Full text data of BCAP31
BCAP31
(BAP31, DXS1357E)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
B-cell receptor-associated protein 31; BCR-associated protein 31; Bap31 (6C6-AG tumor-associated antigen; Protein CDM; p28)
B-cell receptor-associated protein 31; BCR-associated protein 31; Bap31 (6C6-AG tumor-associated antigen; Protein CDM; p28)
Comments
Isoform P51572-2 was detected.
Isoform P51572-2 was detected.
UniProt
P51572
ID BAP31_HUMAN Reviewed; 246 AA.
AC P51572; B3KQ79; D3DWV5; Q13836; Q96CF0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 133.
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, DXS1357E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT Xq28 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
RT antigen 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;
RA Adachi T., Schamel W.W.A., Kim K.-M., Watanabe T., Becker B.,
RA Nielsen P.J., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP BCL2; 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.,
RA Cromlish J.A., 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
RP 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 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
RT complex at the endoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4331-4336(2002).
RN [13]
RP INTERACTION WITH PTPLB.
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
RT identifies BAP31 as a regulator of the turnover of endoplasmic
RT reticulum-associated protein tyrosine phosphatase-like B.";
RL Mol. Cell. Biol. 24:2767-2778(2004).
RN [14]
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)
RT and DXS1357E: a novel neonatal phenotype similar to peroxisomal
RT biogenesis disorders.";
RL Am. J. Hum. Genet. 70:1520-1531(2002).
RN [15]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role in anterograde transport of membrane
CC proteins from the endoplasmic reticulum to the Golgi. May be
CC involved in CASP8-mediated apoptosis.
CC -!- SUBUNIT: Homodimer and heterodimer with BCAP29. Binds CASP8
CC (isoform 9) as a complex containing BCAP31, BCAP29, BCL2 and/or
CC BCL2L1. Interacts with VAMP3, VAMP1 and membrane IgD
CC immunoglobulins. May interact with ACTG1 and non-muscle myosin II.
CC Interacts with PTPLB.
CC -!- INTERACTION:
CC P10415:BCL2; NbExp=2; IntAct=EBI-77683, EBI-77694;
CC Q14790:CASP8; NbExp=3; IntAct=EBI-77683, EBI-78060;
CC P13569:CFTR; NbExp=3; IntAct=EBI-77683, EBI-349854;
CC Q9BUN8:DERL1; NbExp=3; IntAct=EBI-77683, EBI-398977;
CC Q9Y3D6:FIS1; NbExp=8; IntAct=EBI-77683, EBI-3385283;
CC Q6Y1H2:PTPLB; NbExp=4; IntAct=EBI-77683, EBI-530257;
CC P60468:SEC61B; NbExp=7; IntAct=EBI-77683, EBI-1788819;
CC Q15629:TRAM1; NbExp=5; IntAct=EBI-77683, EBI-1788852;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Multi-pass membrane protein. Note=May
CC shuttle between the ER and the intermediate compartment/cis-Golgi
CC complex.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Cleaved by CASP8 and other caspases.
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.
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family.
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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 PIR; S44279; S44279.
DR RefSeq; NP_001132913.1; NM_001139441.1.
DR RefSeq; NP_001132929.1; NM_001139457.2.
DR RefSeq; NP_001243376.1; NM_001256447.1.
DR RefSeq; NP_005736.3; NM_005745.7.
DR UniGene; Hs.522817; -.
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 ProteinModelPortal; P51572; -.
DR IntAct; P51572; 22.
DR MINT; MINT-3018869; -.
DR STRING; 9606.ENSP00000392330; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR PhosphoSite; P51572; -.
DR DMDM; 1705725; -.
DR PaxDb; P51572; -.
DR PRIDE; P51572; -.
DR DNASU; 10134; -.
DR Ensembl; ENST00000345046; ENSP00000343458; ENSG00000185825.
DR Ensembl; ENST00000441714; ENSP00000405417; ENSG00000185825.
DR Ensembl; ENST00000458587; ENSP00000392330; ENSG00000185825.
DR Ensembl; ENST00000596601; ENSP00000473146; ENSG00000267977.
DR Ensembl; ENST00000597329; ENSP00000472030; ENSG00000267977.
DR Ensembl; ENST00000600824; ENSP00000472405; ENSG00000267977.
DR GeneID; 10134; -.
DR KEGG; hsa:10134; -.
DR UCSC; uc004fie.2; human.
DR CTD; 10134; -.
DR GeneCards; GC0XM152965; -.
DR HGNC; HGNC:16695; BCAP31.
DR HPA; CAB015350; -.
DR HPA; CAB015424; -.
DR HPA; HPA003906; -.
DR MIM; 300398; gene.
DR neXtProt; NX_P51572; -.
DR PharmGKB; PA128394569; -.
DR eggNOG; NOG244998; -.
DR HOGENOM; HOG000204790; -.
DR HOVERGEN; HBG050661; -.
DR InParanoid; P51572; -.
DR KO; K14009; -.
DR OMA; HSMRLFR; -.
DR PhylomeDB; P51572; -.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; BCAP31; human.
DR GeneWiki; BCAP31; -.
DR GenomeRNAi; 10134; -.
DR NextBio; 38337; -.
DR PMAP-CutDB; P51572; -.
DR PRO; PR:P51572; -.
DR ArrayExpress; P51572; -.
DR Bgee; P51572; -.
DR CleanEx; HS_BCAP31; -.
DR Genevestigator; P51572; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0005102; F:receptor binding; NAS:UniProtKB.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IMP:UniProtKB.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
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: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:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR008417; Bap31.
DR PANTHER; PTHR12701; PTHR12701; 1.
DR Pfam; PF05529; Bap31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 246 B-cell receptor-associated protein 31.
FT /FTId=PRO_0000142891.
FT TOPO_DOM 2 6 Lumenal (Potential).
FT TRANSMEM 7 27 Helical; (Potential).
FT TOPO_DOM 28 43 Cytoplasmic (Potential).
FT TRANSMEM 44 64 Helical; (Potential).
FT TOPO_DOM 65 102 Lumenal (Potential).
FT TRANSMEM 103 123 Helical; (Potential).
FT TOPO_DOM 124 246 Cytoplasmic (Potential).
FT MOTIF 243 246 Di-lysine motif.
FT SITE 164 165 Cleavage; by caspase-8 (Potential).
FT SITE 238 239 Cleavage; by caspase-8 (Potential).
FT VAR_SEQ 1 1 M -> MGAEASSSWCPGTALPEERLSVKRASEISGFLGQGS
FT SGEAALDVLTHVLEGAGNKLTSSCGKPSSNRM (in
FT isoform 2).
FT /FTId=VSP_043116.
FT MUTAGEN 164 164 D->A: Abolishes cleavage by caspases,
FT inhibits apoptotic membrane blebbing and
FT release of cytochrome c from
FT mitochondria; when associated with A-238.
FT MUTAGEN 238 238 D->A: Abolishes cleavage by caspases,
FT inhibits apoptotic membrane blebbing and
FT release of cytochrome c from
FT mitochondria; when associated with A-164.
FT CONFLICT 2 2 S -> T (in Ref. 3; CAA57415).
FT CONFLICT 72 72 K -> E (in Ref. 7; AAH14323).
FT CONFLICT 208 208 Q -> E (in Ref. 3; CAA57415).
FT HELIX 170 219
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
//
ID BAP31_HUMAN Reviewed; 246 AA.
AC P51572; B3KQ79; D3DWV5; Q13836; Q96CF0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 133.
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, DXS1357E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT Xq28 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
RT antigen 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;
RA Adachi T., Schamel W.W.A., Kim K.-M., Watanabe T., Becker B.,
RA Nielsen P.J., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP BCL2; 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.,
RA Cromlish J.A., 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
RP 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 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
RT complex at the endoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4331-4336(2002).
RN [13]
RP INTERACTION WITH PTPLB.
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
RT identifies BAP31 as a regulator of the turnover of endoplasmic
RT reticulum-associated protein tyrosine phosphatase-like B.";
RL Mol. Cell. Biol. 24:2767-2778(2004).
RN [14]
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)
RT and DXS1357E: a novel neonatal phenotype similar to peroxisomal
RT biogenesis disorders.";
RL Am. J. Hum. Genet. 70:1520-1531(2002).
RN [15]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role in anterograde transport of membrane
CC proteins from the endoplasmic reticulum to the Golgi. May be
CC involved in CASP8-mediated apoptosis.
CC -!- SUBUNIT: Homodimer and heterodimer with BCAP29. Binds CASP8
CC (isoform 9) as a complex containing BCAP31, BCAP29, BCL2 and/or
CC BCL2L1. Interacts with VAMP3, VAMP1 and membrane IgD
CC immunoglobulins. May interact with ACTG1 and non-muscle myosin II.
CC Interacts with PTPLB.
CC -!- INTERACTION:
CC P10415:BCL2; NbExp=2; IntAct=EBI-77683, EBI-77694;
CC Q14790:CASP8; NbExp=3; IntAct=EBI-77683, EBI-78060;
CC P13569:CFTR; NbExp=3; IntAct=EBI-77683, EBI-349854;
CC Q9BUN8:DERL1; NbExp=3; IntAct=EBI-77683, EBI-398977;
CC Q9Y3D6:FIS1; NbExp=8; IntAct=EBI-77683, EBI-3385283;
CC Q6Y1H2:PTPLB; NbExp=4; IntAct=EBI-77683, EBI-530257;
CC P60468:SEC61B; NbExp=7; IntAct=EBI-77683, EBI-1788819;
CC Q15629:TRAM1; NbExp=5; IntAct=EBI-77683, EBI-1788852;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Multi-pass membrane protein. Note=May
CC shuttle between the ER and the intermediate compartment/cis-Golgi
CC complex.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Cleaved by CASP8 and other caspases.
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.
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family.
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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 PIR; S44279; S44279.
DR RefSeq; NP_001132913.1; NM_001139441.1.
DR RefSeq; NP_001132929.1; NM_001139457.2.
DR RefSeq; NP_001243376.1; NM_001256447.1.
DR RefSeq; NP_005736.3; NM_005745.7.
DR UniGene; Hs.522817; -.
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 ProteinModelPortal; P51572; -.
DR IntAct; P51572; 22.
DR MINT; MINT-3018869; -.
DR STRING; 9606.ENSP00000392330; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR PhosphoSite; P51572; -.
DR DMDM; 1705725; -.
DR PaxDb; P51572; -.
DR PRIDE; P51572; -.
DR DNASU; 10134; -.
DR Ensembl; ENST00000345046; ENSP00000343458; ENSG00000185825.
DR Ensembl; ENST00000441714; ENSP00000405417; ENSG00000185825.
DR Ensembl; ENST00000458587; ENSP00000392330; ENSG00000185825.
DR Ensembl; ENST00000596601; ENSP00000473146; ENSG00000267977.
DR Ensembl; ENST00000597329; ENSP00000472030; ENSG00000267977.
DR Ensembl; ENST00000600824; ENSP00000472405; ENSG00000267977.
DR GeneID; 10134; -.
DR KEGG; hsa:10134; -.
DR UCSC; uc004fie.2; human.
DR CTD; 10134; -.
DR GeneCards; GC0XM152965; -.
DR HGNC; HGNC:16695; BCAP31.
DR HPA; CAB015350; -.
DR HPA; CAB015424; -.
DR HPA; HPA003906; -.
DR MIM; 300398; gene.
DR neXtProt; NX_P51572; -.
DR PharmGKB; PA128394569; -.
DR eggNOG; NOG244998; -.
DR HOGENOM; HOG000204790; -.
DR HOVERGEN; HBG050661; -.
DR InParanoid; P51572; -.
DR KO; K14009; -.
DR OMA; HSMRLFR; -.
DR PhylomeDB; P51572; -.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; BCAP31; human.
DR GeneWiki; BCAP31; -.
DR GenomeRNAi; 10134; -.
DR NextBio; 38337; -.
DR PMAP-CutDB; P51572; -.
DR PRO; PR:P51572; -.
DR ArrayExpress; P51572; -.
DR Bgee; P51572; -.
DR CleanEx; HS_BCAP31; -.
DR Genevestigator; P51572; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0005102; F:receptor binding; NAS:UniProtKB.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IMP:UniProtKB.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
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: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:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR008417; Bap31.
DR PANTHER; PTHR12701; PTHR12701; 1.
DR Pfam; PF05529; Bap31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 246 B-cell receptor-associated protein 31.
FT /FTId=PRO_0000142891.
FT TOPO_DOM 2 6 Lumenal (Potential).
FT TRANSMEM 7 27 Helical; (Potential).
FT TOPO_DOM 28 43 Cytoplasmic (Potential).
FT TRANSMEM 44 64 Helical; (Potential).
FT TOPO_DOM 65 102 Lumenal (Potential).
FT TRANSMEM 103 123 Helical; (Potential).
FT TOPO_DOM 124 246 Cytoplasmic (Potential).
FT MOTIF 243 246 Di-lysine motif.
FT SITE 164 165 Cleavage; by caspase-8 (Potential).
FT SITE 238 239 Cleavage; by caspase-8 (Potential).
FT VAR_SEQ 1 1 M -> MGAEASSSWCPGTALPEERLSVKRASEISGFLGQGS
FT SGEAALDVLTHVLEGAGNKLTSSCGKPSSNRM (in
FT isoform 2).
FT /FTId=VSP_043116.
FT MUTAGEN 164 164 D->A: Abolishes cleavage by caspases,
FT inhibits apoptotic membrane blebbing and
FT release of cytochrome c from
FT mitochondria; when associated with A-238.
FT MUTAGEN 238 238 D->A: Abolishes cleavage by caspases,
FT inhibits apoptotic membrane blebbing and
FT release of cytochrome c from
FT mitochondria; when associated with A-164.
FT CONFLICT 2 2 S -> T (in Ref. 3; CAA57415).
FT CONFLICT 72 72 K -> E (in Ref. 7; AAH14323).
FT CONFLICT 208 208 Q -> E (in Ref. 3; CAA57415).
FT HELIX 170 219
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
//
MIM
300398
*RECORD*
*FIELD* NO
300398
*FIELD* TI
*300398 B-CELL RECEPTOR-ASSOCIATED PROTEIN 31; BCAP31
;;BAP31;;
DXS1357E
*FIELD* TX
read more
DESCRIPTION
The BCAP31 gene encodes a chaperone that is highly expressed in the
membrane of the endoplasmic reticulum (ER). It plays a role in the
export of secreted proteins from the ER and the recognition of
abnormally folded proteins that are targeted to the ER-associated
degradation pathway. The protein serves as a cargo receptor for the
export of transmembrane proteins (summary by Cacciagli et al., 2013).
CLONING
By screening a fibroblast cDNA library with a probe used to identify the
ALD gene (ABCD1; 300371), Mosser et al. (1994) obtained a cDNA encoding
BCAP31, which they termed CDM. The deduced 246-amino acid protein
contains a coiled-coil domain and membrane-associated helices and is
weakly similar to the rodlike tail of myosin heavy chains. Northern blot
analysis revealed ubiquitous expression of a 1.5-kb transcript.
By micropeptide sequence analysis and PCR with degenerate primers to
screen mouse myeloma, spleen, and bone marrow cDNA libraries and human
leukemia and B-cell cDNA libraries, Adachi et al. (1996) isolated cDNAs
encoding mouse and human BCAP31. The mouse and human proteins are 95%
identical, and the mouse protein is 43% identical to mouse Bap29.
Western blot analysis showed expression of a 30-kD protein in Burkitt
lymphoma cells. Immunoblot and mutational analysis showed that Bap31
associates with a threonine residue in the transmembrane segment of IgD.
Li et al. (1996) cloned and characterized BCAP31, which they termed 6C6
antigen. Immunohistochemical and Western blot analysis demonstrated
increased expression of the 28-kD protein in breast cancer cells
compared with normal tissue. Li et al. (1996) identified 3 highly
hydrophobic N-terminal sequences and a hydrophilic C-terminal region
containing a possible N-glycosylation site in the protein. Glycosidase
treatment and biochemical analysis indicated, however, that the protein
is not glycosylated. Immunoprecipitation analysis showed that BCAP31 is
a multiple-membrane-spanning protein. Northern blot analysis indicated
higher expression of BCAP31 in breast cancer cells and pancreatic tissue
compared with other tissues and cell lines.
GENE FUNCTION
Using fluorescence microscopy and immunoblot analysis, Lambert et al.
(2001) showed that BCAP31 colocalizes with and controls the expression
of both wildtype cystic fibrosis transmembrane conductance regulator
(CFTR; 602421) and CFTR with a deletion of phe508 (delF508; 602421.0001)
in CHO cells and Xenopus oocytes. Antisense inhibition of BCAP31
increased expression of both CFTR and the delF508 variant. Inhibition
also enhanced chloride conductance and recovered chloride channel
activity in cells expressing the delF508 mutation. Lambert et al. (2001)
proposed that interfering with the expression or function of BCAP31 in
epithelial cells may be a way to circumvent the chloride channel defect
in cystic fibrosis.
MAPPING
By somatic cell hybrid analysis, Mosser et al. (1994) mapped the BCAP31
gene near the ALD gene on chromosome Xq28. The BCAP31 and ALD genes show
a head-to-head organization and are transcribed from the same CpG island
in the opposite direction. By interspecific backcross analysis, Adachi
et al. (1996) mapped the mouse Bap31 gene to the X chromosome.
MOLECULAR GENETICS
In 7 affected males from 3 unrelated families with an X-linked mental
retardation syndrome characterized by deafness, dystonia, and central
hypomyelination (DDCH; 300475), Cacciagli et al. (2013) identified 3
different hemizygous mutations in the BCAP31 gene
(300398.0001-300398.0003). All mutations caused a loss of protein
function. The mutation in the first family was found by X-chromosome
exome analysis, and the other 2 mutations were found by screening the
BCAP31 gene in 29 male probands with severe intellectual disability,
dystonia, and deafness. The patients also had dysmorphic facial
features, failure to thrive, pyramidal signs with quadriplegia,
microcephaly, and hypomyelinating white matter changes on brain imaging.
Four of the 7 died in the first years of life. Patient fibroblasts
showed swollen endoplasmic reticulum lumens and abnormal Golgi
morphology. The cells contained large cytoplasmic vesicles partially
filled with electron-dense inclusions that suggested impaired
ER-to-Golgi exchanges. However, there was not a massive accumulation of
misfolded proteins, abnormal activation of the unfolded protein
response, or apoptosis. The findings linked intracellular protein
trafficking to severe congenital brain dysfunction, including defective
myelination, and deafness.
*FIELD* AV
.0001
DEAFNESS, DYSTONIA, AND CEREBRAL HYPOMYELINATION
BCAP31, IVS3AS, A-G, -2
In 2 brothers with deafness, dystonia, and central hypomyelination
(DDCH; 300475), Cacciagli et al. (2013) identified a hemizygous A-to-G
transition in intron 3 of the BCAP1 gene (c.194-2A-G), resulting in
activation of a cryptic splice site and a transcript predicted to encode
a truncated protein (Ile64fsTer25). The mutation was found by
X-chromosome exome sequencing and was not present in the dbSNP or NHLBI
Exome Variant Server databases. Patient cells showed about 7% mutant
transcript compared to control, suggesting that it is subject to
nonsense-mediated mRNA decay and that there is a lack of protein
expression. A carrier female was not affected.
.0002
DEAFNESS, DYSTONIA, AND CEREBRAL HYPOMYELINATION
BCAP31, 5.3-KB DEL
In 4 affected males from a family with DDCH (300475), Cacciagli et al.
(2013) identified a hemizygous 5.3-kb deletion resulting in the loss of
exon 8 of the BCAP31 gene and the loss of 248 bp of the 3-prime
untranslated region of the neighboring SLC6A8 gene (300036). Patient
fibroblasts showed a 54% reduction in SLC6A8 mRNA, but magnetic
resonance spectroscopy of 1 patient showed normal creatine peaks.
Cacciagli et al. (2013) noted that individuals with the deletion may
have expression of a different SLC6A8 transcript, and concluded that
SLC6A8 is not involved in the phenotype of this family. Carrier females
were not affected.
.0003
DEAFNESS, DYSTONIA, AND CEREBRAL HYPOMYELINATION
BCAP32, GLN33TER
In a boy with DDCH (300475), Cacciagli et al. (2013) identified a
hemizygous c.97C-T transition in exon 3 of the BCAP31 gene, resulting in
a gln33-to-ter (Q33X) substitution. Carrier females were not affected.
*FIELD* RF
1. Adachi, T.; Schamel, W. W. A.; Kim, K.-M.; Watanabe, T.; Becker,
B.; Nielsen, P. J.; Reth, M.: The specificity of association of the
IgD molecule with the accessory proteins BAP31/BAP29 lies in the IgD
transmembrane sequence. EMBO J. 15: 1534-1541, 1996.
2. Cacciagli, P.; Sutera-Sardo, J.; Borges-Correia, A.; Roux, J.-C.;
Dorboz, I.; Desvignes, J.-P.; Badens, C.; Delepine, M.; Lathrop, M.;
Cau, P.; Levy, N.; Girard, N.; Sarda, P.; Boespflug-Tanguy, O.; Villard,
L.: Mutations in BCAP31 cause a severe X-linked phenotype with deafness,
dystonia, and central hypomyelination and disorganize the Golgi apparatus. Am.
J. Hum. Genet. 93: 579-586, 2013.
3. Lambert, G.; Becker, B.; Schreiber, R.; Boucherot, A.; Reth, M.;
Kunzelmann, K.: Control of cystic fibrosis transmembrane conductance
regulator expression by BAP31. J. Biol. Chem. 276: 20340-20345,
2001.
4. Li, E.; Bestagno, M.; Burrone, O.: Molecular cloning and characterization
of a transmembrane surface antigen in human cells. Europ. J. Biochem. 238:
631-638, 1996.
5. Mosser, J.; Sarde, C.-O.; Vicaire, S.; Yates, J. R. W.; Mandel,
J.-L.: A new human gene (DXS1357E) with ubiquitous expression, located
in Xq28 adjacent to the adrenoleukodystrophy gene. Genomics 22:
469-471, 1994.
*FIELD* CN
Cassandra L. Kniffin - updated: 10/15/2013
Victor A. McKusick - updated: 6/11/2002
*FIELD* CD
Paul J. Converse: 6/7/2002
*FIELD* ED
carol: 10/18/2013
ckniffin: 10/15/2013
carol: 3/4/2004
carol: 2/3/2004
terry: 6/11/2002
mgross: 6/7/2002
*RECORD*
*FIELD* NO
300398
*FIELD* TI
*300398 B-CELL RECEPTOR-ASSOCIATED PROTEIN 31; BCAP31
;;BAP31;;
DXS1357E
*FIELD* TX
read more
DESCRIPTION
The BCAP31 gene encodes a chaperone that is highly expressed in the
membrane of the endoplasmic reticulum (ER). It plays a role in the
export of secreted proteins from the ER and the recognition of
abnormally folded proteins that are targeted to the ER-associated
degradation pathway. The protein serves as a cargo receptor for the
export of transmembrane proteins (summary by Cacciagli et al., 2013).
CLONING
By screening a fibroblast cDNA library with a probe used to identify the
ALD gene (ABCD1; 300371), Mosser et al. (1994) obtained a cDNA encoding
BCAP31, which they termed CDM. The deduced 246-amino acid protein
contains a coiled-coil domain and membrane-associated helices and is
weakly similar to the rodlike tail of myosin heavy chains. Northern blot
analysis revealed ubiquitous expression of a 1.5-kb transcript.
By micropeptide sequence analysis and PCR with degenerate primers to
screen mouse myeloma, spleen, and bone marrow cDNA libraries and human
leukemia and B-cell cDNA libraries, Adachi et al. (1996) isolated cDNAs
encoding mouse and human BCAP31. The mouse and human proteins are 95%
identical, and the mouse protein is 43% identical to mouse Bap29.
Western blot analysis showed expression of a 30-kD protein in Burkitt
lymphoma cells. Immunoblot and mutational analysis showed that Bap31
associates with a threonine residue in the transmembrane segment of IgD.
Li et al. (1996) cloned and characterized BCAP31, which they termed 6C6
antigen. Immunohistochemical and Western blot analysis demonstrated
increased expression of the 28-kD protein in breast cancer cells
compared with normal tissue. Li et al. (1996) identified 3 highly
hydrophobic N-terminal sequences and a hydrophilic C-terminal region
containing a possible N-glycosylation site in the protein. Glycosidase
treatment and biochemical analysis indicated, however, that the protein
is not glycosylated. Immunoprecipitation analysis showed that BCAP31 is
a multiple-membrane-spanning protein. Northern blot analysis indicated
higher expression of BCAP31 in breast cancer cells and pancreatic tissue
compared with other tissues and cell lines.
GENE FUNCTION
Using fluorescence microscopy and immunoblot analysis, Lambert et al.
(2001) showed that BCAP31 colocalizes with and controls the expression
of both wildtype cystic fibrosis transmembrane conductance regulator
(CFTR; 602421) and CFTR with a deletion of phe508 (delF508; 602421.0001)
in CHO cells and Xenopus oocytes. Antisense inhibition of BCAP31
increased expression of both CFTR and the delF508 variant. Inhibition
also enhanced chloride conductance and recovered chloride channel
activity in cells expressing the delF508 mutation. Lambert et al. (2001)
proposed that interfering with the expression or function of BCAP31 in
epithelial cells may be a way to circumvent the chloride channel defect
in cystic fibrosis.
MAPPING
By somatic cell hybrid analysis, Mosser et al. (1994) mapped the BCAP31
gene near the ALD gene on chromosome Xq28. The BCAP31 and ALD genes show
a head-to-head organization and are transcribed from the same CpG island
in the opposite direction. By interspecific backcross analysis, Adachi
et al. (1996) mapped the mouse Bap31 gene to the X chromosome.
MOLECULAR GENETICS
In 7 affected males from 3 unrelated families with an X-linked mental
retardation syndrome characterized by deafness, dystonia, and central
hypomyelination (DDCH; 300475), Cacciagli et al. (2013) identified 3
different hemizygous mutations in the BCAP31 gene
(300398.0001-300398.0003). All mutations caused a loss of protein
function. The mutation in the first family was found by X-chromosome
exome analysis, and the other 2 mutations were found by screening the
BCAP31 gene in 29 male probands with severe intellectual disability,
dystonia, and deafness. The patients also had dysmorphic facial
features, failure to thrive, pyramidal signs with quadriplegia,
microcephaly, and hypomyelinating white matter changes on brain imaging.
Four of the 7 died in the first years of life. Patient fibroblasts
showed swollen endoplasmic reticulum lumens and abnormal Golgi
morphology. The cells contained large cytoplasmic vesicles partially
filled with electron-dense inclusions that suggested impaired
ER-to-Golgi exchanges. However, there was not a massive accumulation of
misfolded proteins, abnormal activation of the unfolded protein
response, or apoptosis. The findings linked intracellular protein
trafficking to severe congenital brain dysfunction, including defective
myelination, and deafness.
*FIELD* AV
.0001
DEAFNESS, DYSTONIA, AND CEREBRAL HYPOMYELINATION
BCAP31, IVS3AS, A-G, -2
In 2 brothers with deafness, dystonia, and central hypomyelination
(DDCH; 300475), Cacciagli et al. (2013) identified a hemizygous A-to-G
transition in intron 3 of the BCAP1 gene (c.194-2A-G), resulting in
activation of a cryptic splice site and a transcript predicted to encode
a truncated protein (Ile64fsTer25). The mutation was found by
X-chromosome exome sequencing and was not present in the dbSNP or NHLBI
Exome Variant Server databases. Patient cells showed about 7% mutant
transcript compared to control, suggesting that it is subject to
nonsense-mediated mRNA decay and that there is a lack of protein
expression. A carrier female was not affected.
.0002
DEAFNESS, DYSTONIA, AND CEREBRAL HYPOMYELINATION
BCAP31, 5.3-KB DEL
In 4 affected males from a family with DDCH (300475), Cacciagli et al.
(2013) identified a hemizygous 5.3-kb deletion resulting in the loss of
exon 8 of the BCAP31 gene and the loss of 248 bp of the 3-prime
untranslated region of the neighboring SLC6A8 gene (300036). Patient
fibroblasts showed a 54% reduction in SLC6A8 mRNA, but magnetic
resonance spectroscopy of 1 patient showed normal creatine peaks.
Cacciagli et al. (2013) noted that individuals with the deletion may
have expression of a different SLC6A8 transcript, and concluded that
SLC6A8 is not involved in the phenotype of this family. Carrier females
were not affected.
.0003
DEAFNESS, DYSTONIA, AND CEREBRAL HYPOMYELINATION
BCAP32, GLN33TER
In a boy with DDCH (300475), Cacciagli et al. (2013) identified a
hemizygous c.97C-T transition in exon 3 of the BCAP31 gene, resulting in
a gln33-to-ter (Q33X) substitution. Carrier females were not affected.
*FIELD* RF
1. Adachi, T.; Schamel, W. W. A.; Kim, K.-M.; Watanabe, T.; Becker,
B.; Nielsen, P. J.; Reth, M.: The specificity of association of the
IgD molecule with the accessory proteins BAP31/BAP29 lies in the IgD
transmembrane sequence. EMBO J. 15: 1534-1541, 1996.
2. Cacciagli, P.; Sutera-Sardo, J.; Borges-Correia, A.; Roux, J.-C.;
Dorboz, I.; Desvignes, J.-P.; Badens, C.; Delepine, M.; Lathrop, M.;
Cau, P.; Levy, N.; Girard, N.; Sarda, P.; Boespflug-Tanguy, O.; Villard,
L.: Mutations in BCAP31 cause a severe X-linked phenotype with deafness,
dystonia, and central hypomyelination and disorganize the Golgi apparatus. Am.
J. Hum. Genet. 93: 579-586, 2013.
3. Lambert, G.; Becker, B.; Schreiber, R.; Boucherot, A.; Reth, M.;
Kunzelmann, K.: Control of cystic fibrosis transmembrane conductance
regulator expression by BAP31. J. Biol. Chem. 276: 20340-20345,
2001.
4. Li, E.; Bestagno, M.; Burrone, O.: Molecular cloning and characterization
of a transmembrane surface antigen in human cells. Europ. J. Biochem. 238:
631-638, 1996.
5. Mosser, J.; Sarde, C.-O.; Vicaire, S.; Yates, J. R. W.; Mandel,
J.-L.: A new human gene (DXS1357E) with ubiquitous expression, located
in Xq28 adjacent to the adrenoleukodystrophy gene. Genomics 22:
469-471, 1994.
*FIELD* CN
Cassandra L. Kniffin - updated: 10/15/2013
Victor A. McKusick - updated: 6/11/2002
*FIELD* CD
Paul J. Converse: 6/7/2002
*FIELD* ED
carol: 10/18/2013
ckniffin: 10/15/2013
carol: 3/4/2004
carol: 2/3/2004
terry: 6/11/2002
mgross: 6/7/2002