BAP29_HUMAN
ID BAP29_HUMAN Reviewed; 241 AA.
AC Q9UHQ4; G5E9L4; O95003;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=B-cell receptor-associated protein 29;
DE Short=BCR-associated protein 29;
DE Short=Bap29;
GN Name=BCAP29; Synonyms=BAP29;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 168-229, SUBUNIT, AND COILED
RP COIL.
RX PubMed=25327138; DOI=10.1039/c4cc07326f;
RA Quistgaard E.M.;
RT "A disulfide polymerized protein crystal.";
RL Chem. Commun. (Camb.) 50:14995-14997(2014).
CC -!- FUNCTION: May play a role in anterograde transport of membrane proteins
CC from the endoplasmic reticulum to the Golgi. May be involved in CASP8-
CC mediated apoptosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (PubMed:25327138). Heterodimer with BCAP31. Binds
CC CASP8 (isoform 9) as a complex containing BCAP31, BCAP29, BCL2 and/or
CC BCL2L1. Interacts with VAMP3, VAMP1 and membrane IgD immunoglobulins.
CC May interact with ACTG1 and non-muscle myosin II (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:25327138}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHQ4-2; Sequence=VSP_047096;
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family. {ECO:0000305}.
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DR EMBL; AF126020; AAF17230.1; -; mRNA.
DR EMBL; BT006981; AAP35627.1; -; mRNA.
DR EMBL; AC004839; AAC83971.1; -; Genomic_DNA.
DR EMBL; AC078937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471070; EAW83408.1; -; Genomic_DNA.
DR EMBL; BC008478; AAH08478.1; -; mRNA.
DR CCDS; CCDS34730.1; -. [Q9UHQ4-2]
DR CCDS; CCDS34731.1; -. [Q9UHQ4-1]
DR RefSeq; NP_001008405.1; NM_001008405.2. [Q9UHQ4-2]
DR RefSeq; NP_061332.2; NM_018844.3. [Q9UHQ4-1]
DR RefSeq; XP_006716114.1; XM_006716051.2.
DR RefSeq; XP_011514708.1; XM_011516406.2.
DR PDB; 4W7Y; X-ray; 2.50 A; A/B=168-229.
DR PDB; 4W7Z; X-ray; 2.20 A; A/B/C/D=168-229.
DR PDB; 4W80; X-ray; 3.20 A; A/B/C/D=168-229.
DR PDBsum; 4W7Y; -.
DR PDBsum; 4W7Z; -.
DR PDBsum; 4W80; -.
DR AlphaFoldDB; Q9UHQ4; -.
DR SMR; Q9UHQ4; -.
DR BioGRID; 121019; 60.
DR IntAct; Q9UHQ4; 10.
DR MINT; Q9UHQ4; -.
DR STRING; 9606.ENSP00000368414; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; Q9UHQ4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHQ4; -.
DR MetOSite; Q9UHQ4; -.
DR PhosphoSitePlus; Q9UHQ4; -.
DR SwissPalm; Q9UHQ4; -.
DR BioMuta; BCAP29; -.
DR DMDM; 25008167; -.
DR EPD; Q9UHQ4; -.
DR jPOST; Q9UHQ4; -.
DR MassIVE; Q9UHQ4; -.
DR MaxQB; Q9UHQ4; -.
DR PaxDb; Q9UHQ4; -.
DR PeptideAtlas; Q9UHQ4; -.
DR PRIDE; Q9UHQ4; -.
DR ProteomicsDB; 33975; -.
DR ProteomicsDB; 84399; -. [Q9UHQ4-1]
DR Antibodypedia; 17207; 297 antibodies from 32 providers.
DR Antibodypedia; 81585; 1 antibodies from 1 providers.
DR DNASU; 55973; -.
DR Ensembl; ENST00000005259.9; ENSP00000005259.4; ENSG00000075790.12. [Q9UHQ4-1]
DR Ensembl; ENST00000379117.6; ENSP00000368412.2; ENSG00000075790.12. [Q9UHQ4-1]
DR Ensembl; ENST00000445771.6; ENSP00000400718.2; ENSG00000075790.12. [Q9UHQ4-2]
DR Ensembl; ENST00000640518.4; ENSP00000491801.4; ENSG00000283852.4. [Q9UHQ4-1]
DR Ensembl; ENST00000640915.4; ENSP00000490977.4; ENSG00000283852.4. [Q9UHQ4-1]
DR GeneID; 55973; -.
DR KEGG; hsa:55973; -.
DR MANE-Select; ENST00000005259.9; ENSP00000005259.4; NM_018844.4; NP_061332.2.
DR UCSC; uc003vej.3; human. [Q9UHQ4-1]
DR CTD; 55973; -.
DR DisGeNET; 55973; -.
DR GeneCards; BCAP29; -.
DR HGNC; HGNC:24131; BCAP29.
DR HPA; ENSG00000075790; Low tissue specificity.
DR HPA; ENSG00000288558; Low tissue specificity.
DR MIM; 619612; gene.
DR neXtProt; NX_Q9UHQ4; -.
DR OpenTargets; ENSG00000075790; -.
DR PharmGKB; PA134939094; -.
DR VEuPathDB; HostDB:ENSG00000075790; -.
DR VEuPathDB; HostDB:ENSG00000288558; -.
DR eggNOG; KOG1962; Eukaryota.
DR GeneTree; ENSGT00390000011863; -.
DR GeneTree; ENSGT00550000074907; -.
DR InParanoid; Q9UHQ4; -.
DR PhylomeDB; Q9UHQ4; -.
DR TreeFam; TF315310; -.
DR PathwayCommons; Q9UHQ4; -.
DR SignaLink; Q9UHQ4; -.
DR BioGRID-ORCS; 55973; 50 hits in 1046 CRISPR screens.
DR ChiTaRS; BCAP29; human.
DR GeneWiki; BCAP29; -.
DR GenomeRNAi; 55973; -.
DR Pharos; Q9UHQ4; Tbio.
DR PRO; PR:Q9UHQ4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UHQ4; protein.
DR Bgee; ENSG00000075790; Expressed in calcaneal tendon and 96 other tissues.
DR ExpressionAtlas; Q9UHQ4; baseline and differential.
DR Genevisible; Q9UHQ4; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
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;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..241
FT /note="B-cell receptor-associated protein 29"
FT /id="PRO_0000142888"
FT TOPO_DOM 1..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..103
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 198..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 166..233
FT /evidence="ECO:0000269|PubMed:25327138"
FT MOTIF 238..241
FT /note="Di-lysine motif"
FT VAR_SEQ 231..241
FT /note="DRLERGNKKRL -> HSSFGEFLSKRSHKNGSIGKQTGSRKGSFRKRQQEKT
FT VNFIKDTCNILCQNDNFVMLASRKFKFRKMHYDRFVIFLMPHIGCIVMALSKYLMMFQI
FT YCKVCIPALKKNISMLNTIFTY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047096"
FT CONFLICT 25
FT /note="P -> L (in Ref. 1; AAF17230)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..106
FT /note="YI -> SIL (in Ref. 1; AAF17230)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="L -> R (in Ref. 1; AAF17230)"
FT /evidence="ECO:0000305"
FT HELIX 168..225
FT /evidence="ECO:0007829|PDB:4W7Z"
SQ SEQUENCE 241 AA; 28320 MW; 964C39A53E072274 CRC64;
MTLQWAAVAT FLYAEIGLIL IFCLPFIPPQ RWQKIFSFNV WGKIATFWNK AFLTIIILLI
VLFLDAVREV RKYSSVHTIE KSSTSRPDAY EHTQMKLFRS QRNLYISGFS LFFWLVLRRL
VTLITQLAKE LSNKGVLKTQ AENTNKAAKK FMEENEKLKR ILKSHGKDEE CVLEAENKKL
VEDQEKLKTE LRKTSDALSK AQNDVMEMKM QSERLSKEYD QLLKEHSELQ DRLERGNKKR
L
