BAP31_HUMAN
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 03-AUG-2022, entry version 202.
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; 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 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 [22]
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 [23]
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 [24]
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). {ECO:0000250|UniProtKB:Q61335,
CC ECO:0000269|PubMed:11917123, ECO:0000269|PubMed:15024066,
CC ECO:0000269|PubMed:23967155, ECO:0000269|PubMed:31206022,
CC 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=3; 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 -!- 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}.
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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; 484.
DR IntAct; P51572; 85.
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; P51572; -.
DR PeptideAtlas; P51572; -.
DR PRIDE; P51572; -.
DR ProteomicsDB; 56335; -. [P51572-1]
DR ProteomicsDB; 56336; -. [P51572-2]
DR TopDownProteomics; P51572-1; -. [P51572-1]
DR TopDownProteomics; P51572-2; -. [P51572-2]
DR Antibodypedia; 590; 509 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 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; NQASIYF; -.
DR OrthoDB; 1514108at2759; -.
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; 49 hits in 710 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 201 other tissues.
DR ExpressionAtlas; P51572; baseline and differential.
DR Genevisible; P51572; HS.
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:UniProtKB.
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:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
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: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: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:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; 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: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 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 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
