Cd79a
entrez
12518
canonical
uniprot
P11911
canonical
ensembl
ENSMUSG00000003379
resolver
ensp
ENSMUSP00000003469
resolver
enst
ENSMUST00000003469
resolver
genesymbol
Cd79a
resolver
genesymbol_syn
Iga
resolver
genesymbol_syn
Mb-1
resolver
uniprot
Q6GTY0
resolver
uniprot_entry
CD79A_MOUSE
resolver
uniprot_sec
Q6GTY0
resolver
amino_acid_sequence
MPGGLEALRALPLLLFLSYACLGPGCQALRVEGGPPSLTVNLGEEARLTCENNGRNPNITWWFSLQSNITWPPVPLGPGQGTTGQLFFPEVNKNHRGLYWCQVIENNILKRSCGTYLRVRNPVPRPFLDMGEGTKNRIITAEGIILLFCAVVPGTLLLFRKRWQNEKFGVDMPDDYEDENLYEGLNLDDCSMYEDISRGLQGTYQDVGNLHIGDAQLEKP
uniprot
proteins
function
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. {ECO:0000269|PubMed:10352267, ECO:0000269|PubMed:10591178, ECO:0000269|PubMed:11514602, ECO:0000269|PubMed:11859098, ECO:0000269|PubMed:12097390, ECO:0000269|PubMed:12356683, ECO:0000269|PubMed:15661879, ECO:0000269|PubMed:16860757, ECO:0000269|PubMed:17163454, ECO:0000269|PubMed:8175787, ECO:0000269|PubMed:9469435}.
uniprot
proteins
mass_dalton
24583
uniprot
proteins
mutagenesis
MUTAGEN 176; /note="Y->F: Increases tyrosine phosphorylation. Inhibits phosphorylation of BLNK. Impaired antigen presentation; when associated with F-204."; /evidence="ECO:0000269|PubMed:11859098, ECO:0000269|PubMed:11909947, ECO:0000269|PubMed:16860757, ECO:0000269|PubMed:17163454, ECO:0000269|PubMed:8306975"; MUTAGEN 182; /note="Y->F: Strongly reduces tyrosine phosphorylation and pre-B-cell differentiation; when associated with F-193. Abolishes constitutive internalization of BCR."; /evidence="ECO:0000269|PubMed:11514602, ECO:0000269|PubMed:17163454, ECO:0000269|PubMed:8306975, ECO:0000269|PubMed:9469435"; MUTAGEN 193; /note="Y->F: Strongly reduces tyrosine phosphorylation and pre-B-cell differentiation; when associated with F-182. No effect on constitutive internalization of BCR."; /evidence="ECO:0000269|PubMed:11514602, ECO:0000269|PubMed:17163454, ECO:0000269|PubMed:8306975, ECO:0000269|PubMed:9469435"; MUTAGEN 198; /note="R->K: Associates more strongly with SYK. Increases calcium response upon BCR ligation."; /evidence="ECO:0000269|PubMed:20231378"; MUTAGEN 204; /note="Y->F: Has little effect on tyrosine phosphorylation. Reduces pre-B-cell differentiation. Abolishes binding to BLNK. Inhibits phosphorylation of BLNK. No effect on cap formation or BCR internalization. Impaired antigen presentation; when associated with F-176."; /evidence="ECO:0000269|PubMed:11449366, ECO:0000269|PubMed:11859098, ECO:0000269|PubMed:11909947, ECO:0000269|PubMed:16860757, ECO:0000269|PubMed:17163454
uniprot
proteins
post_translational_modification
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. {ECO:0000269|PubMed:11449366, ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:7592958, ECO:0000269|PubMed:8306975}.; PTM: Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation. {ECO:0000269|PubMed:20231378}.; PTM: Ubiquitinated by the BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex composed of at least CUL3, KLHL6 and RBX1; leading to proteasomal degradation. {ECO:0000250|UniProtKB:P11912}.
uniprot
proteins
pubmed
10352267
uniprot
proteins
pubmed
10587346
uniprot
proteins
pubmed
10591178
uniprot
proteins
pubmed
11238609
uniprot
proteins
pubmed
11449366
uniprot
proteins
pubmed
11514602
uniprot
proteins
pubmed
11859098
uniprot
proteins
pubmed
11909947
uniprot
proteins
pubmed
12097390
uniprot
proteins
pubmed
12356683
uniprot
proteins
pubmed
1506682
uniprot
proteins
pubmed
15335855
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15661879
uniprot
proteins
pubmed
1639443
uniprot
proteins
pubmed
16860757
uniprot
proteins
pubmed
17163454
uniprot
proteins
pubmed
1922076
uniprot
proteins
pubmed
20231378
uniprot
proteins
pubmed
2023945
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2269334
uniprot
proteins
pubmed
2358676
uniprot
proteins
pubmed
2463161
uniprot
proteins
pubmed
7538118
uniprot
proteins
pubmed
7592958
uniprot
proteins
pubmed
8168489
uniprot
proteins
pubmed
8175787
uniprot
proteins
pubmed
8306975
uniprot
proteins
pubmed
8976175
uniprot
proteins
pubmed
9469435
uniprot
proteins
sequence_length
220
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}; Single-pass type I membrane protein {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}. 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.
uniprot
proteins
transmembrane_region
TRANSMEM 138..159; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins