CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z31696; CAA83501.1; -; mRNA. DR EMBL; X81109; CAA57015.1; -; mRNA. DR EMBL; X81817; CAA57415.1; -; mRNA. DR EMBL; AK057613; BAG51941.1; -; mRNA. DR EMBL; AK125631; BAG54226.1; -; mRNA. DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471172; EAW72818.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72819.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72820.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72821.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72823.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72824.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72825.1; -; Genomic_DNA. DR EMBL; BC014323; AAH14323.1; -; mRNA. DR EMBL; BC065292; AAH65292.1; -; mRNA. DR EMBL; U36341; AAA79508.1; -; Genomic_DNA. DR CCDS; CCDS14727.1; -. [P51572-1] DR CCDS; CCDS48191.1; -. [P51572-2] DR PIR; S44279; S44279. DR RefSeq; NP_001132913.1; NM_001139441.1. [P51572-1] DR RefSeq; NP_001132929.1; NM_001139457.2. [P51572-2] DR RefSeq; NP_001243376.1; NM_001256447.1. [P51572-1] DR RefSeq; NP_005736.3; NM_005745.7. [P51572-1] DR PDB; 4JZL; X-ray; 2.20 A; A/B/C/D=168-233. DR PDB; 4JZP; X-ray; 2.10 A; A/B=168-233. DR PDBsum; 4JZL; -. DR PDBsum; 4JZP; -. DR AlphaFoldDB; P51572; -. DR SMR; P51572; -. DR BioGRID; 115437; 538. DR IntAct; P51572; 89. DR MINT; P51572; -. DR STRING; 9606.ENSP00000392330; -. DR ChEMBL; CHEMBL4295778; -. DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family. DR GlyGen; P51572; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P51572; -. DR MetOSite; P51572; -. DR PhosphoSitePlus; P51572; -. DR SwissPalm; P51572; -. DR BioMuta; BCAP31; -. DR DMDM; 1705725; -. DR EPD; P51572; -. DR jPOST; P51572; -. DR MassIVE; P51572; -. DR MaxQB; P51572; -. DR PaxDb; 9606-ENSP00000392330; -. DR PeptideAtlas; P51572; -. DR ProteomicsDB; 56335; -. [P51572-1] DR ProteomicsDB; 56336; -. [P51572-2] DR Pumba; P51572; -. DR TopDownProteomics; P51572-1; -. [P51572-1] DR TopDownProteomics; P51572-2; -. [P51572-2] DR Antibodypedia; 590; 550 antibodies from 45 providers. DR DNASU; 10134; -. DR Ensembl; ENST00000345046.12; ENSP00000343458.6; ENSG00000185825.17. [P51572-1] DR Ensembl; ENST00000458587.8; ENSP00000392330.2; ENSG00000185825.17. [P51572-2] DR Ensembl; ENST00000647529.1; ENSP00000494052.1; ENSG00000185825.17. [P51572-1] DR Ensembl; ENST00000672675.1; ENSP00000499882.1; ENSG00000185825.17. [P51572-1] DR GeneID; 10134; -. DR KEGG; hsa:10134; -. DR MANE-Select; ENST00000345046.12; ENSP00000343458.6; NM_001256447.2; NP_001243376.1. DR UCSC; uc004fid.4; human. [P51572-1] DR AGR; HGNC:16695; -. DR CTD; 10134; -. DR DisGeNET; 10134; -. DR GeneCards; BCAP31; -. DR HGNC; HGNC:16695; BCAP31. DR HPA; ENSG00000185825; Low tissue specificity. DR MalaCards; BCAP31; -. DR MIM; 300398; gene. DR MIM; 300475; phenotype. DR neXtProt; NX_P51572; -. DR OpenTargets; ENSG00000185825; -. DR Orphanet; 369942; CADDS. DR Orphanet; 369939; Severe motor and intellectual disabilities-sensorineural deafness-dystonia syndrome. DR PharmGKB; PA128394569; -. DR VEuPathDB; HostDB:ENSG00000185825; -. DR eggNOG; KOG1962; Eukaryota. DR GeneTree; ENSGT00390000011863; -. DR HOGENOM; CLU_070975_1_0_1; -. DR InParanoid; P51572; -. DR OMA; AGREIWK; -. DR OrthoDB; 2882163at2759; -. DR PhylomeDB; P51572; -. DR TreeFam; TF315310; -. DR PathwayCommons; P51572; -. DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins. DR Reactome; R-HSA-75153; Apoptotic execution phase. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; P51572; -. DR BioGRID-ORCS; 10134; 52 hits in 786 CRISPR screens. DR ChiTaRS; BCAP31; human. DR GeneWiki; BCAP31; -. DR GenomeRNAi; 10134; -. DR Pharos; P51572; Tbio. DR PRO; PR:P51572; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P51572; Protein. DR Bgee; ENSG00000185825; Expressed in left adrenal gland and 203 other cell types or tissues. DR ExpressionAtlas; P51572; baseline and differential. DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:Ensembl. DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl. DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:AgBase. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042288; F:MHC class I protein binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IMP:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IMP:UniProtKB. DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:UniProtKB. DR GO; GO:1904294; P:positive regulation of ERAD pathway; IGI:ParkinsonsUK-UCL. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IMP:UniProtKB. DR GO; GO:1904154; P:positive regulation of retrograde protein transport, ER to cytosol; IDA:ParkinsonsUK-UCL. DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL. DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central. DR GO; GO:0006626; P:protein targeting to mitochondrion; IGI:UniProtKB. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. 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; P51572; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Coiled coil; Deafness; KW Direct protein sequencing; Dystonia; Endoplasmic reticulum; KW ER-Golgi transport; Host-virus interaction; Intellectual disability; KW Membrane; Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9334338" FT CHAIN 2..246 FT /note="B-cell receptor-associated protein 31" FT /id="PRO_0000142891" 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..246 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT COILED 165..237 FT /evidence="ECO:0000269|PubMed:23967155" FT MOTIF 243..246 FT /note="Di-lysine motif" FT SITE 164..165 FT /note="Cleavage; by caspase-8" FT /evidence="ECO:0000255" FT SITE 238..239 FT /note="Cleavage; by caspase-8" FT /evidence="ECO:0000255" FT VAR_SEQ 1 FT /note="M -> MGAEASSSWCPGTALPEERLSVKRASEISGFLGQGSSGEAALDVLTH FT VLEGAGNKLTSSCGKPSSNRM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043116" FT MUTAGEN 164 FT /note="D->A: Abolishes cleavage by caspases, inhibits FT apoptotic membrane blebbing and release of cytochrome c FT from mitochondria; when associated with A-238." FT /evidence="ECO:0000269|PubMed:10958671" FT MUTAGEN 238 FT /note="D->A: Abolishes cleavage by caspases, inhibits FT apoptotic membrane blebbing and release of cytochrome c FT from mitochondria; when associated with A-164." FT /evidence="ECO:0000269|PubMed:10958671" FT CONFLICT 2 FT /note="S -> T (in Ref. 3; CAA57415)" FT /evidence="ECO:0000305" FT CONFLICT 72 FT /note="K -> E (in Ref. 7; AAH14323)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="Q -> E (in Ref. 3; CAA57415)" FT /evidence="ECO:0000305" FT HELIX 170..219 FT /evidence="ECO:0007829|PDB:4JZP" SQ SEQUENCE 246 AA; 27992 MW; D34367F870D6EB00 CRC64; MSLQWTAVAT FLYAEVFVVL LLCIPFISPK RWQKIFKSRL VELLVSYGNT FFVVLIVILV LLVIDAVREI RKYDDVTEKV NLQNNPGAME HFHMKLFRAQ RNLYIAGFSL LLSFLLRRLV TLISQQATLL ASNEAFKKQA ESASEAAKKY MEENDQLKKG AAVDGGKLDV GNAEVKLEEE NRSLKADLQK LKDELASTKQ KLEKAENQVL AMRKQSEGLT KEYDRLLEEH AKLQAAVDGP MDKKEE //