CD79A_HUMAN
ID CD79A_HUMAN Reviewed; 226 AA.
AC P11912; A0N775; Q53FB8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=B-cell antigen receptor complex-associated protein alpha chain;
DE AltName: Full=Ig-alpha;
DE AltName: Full=MB-1 membrane glycoprotein;
DE AltName: Full=Membrane-bound immunoglobulin-associated protein;
DE AltName: Full=Surface IgM-associated protein;
DE AltName: CD_antigen=CD79a;
DE Flags: Precursor;
GN Name=CD79A; Synonyms=IGA, MB1;
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=1395095; DOI=10.1111/j.1365-2249.1992.tb05846.x;
RA Leduc I., Preud'Homme J.L., Cogne M.;
RT "Structure and expression of the mb-1 transcript in human lymphoid cells.";
RL Clin. Exp. Immunol. 90:141-146(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Tonsil;
RX PubMed=1534761; DOI=10.1002/eji.1830220641;
RA Mueller B.S., Cooper L., Terhorst C.;
RT "Cloning and sequencing of the cDNA encoding the human homologue of the
RT murine immunoglobulin-associated protein B29.";
RL Eur. J. Immunol. 22:1621-1625(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1639443; DOI=10.1007/bf00215058;
RA Flaswinkel H., Reth M.;
RT "Molecular cloning of the Ig-alpha subunit of the human B-cell antigen
RT receptor complex.";
RL Immunogenetics 36:266-269(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1729378;
RA Yu L.M., Chang T.W.;
RT "Human mb-1 gene: complete cDNA sequence and its expression in B cells
RT bearing membrane Ig of various isotypes.";
RL J. Immunol. 148:633-637(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=1538135;
RA Ha H.J., Kubagawa H., Burrows P.D.;
RT "Molecular cloning and expression pattern of a human gene homologous to the
RT murine mb-1 gene.";
RL J. Immunol. 148:1526-1531(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7916003; DOI=10.1007/bf00189974;
RA Hashimoto S., Mohrenweiser H.W., Gregersen P.K., Chiorazzi N.;
RT "Chromosomal localization, genomic structure, and allelic polymorphism of
RT the human CD79 alpha (Ig-alpha/mb-1) gene.";
RL Immunogenetics 40:287-295(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8207205;
RA Ha H., Barnoski B.L., Sun L., Emanuel B.S., Burrows P.D.;
RT "Structure, chromosomal localization, and methylation pattern of the human
RT mb-1 gene.";
RL J. Immunol. 152:5749-5757(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7643857; DOI=10.1016/0161-5890(95)00023-8;
RA Hashimoto S., Chiorazzi N., Gregersen P.K.;
RT "Alternative splicing of CD79a (Ig-alpha/mb-1) and CD79b (Ig-beta/B29) RNA
RT transcripts in human B cells.";
RL Mol. Immunol. 32:651-659(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Koyama M., Nakamura T.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PROTEIN SEQUENCE OF 33-52.
RX PubMed=7514267; DOI=10.1016/0161-5890(94)90061-2;
RA Vasile S., Coligan J.E., Yoshida M., Seon B.K.;
RT "Isolation and chemical characterization of the human B29 and mb-1 proteins
RT of the B cell antigen receptor complex.";
RL Mol. Immunol. 31:419-427(1994).
RN [12]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 190-226 (ISOFORM 1).
RX PubMed=2463161; DOI=10.1002/j.1460-2075.1988.tb03220.x;
RA Sakaguchi N., Kashiwamura S., Kimoto M., Thalmann P., Melchers F.;
RT "B lymphocyte lineage-restricted expression of mb-1, a gene with CD3-like
RT structural properties.";
RL EMBO J. 7:3457-3464(1988).
RN [13]
RP FUNCTION.
RX PubMed=8617796; DOI=10.1074/jbc.271.9.5158;
RA Luisiri P., Lee Y.J., Eisfelder B.J., Clark M.R.;
RT "Cooperativity and segregation of function within the Ig-alpha/beta
RT heterodimer of the B cell antigen receptor complex.";
RL J. Biol. Chem. 271:5158-5163(1996).
RN [14]
RP FUNCTION.
RX PubMed=9057631;
RA Tseng J., Eisfelder B.J., Clark M.R.;
RT "B-cell antigen receptor-induced apoptosis requires both Ig alpha and Ig
RT beta.";
RL Blood 89:1513-1520(1997).
RN [15]
RP INVOLVEMENT IN AGM3.
RX PubMed=10525050; DOI=10.1172/jci7696;
RA Minegishi Y., Coustan-Smith E., Rapalus L., Ersoy F., Campana D.,
RA Conley M.E.;
RT "Mutations in Igalpha (CD79a) result in a complete block in B-cell
RT development.";
RL J. Clin. Invest. 104:1115-1121(1999).
RN [16]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-197; SER-203 AND THR-209.
RX PubMed=10900006; DOI=10.1073/pnas.97.15.8451;
RA Mueller R., Wienands J., Reth M.;
RT "The serine and threonine residues in the Ig-alpha cytoplasmic tail
RT negatively regulate immunoreceptor tyrosine-based activation motif-mediated
RT signal transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8451-8454(2000).
RN [17]
RP INVOLVEMENT IN AGM3.
RX PubMed=11920841; DOI=10.1002/ajmg.10296;
RA Wang Y., Kanegane H., Sanal O., Tezcan I., Ersoy F., Futatani T.,
RA Miyawaki T.;
RT "Novel Igalpha (CD79a) gene mutation in a Turkish patient with B cell-
RT deficient agammaglobulinemia.";
RL Am. J. Med. Genet. 108:333-336(2002).
RN [18]
RP STRUCTURE BY NMR OF 184-195, PHOSPHORYLATION, AND INTERACTION WITH LYN.
RX PubMed=10748115; DOI=10.1074/jbc.m909044199;
RA Gaul B.S., Harrison M.L., Geahlen R.L., Burton R.A., Post C.B.;
RT "Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of
RT the immunoreceptor tyrosine-based activation motif signaling region of the
RT B cell antigen receptor.";
RL J. Biol. Chem. 275:16174-16182(2000).
CC -!- FUNCTION: Required in cooperation with CD79B for initiation of the
CC signal transduction cascade activated by binding of antigen to the B-
CC cell antigen receptor complex (BCR) which leads to internalization of
CC the complex, trafficking to late endosomes and antigen presentation.
CC Also required for BCR surface expression and for efficient
CC differentiation of pro- and pre-B-cells. Stimulates SYK
CC autophosphorylation and activation. Binds to BLNK, bringing BLNK into
CC proximity with SYK and allowing SYK to phosphorylate BLNK. Also
CC interacts with and increases activity of some Src-family tyrosine
CC kinases. Represses BCR signaling during development of immature B-
CC cells. {ECO:0000269|PubMed:8617796, ECO:0000269|PubMed:9057631}.
CC -!- SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked. Part
CC of the B-cell antigen receptor complex where the alpha/beta chain
CC heterodimer is non-covalently associated with an antigen-specific
CC membrane-bound surface immunoglobulin of two heavy chains and two light
CC chains. Interacts through its phosphorylated ITAM domain with the SH2
CC domains of SYK which stimulates SYK autophosphorylation and activation.
CC Also interacts, when phosphorylated on Tyr-210, with the SH2 domain of
CC BLNK/SLP65, bringing BLNK into proximity with SYK and allowing SYK to
CC phosphorylate BLNK which is necessary for trafficking of the BCR to
CC late endosomes. Interacts with Src-family tyrosine kinases including
CC FYN and LYN, increasing their activity (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P11912; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-7797864, EBI-10827839;
CC P11912; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-7797864, EBI-11522760;
CC P11912; Q5BKT4: ALG10; NbExp=3; IntAct=EBI-7797864, EBI-13064220;
CC P11912; Q5I7T1: ALG10B; NbExp=3; IntAct=EBI-7797864, EBI-18075734;
CC P11912; Q92685: ALG3; NbExp=3; IntAct=EBI-7797864, EBI-2848814;
CC P11912; P05090: APOD; NbExp=3; IntAct=EBI-7797864, EBI-715495;
CC P11912; P29972: AQP1; NbExp=3; IntAct=EBI-7797864, EBI-745213;
CC P11912; Q92482: AQP3; NbExp=3; IntAct=EBI-7797864, EBI-2808854;
CC P11912; P27449: ATP6V0C; NbExp=3; IntAct=EBI-7797864, EBI-721179;
CC P11912; Q92843: BCL2L2; NbExp=3; IntAct=EBI-7797864, EBI-707714;
CC P11912; O15155: BET1; NbExp=3; IntAct=EBI-7797864, EBI-749204;
CC P11912; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-7797864, EBI-12244618;
CC P11912; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-7797864, EBI-8648738;
CC P11912; O14523: C2CD2L; NbExp=3; IntAct=EBI-7797864, EBI-12822627;
CC P11912; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-7797864, EBI-12003442;
CC P11912; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-7797864, EBI-9083477;
CC P11912; O14735: CDIPT; NbExp=3; IntAct=EBI-7797864, EBI-358858;
CC P11912; O95832: CLDN1; NbExp=3; IntAct=EBI-7797864, EBI-723889;
CC P11912; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-7797864, EBI-6165897;
CC P11912; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-7797864, EBI-11522780;
CC P11912; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-7797864, EBI-2807956;
CC P11912; O95406: CNIH1; NbExp=3; IntAct=EBI-7797864, EBI-12172273;
CC P11912; Q8TBE1: CNIH3; NbExp=3; IntAct=EBI-7797864, EBI-12208021;
CC P11912; P29400-2: COL4A5; NbExp=3; IntAct=EBI-7797864, EBI-12211159;
CC P11912; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-7797864, EBI-12019274;
CC P11912; P49447: CYB561; NbExp=3; IntAct=EBI-7797864, EBI-8646596;
CC P11912; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-7797864, EBI-10269179;
CC P11912; O14569: CYB561D2; NbExp=3; IntAct=EBI-7797864, EBI-717654;
CC P11912; O43169: CYB5B; NbExp=3; IntAct=EBI-7797864, EBI-1058710;
CC P11912; Q9H1M4: DEFB127; NbExp=3; IntAct=EBI-7797864, EBI-10305240;
CC P11912; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-7797864, EBI-8645574;
CC P11912; P56851: EDDM3B; NbExp=3; IntAct=EBI-7797864, EBI-10215665;
CC P11912; Q9BV81: EMC6; NbExp=3; IntAct=EBI-7797864, EBI-2820492;
CC P11912; P54849: EMP1; NbExp=3; IntAct=EBI-7797864, EBI-4319440;
CC P11912; P54852: EMP3; NbExp=3; IntAct=EBI-7797864, EBI-3907816;
CC P11912; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-7797864, EBI-11337888;
CC P11912; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-7797864, EBI-12118888;
CC P11912; Q969F0: FATE1; NbExp=6; IntAct=EBI-7797864, EBI-743099;
CC P11912; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-7797864, EBI-12142299;
CC P11912; P37268: FDFT1; NbExp=3; IntAct=EBI-7797864, EBI-714550;
CC P11912; O14843: FFAR3; NbExp=3; IntAct=EBI-7797864, EBI-17762181;
CC P11912; Q14318: FKBP8; NbExp=3; IntAct=EBI-7797864, EBI-724839;
CC P11912; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-7797864, EBI-714482;
CC P11912; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-7797864, EBI-12175685;
CC P11912; Q8N3T1: GALNT15; NbExp=3; IntAct=EBI-7797864, EBI-3925203;
CC P11912; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-7797864, EBI-11991950;
CC P11912; P08034: GJB1; NbExp=3; IntAct=EBI-7797864, EBI-17565645;
CC P11912; O15529: GPR42; NbExp=3; IntAct=EBI-7797864, EBI-18076404;
CC P11912; Q5VWC8: HACD4; NbExp=3; IntAct=EBI-7797864, EBI-18076069;
CC P11912; P09601: HMOX1; NbExp=3; IntAct=EBI-7797864, EBI-2806151;
CC P11912; P30519: HMOX2; NbExp=3; IntAct=EBI-7797864, EBI-712096;
CC P11912; P46695: IER3; NbExp=3; IntAct=EBI-7797864, EBI-1748945;
CC P11912; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-7797864, EBI-8503746;
CC P11912; P11215: ITGAM; NbExp=3; IntAct=EBI-7797864, EBI-2568251;
CC P11912; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-7797864, EBI-10266796;
CC P11912; P07942: LAMB1; NbExp=3; IntAct=EBI-7797864, EBI-949174;
CC P11912; O95214: LEPROTL1; NbExp=3; IntAct=EBI-7797864, EBI-750776;
CC P11912; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-7797864, EBI-2820517;
CC P11912; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-7797864, EBI-12033434;
CC P11912; Q16873: LTC4S; NbExp=3; IntAct=EBI-7797864, EBI-12241118;
CC P11912; Q13021: MALL; NbExp=3; IntAct=EBI-7797864, EBI-750078;
CC P11912; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-7797864, EBI-10317612;
CC P11912; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-7797864, EBI-11956541;
CC P11912; Q6NUT3-2: MFSD12; NbExp=3; IntAct=EBI-7797864, EBI-17295698;
CC P11912; Q6N075: MFSD5; NbExp=3; IntAct=EBI-7797864, EBI-3920969;
CC P11912; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-7797864, EBI-2858252;
CC P11912; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-7797864, EBI-12866138;
CC P11912; Q8IY49-2: MMD2; NbExp=3; IntAct=EBI-7797864, EBI-13349813;
CC P11912; O75425: MOSPD3; NbExp=3; IntAct=EBI-7797864, EBI-12179105;
CC P11912; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-7797864, EBI-12070086;
CC P11912; Q96S97: MYADM; NbExp=3; IntAct=EBI-7797864, EBI-13301517;
CC P11912; A6NDP7: MYADML2; NbExp=3; IntAct=EBI-7797864, EBI-17641390;
CC P11912; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-7797864, EBI-2863634;
CC P11912; Q99519: NEU1; NbExp=3; IntAct=EBI-7797864, EBI-721517;
CC P11912; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-7797864, EBI-10317425;
CC P11912; Q6P499: NIPAL3; NbExp=3; IntAct=EBI-7797864, EBI-10252783;
CC P11912; Q16617: NKG7; NbExp=3; IntAct=EBI-7797864, EBI-3919611;
CC P11912; Q8N912: NRAC; NbExp=3; IntAct=EBI-7797864, EBI-12051377;
CC P11912; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-7797864, EBI-11075081;
CC P11912; Q7RTS6: OTOP2; NbExp=3; IntAct=EBI-7797864, EBI-7642372;
CC P11912; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-7797864, EBI-12092917;
CC P11912; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-7797864, EBI-12257782;
CC P11912; Q04941: PLP2; NbExp=3; IntAct=EBI-7797864, EBI-608347;
CC P11912; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-7797864, EBI-11721828;
CC P11912; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-7797864, EBI-12955265;
CC P11912; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-7797864, EBI-8652812;
CC P11912; Q59EV6: PPGB; NbExp=3; IntAct=EBI-7797864, EBI-14210385;
CC P11912; O60831: PRAF2; NbExp=3; IntAct=EBI-7797864, EBI-2506064;
CC P11912; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-7797864, EBI-14199621;
CC P11912; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-7797864, EBI-14065960;
CC P11912; P08100: RHO; NbExp=3; IntAct=EBI-7797864, EBI-1394177;
CC P11912; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-7797864, EBI-10244780;
CC P11912; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-7797864, EBI-3917235;
CC P11912; O75396: SEC22B; NbExp=3; IntAct=EBI-7797864, EBI-1058865;
CC P11912; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-7797864, EBI-10329948;
CC P11912; P11686: SFTPC; NbExp=3; IntAct=EBI-7797864, EBI-10197617;
CC P11912; Q9UKG4: SLC13A4; NbExp=6; IntAct=EBI-7797864, EBI-12808018;
CC P11912; Q86YT5: SLC13A5; NbExp=3; IntAct=EBI-7797864, EBI-12002412;
CC P11912; Q6ZSM3: SLC16A12; NbExp=3; IntAct=EBI-7797864, EBI-17460560;
CC P11912; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-7797864, EBI-12243266;
CC P11912; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-7797864, EBI-8644112;
CC P11912; P78383: SLC35B1; NbExp=3; IntAct=EBI-7797864, EBI-12147661;
CC P11912; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-7797864, EBI-10281213;
CC P11912; Q9H2H9: SLC38A1; NbExp=6; IntAct=EBI-7797864, EBI-9978441;
CC P11912; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-7797864, EBI-12898013;
CC P11912; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-7797864, EBI-2823239;
CC P11912; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-7797864, EBI-12266234;
CC P11912; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-7797864, EBI-10290130;
CC P11912; Q7Z3Q1-2: SLC46A3; NbExp=3; IntAct=EBI-7797864, EBI-18074862;
CC P11912; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-7797864, EBI-3907610;
CC P11912; P48065: SLC6A12; NbExp=3; IntAct=EBI-7797864, EBI-3843589;
CC P11912; P30825: SLC7A1; NbExp=3; IntAct=EBI-7797864, EBI-4289564;
CC P11912; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-7797864, EBI-8640191;
CC P11912; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-7797864, EBI-741850;
CC P11912; P0DN84: STRIT1; NbExp=3; IntAct=EBI-7797864, EBI-12200293;
CC P11912; Q86Y82: STX12; NbExp=3; IntAct=EBI-7797864, EBI-2691717;
CC P11912; Q13277: STX3; NbExp=3; IntAct=EBI-7797864, EBI-1394295;
CC P11912; Q9UNK0: STX8; NbExp=3; IntAct=EBI-7797864, EBI-727240;
CC P11912; P57105: SYNJ2BP; NbExp=3; IntAct=EBI-7797864, EBI-1049004;
CC P11912; Q9NZ01: TECR; NbExp=3; IntAct=EBI-7797864, EBI-2877718;
CC P11912; P07204: THBD; NbExp=3; IntAct=EBI-7797864, EBI-941422;
CC P11912; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-7797864, EBI-6448756;
CC P11912; P48230: TM4SF4; NbExp=3; IntAct=EBI-7797864, EBI-8650934;
CC P11912; P55061: TMBIM6; NbExp=3; IntAct=EBI-7797864, EBI-1045825;
CC P11912; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-7797864, EBI-12845616;
CC P11912; P17152: TMEM11; NbExp=3; IntAct=EBI-7797864, EBI-723946;
CC P11912; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-7797864, EBI-10694905;
CC P11912; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-7797864, EBI-2844246;
CC P11912; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-7797864, EBI-348587;
CC P11912; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-7797864, EBI-8638294;
CC P11912; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-7797864, EBI-2800645;
CC P11912; Q14656: TMEM187; NbExp=3; IntAct=EBI-7797864, EBI-13046724;
CC P11912; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-7797864, EBI-741829;
CC P11912; A2RU14: TMEM218; NbExp=3; IntAct=EBI-7797864, EBI-10173151;
CC P11912; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-7797864, EBI-347385;
CC P11912; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-7797864, EBI-12195227;
CC P11912; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-7797864, EBI-11528917;
CC P11912; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-7797864, EBI-12887458;
CC P11912; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-7797864, EBI-11956809;
CC P11912; E9PQX1: TMEM262; NbExp=3; IntAct=EBI-7797864, EBI-17180389;
CC P11912; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-7797864, EBI-12038591;
CC P11912; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-7797864, EBI-12015604;
CC P11912; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-7797864, EBI-2548832;
CC P11912; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-7797864, EBI-11724433;
CC P11912; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-7797864, EBI-717441;
CC P11912; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-7797864, EBI-11996766;
CC P11912; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-7797864, EBI-12003468;
CC P11912; O60636: TSPAN2; NbExp=3; IntAct=EBI-7797864, EBI-3914288;
CC P11912; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-7797864, EBI-12195249;
CC P11912; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-7797864, EBI-11988865;
CC P11912; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-7797864, EBI-988826;
CC P11912; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-7797864, EBI-2819725;
CC P11912; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-7797864, EBI-4401271;
CC P11912; Q15836: VAMP3; NbExp=3; IntAct=EBI-7797864, EBI-722343;
CC P11912; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-7797864, EBI-1059156;
CC P11912; O95292: VAPB; NbExp=3; IntAct=EBI-7797864, EBI-1188298;
CC P11912; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-7797864, EBI-723716;
CC P11912; Q14508: WFDC2; NbExp=3; IntAct=EBI-7797864, EBI-723529;
CC P11912; O76024: WFS1; NbExp=3; IntAct=EBI-7797864, EBI-720609;
CC P11912; O95070: YIF1A; NbExp=3; IntAct=EBI-7797864, EBI-2799703;
CC P11912; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-7797864, EBI-751253;
CC P11912; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-7797864, EBI-751210;
CC P11912; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-7797864, EBI-12837904;
CC P11912; Q8N966: ZDHHC22; NbExp=3; IntAct=EBI-7797864, EBI-10268111;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Note=Following antigen binding, the BCR has been shown to
CC translocate from detergent-soluble regions of the cell membrane to
CC lipid rafts although signal transduction through the complex can also
CC occur outside lipid rafts. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=P11912-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P11912-2; Sequence=VSP_002476;
CC -!- TISSUE SPECIFICITY: B-cells.
CC -!- PTM: Phosphorylated on tyrosine, serine and threonine residues upon B-
CC cell activation. Phosphorylation of tyrosine residues by Src-family
CC kinases is an early and essential feature of the BCR signaling cascade.
CC The phosphorylated tyrosines serve as docking sites for SH2-domain
CC containing kinases, leading to their activation which in turn leads to
CC phosphorylation of downstream targets. Phosphorylated by LYN.
CC Phosphorylation of serine and threonine residues may prevent subsequent
CC tyrosine phosphorylation. {ECO:0000269|PubMed:10748115,
CC ECO:0000269|PubMed:10900006}.
CC -!- PTM: Arginine methylation in the ITAM domain may interfere with the
CC binding of SYK. It promotes signals leading to B-cell differentiation
CC (By similarity). {ECO:0000250}.
CC -!- DISEASE: Agammaglobulinemia 3, autosomal recessive (AGM3) [MIM:613501]:
CC A primary immunodeficiency characterized by profoundly low or absent
CC serum antibodies and low or absent circulating B-cells due to an early
CC block of B-cell development. Affected individuals develop severe
CC infections in the first years of life. {ECO:0000269|PubMed:10525050,
CC ECO:0000269|PubMed:11920841}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Two different mutations,
CC one at the splice donor site of intron 2 and the other at the splice
CC acceptor site for exon 3, have been identified. Both mutations give
CC rise to a truncated protein.
CC -!- WEB RESOURCE: Name=CD79Abase; Note=CD79A mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CD79Abase/";
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DR EMBL; S46706; AAB23558.1; -; mRNA.
DR EMBL; M80462; AAA59556.1; -; mRNA.
DR EMBL; M74721; AAA60270.1; -; mRNA.
DR EMBL; S75217; AAB20812.1; -; mRNA.
DR EMBL; M86921; AAA59557.1; -; mRNA.
DR EMBL; U05259; AAA20495.1; -; Genomic_DNA.
DR EMBL; S79248; AAC60653.1; -; mRNA.
DR EMBL; X83540; CAA58523.1; -; mRNA.
DR EMBL; AK223371; BAD97091.1; -; mRNA.
DR EMBL; X13451; CAA31802.1; ALT_SEQ; mRNA.
DR CCDS; CCDS12589.1; -. [P11912-1]
DR CCDS; CCDS46088.1; -. [P11912-2]
DR PIR; I54539; A46477.
DR PIR; S12504; S12504.
DR RefSeq; NP_001774.1; NM_001783.3. [P11912-1]
DR RefSeq; NP_067612.1; NM_021601.3. [P11912-2]
DR PDB; 1CV9; NMR; -; A=184-195.
DR PDBsum; 1CV9; -.
DR AlphaFoldDB; P11912; -.
DR BMRB; P11912; -.
DR SMR; P11912; -.
DR BioGRID; 107411; 241.
DR ELM; P11912; -.
DR IntAct; P11912; 198.
DR MINT; P11912; -.
DR STRING; 9606.ENSP00000221972; -.
DR GlyConnect; 1028; 1 N-Linked glycan (1 site).
DR GlyGen; P11912; 9 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P11912; -.
DR PhosphoSitePlus; P11912; -.
DR BioMuta; CD79A; -.
DR DMDM; 547896; -.
DR CPTAC; CPTAC-1178; -.
DR EPD; P11912; -.
DR MassIVE; P11912; -.
DR MaxQB; P11912; -.
DR PaxDb; P11912; -.
DR PeptideAtlas; P11912; -.
DR PRIDE; P11912; -.
DR ProteomicsDB; 52811; -. [P11912-1]
DR ProteomicsDB; 52812; -. [P11912-2]
DR Antibodypedia; 2990; 2240 antibodies from 47 providers.
DR DNASU; 973; -.
DR Ensembl; ENST00000221972.8; ENSP00000221972.3; ENSG00000105369.10. [P11912-1]
DR Ensembl; ENST00000444740.2; ENSP00000400605.1; ENSG00000105369.10. [P11912-2]
DR GeneID; 973; -.
DR KEGG; hsa:973; -.
DR MANE-Select; ENST00000221972.8; ENSP00000221972.3; NM_001783.4; NP_001774.1.
DR UCSC; uc002oru.4; human. [P11912-1]
DR CTD; 973; -.
DR DisGeNET; 973; -.
DR GeneCards; CD79A; -.
DR HGNC; HGNC:1698; CD79A.
DR HPA; ENSG00000105369; Group enriched (intestine, lymphoid tissue).
DR MalaCards; CD79A; -.
DR MIM; 112205; gene.
DR MIM; 613501; phenotype.
DR neXtProt; NX_P11912; -.
DR OpenTargets; ENSG00000105369; -.
DR Orphanet; 33110; Autosomal agammaglobulinemia.
DR PharmGKB; PA26237; -.
DR VEuPathDB; HostDB:ENSG00000105369; -.
DR eggNOG; ENOG502S1DI; Eukaryota.
DR GeneTree; ENSGT00940000154363; -.
DR HOGENOM; CLU_106774_0_0_1; -.
DR InParanoid; P11912; -.
DR OMA; RWQNEKF; -.
DR OrthoDB; 1165385at2759; -.
DR PhylomeDB; P11912; -.
DR TreeFam; TF336032; -.
DR PathwayCommons; P11912; -.
DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P11912; -.
DR SIGNOR; P11912; -.
DR BioGRID-ORCS; 973; 23 hits in 1065 CRISPR screens.
DR EvolutionaryTrace; P11912; -.
DR GeneWiki; CD79A; -.
DR GenomeRNAi; 973; -.
DR Pharos; P11912; Tbio.
DR PRO; PR:P11912; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P11912; protein.
DR Bgee; ENSG00000105369; Expressed in spleen and 140 other tissues.
DR ExpressionAtlas; P11912; baseline and differential.
DR Genevisible; P11912; HS.
DR GO; GO:0019815; C:B cell receptor complex; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
DR DisProt; DP01486; -.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR039695; CD79a/CD79b.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR PANTHER; PTHR14334; PTHR14334; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF02189; ITAM; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00077; ITAM; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51055; ITAM_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:7514267"
FT CHAIN 33..226
FT /note="B-cell antigen receptor complex-associated protein
FT alpha chain"
FT /id="PRO_0000014558"
FT TOPO_DOM 33..143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..116
FT /note="Ig-like C2-type"
FT DOMAIN 177..205
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT SITE 210
FT /note="Required for binding to BLNK"
FT /evidence="ECO:0000250"
FT MOD_RES 188
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P11911,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 199
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P11911,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 204
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P11911"
FT MOD_RES 210
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P11911,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 119
FT /note="Interchain (with C-136 in beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 89..127
FT /note="GTLIIQNVNKSHGGIYVCRVQEGNESYQQSCGTYLRVRQ -> E (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:7643857, ECO:0000303|Ref.9"
FT /id="VSP_002476"
FT MUTAGEN 197
FT /note="S->A: Increased phosphorylation of Y-188; when
FT associated with A-203 and V-209."
FT /evidence="ECO:0000269|PubMed:10900006"
FT MUTAGEN 203
FT /note="S->A: Increased phosphorylation of Y-188; when
FT associated with A-197 and V-209."
FT /evidence="ECO:0000269|PubMed:10900006"
FT MUTAGEN 209
FT /note="T->V: Increased phosphorylation of Y-188; when
FT associated with A-197 and A-203."
FT /evidence="ECO:0000269|PubMed:10900006"
FT CONFLICT 47
FT /note="G -> V (in Ref. 10; BAD97091)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="V -> I (in Ref. 3; AAA60270)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="E -> G (in Ref. 10; BAD97091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25038 MW; 6E5B837409969292 CRC64;
MPGGPGVLQA LPATIFLLFL LSAVYLGPGC QALWMHKVPA SLMVSLGEDA HFQCPHNSSN
NANVTWWRVL HGNYTWPPEF LGPGEDPNGT LIIQNVNKSH GGIYVCRVQE GNESYQQSCG
TYLRVRQPPP RPFLDMGEGT KNRIITAEGI ILLFCAVVPG TLLLFRKRWQ NEKLGLDAGD
EYEDENLYEG LNLDDCSMYE DISRGLQGTY QDVGSLNIGD VQLEKP
