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B-cell antigen receptor complex-associated protein alpha chain (Ig-alpha) (MB-1 membrane glycoprotein) (Membrane-bound immunoglobulin-associated protein) (Surface IgM-associated protein) (CD antigen CD79a)

 CD79A_BOVIN             Reviewed;         223 AA.
P40293; Q0P5B8; Q28134;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 131.
RecName: Full=B-cell antigen receptor complex-associated protein alpha chain;
AltName: Full=Ig-alpha;
AltName: Full=MB-1 membrane glycoprotein;
AltName: Full=Membrane-bound immunoglobulin-associated protein;
AltName: Full=Surface IgM-associated protein;
AltName: CD_antigen=CD79a;
Flags: Precursor;
Name=CD79A; Synonyms=IGA, MB-1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Leukocyte, and Lymphoblast;
PubMed=7963570;
Youn H.-Y., Goitsuka R., Okuda M., Watari T., Tsujimoto H.,
Hasegawa A.;
"Two forms of the mb-1 gene transcript in cattle.";
J. Immunol. 153:5127-5132(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8810000; DOI=10.1016/0165-2427(95)05546-0;
Youn H.-Y., Goitsuka R., Kato H., Mason D.Y., Watari T., Tsujimoto H.,
Hasegawa A.;
"Molecular cloning of bovine mb-1 cDNA.";
Vet. Immunol. Immunopathol. 52:191-200(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Hereford; TISSUE=Thymus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Required in cooperation with CD79B for initiation of the
signal transduction cascade activated by binding of antigen to the
B-cell antigen receptor complex (BCR) which leads to
internalization of the complex, trafficking to late endosomes and
antigen presentation. Also required for BCR surface expression and
for efficient differentiation of pro- and pre-B-cells. Stimulates
SYK autophosphorylation and activation. Binds to BLNK, bringing
BLNK into proximity with SYK and allowing SYK to phosphorylate
BLNK. Also interacts with and increases activity of some Src-
family tyrosine kinases. Represses BCR signaling during
development of immature B-cells (By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked.
Part of the B-cell antigen receptor complex where the alpha/beta
chain heterodimer is non-covalently associated with an antigen-
specific membrane-bound surface immunoglobulin of two heavy chains
and two light chains. Interacts through its phosphorylated ITAM
domain with the SH2 domains of SYK which stimulates SYK
autophosphorylation and activation. Also interacts, when
phosphorylated on Tyr-207, with the SH2 domain of BLNK/SLP65,
bringing BLNK into proximity with SYK and allowing SYK to
phosphorylate BLNK which is necessary for trafficking of the BCR
to late endosomes. Interacts with Src-family tyrosine kinases
including FYN and LYN, increasing their activity (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Note=Following antigen binding, the BCR has been shown to
translocate from detergent-soluble regions of the cell membrane to
lipid rafts although signal transduction through the complex can
also occur outside lipid rafts. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P40293-1; Sequence=Displayed;
Name=2;
IsoId=P40293-2; Sequence=VSP_027221, VSP_027222;
-!- TISSUE SPECIFICITY: B-cells.
-!- PTM: Phosphorylated on tyrosine, serine and threonine residues
upon B-cell activation. Phosphorylation of tyrosine residues by
Src-family kinases, including LYN, is an early and essential
feature of the BCR signaling cascade. The phosphorylated tyrosines
serve as docking sites for SH2-domain containing kinases, leading
to their activation which in turn leads to phosphorylation of
downstream targets. Phosphorylation of serine and threonine
residues may prevent subsequent tyrosine phosphorylation (By
similarity). {ECO:0000250}.
-!- PTM: Arginine methylation in the ITAM domain may interfere with
the binding of SYK. It promotes signals leading to B-cell
differentiation (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; D16412; BAA03899.1; -; mRNA.
EMBL; D16459; BAA03926.1; -; mRNA.
EMBL; BC120260; AAI20261.1; -; mRNA.
PIR; I45927; I45927.
RefSeq; NP_776691.2; NM_174266.4. [P40293-1]
UniGene; Bt.4436; -.
ProteinModelPortal; P40293; -.
SMR; P40293; -.
STRING; 9913.ENSBTAP00000002451; -.
PaxDb; P40293; -.
PRIDE; P40293; -.
Ensembl; ENSBTAT00000002451; ENSBTAP00000002451; ENSBTAG00000001882. [P40293-1]
Ensembl; ENSBTAT00000031989; ENSBTAP00000031933; ENSBTAG00000001882. [P40293-2]
GeneID; 281674; -.
KEGG; bta:281674; -.
CTD; 973; -.
eggNOG; ENOG410IV8X; Eukaryota.
eggNOG; ENOG4111VIC; LUCA.
GeneTree; ENSGT00510000049127; -.
HOGENOM; HOG000074307; -.
HOVERGEN; HBG050854; -.
InParanoid; P40293; -.
KO; K06506; -.
OMA; EGTKNRI; -.
OrthoDB; EOG091G10RQ; -.
TreeFam; TF336032; -.
Reactome; R-BTA-5690714; CD22 mediated BCR regulation.
Reactome; R-BTA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
Proteomes; UP000009136; Chromosome 18.
Bgee; ENSBTAG00000001882; -.
GO; GO:0019815; C:B cell receptor complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
Pfam; PF02189; ITAM; 1.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00077; ITAM; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51055; ITAM_1; 1.
2: Evidence at transcript level;
Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Methylation; Phosphoprotein;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 223 B-cell antigen receptor complex-
associated protein alpha chain.
/FTId=PRO_0000014557.
TOPO_DOM 32 140 Extracellular. {ECO:0000255}.
TRANSMEM 141 161 Helical. {ECO:0000255}.
TOPO_DOM 162 223 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 120 Ig-like C2-type.
DOMAIN 174 202 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
SITE 207 207 Required for binding to BLNK.
{ECO:0000250}.
MOD_RES 185 185 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000250|UniProtKB:P11911,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 196 196 Phosphotyrosine.
{ECO:0000250|UniProtKB:P11911,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 201 201 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:P11911}.
MOD_RES 207 207 Phosphotyrosine; by Tyr-kinases.
{ECO:0000250|UniProtKB:P11911,
ECO:0000255|PROSITE-ProRule:PRU00379}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 53 104 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 116 116 Interchain (with beta chain).
{ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 124 133 DPLPRPFLDM -> ETMAEHEIRG (in isoform 2).
{ECO:0000303|PubMed:7963570}.
/FTId=VSP_027221.
VAR_SEQ 134 223 Missing (in isoform 2).
{ECO:0000303|PubMed:7963570}.
/FTId=VSP_027222.
SEQUENCE 223 AA; 24630 MW; CE2F0AF175748304 CRC64;
MPEGPQALQS PPATIFLLLI SAAGLGPGCQ ALWVEWGPPS VTVSVGEEVR LQCTHNGSNT
NVTWWHVLQS NSSWPPVMYR GDVGAGGELI IKPVNKTHRG MYRCQVSDGK KIQRSCGTYL
RVRDPLPRPF LDMGEGTKNN IITAEGIILL ICAVVPGTLL LFRKRWQNMK FGADIQDDYE
DENLYEGLNL DDCSMYEDIS RGLQGTYQDV GSLHIGDAQL EKP


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