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Protein

B-cell antigen receptor complex-associated protein alpha chain

Gene

CD79A

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei218 – 2181Required for binding to BLNKBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiREACT_330493. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
B-cell antigen receptor complex-associated protein alpha chain
Alternative name(s):
Ig-alpha
CD_antigen: CD79a
Gene namesi
Name:CD79A
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Chromosome 1

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity

  • 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.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 151119ExtracellularSequence AnalysisAdd
BLAST
Transmembranei152 – 17221HelicalSequence AnalysisAdd
BLAST
Topological domaini173 – 23664CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 236204B-cell antigen receptor complex-associated protein alpha chainPRO_0000373777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 109PROSITE-ProRule annotation
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi127 – 127Interchain (with beta chain)PROSITE-ProRule annotation
Modified residuei196 – 1961Phosphotyrosine; by SRC-type Tyr-kinasesPROSITE-ProRule annotation
Modified residuei207 – 2071PhosphotyrosinePROSITE-ProRule annotation
Modified residuei212 – 2121Asymmetric dimethylarginine; by PRMT1By similarity
Modified residuei218 – 2181Phosphotyrosine; by Tyr-kinasesPROSITE-ProRule annotation

Post-translational modificationi

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).By similarity
Arginine methylation in the ITAM domain may interfere with the binding of SYK. It promotes signals leading to B-cell differentiation (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000007407.

Structurei

3D structure databases

ProteinModelPortaliP0CAN6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12290Ig-like C2-typeAdd
BLAST
Domaini185 – 21329ITAMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ITAM domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41728.
GeneTreeiENSGT00510000049127.
HOGENOMiHOG000074307.
InParanoidiP0CAN6.
KOiK06506.
OMAiPFLDMGE.
OrthoDBiEOG7J70GM.
TreeFamiTF336032.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF02189. ITAM. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CAN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGGPGLLQA LCATTFLLFL ISAGGLGPGS QALWVDGGPP SMTVSLGETA
60 70 80 90 100
RLQCLHNRSR LSSKLNITWW RVLQGNATWP DIFLSYGKGP NGELTIDTVN
110 120 130 140 150
KSHMGMYRCQ VEEKDLNQKI LSSQQSCGTY LRVRERLPRP FLDMGEGTKN
160 170 180 190 200
NIITAEGIIL LFCAVVPGTL LLFRKRWQNM KFGVDAQDDY EDENLYEGLN
210 220 230
LDDCSMYEDI SRGLQGTYQD VGSLHIGDGD VQLEKP
Length:236
Mass (Da):26,120
Last modified:May 5, 2009 - v1
Checksum:iE24C3DDF97119B7E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DN272794 mRNA. No translation available.
DN352654 mRNA. No translation available.
AAEX02033438 Genomic DNA. No translation available.
RefSeqiXP_541597.2. XM_541597.4.

Genome annotation databases

EnsembliENSCAFT00000008000; ENSCAFP00000007407; ENSCAFG00000004980.
GeneIDi484483.
KEGGicfa:484483.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DN272794 mRNA. No translation available.
DN352654 mRNA. No translation available.
AAEX02033438 Genomic DNA. No translation available.
RefSeqiXP_541597.2. XM_541597.4.

3D structure databases

ProteinModelPortaliP0CAN6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000007407.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000008000; ENSCAFP00000007407; ENSCAFG00000004980.
GeneIDi484483.
KEGGicfa:484483.

Organism-specific databases

CTDi973.

Phylogenomic databases

eggNOGiNOG41728.
GeneTreeiENSGT00510000049127.
HOGENOMiHOG000074307.
InParanoidiP0CAN6.
KOiK06506.
OMAiPFLDMGE.
OrthoDBiEOG7J70GM.
TreeFamiTF336032.

Enzyme and pathway databases

ReactomeiREACT_330493. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

NextBioi20858616.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF02189. ITAM. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Staten N.R.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph node and Thymus.
  2. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
    , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Boxer.

Entry informationi

Entry nameiCD79A_CANFA
AccessioniPrimary (citable) accession number: P0CAN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: April 1, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.