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P0CAN6 (CD79A_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
B-cell antigen receptor complex-associated protein alpha chain
Alternative name(s):
Ig-alpha
CD_antigen=CD79a
Gene names
Name:CD79A
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

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.

Subcellular location

Cell membrane; 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.

Post-translational modification

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.

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

Sequence similarities

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 ITAM domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 236204B-cell antigen receptor complex-associated protein alpha chain
PRO_0000373777

Regions

Topological domain33 – 151119Extracellular Potential
Transmembrane152 – 17221Helical; Potential
Topological domain173 – 23664Cytoplasmic Potential
Domain33 – 12290Ig-like C2-type
Domain185 – 21329ITAM

Sites

Site2181Required for binding to BLNK By similarity

Amino acid modifications

Modified residue1961Phosphotyrosine; by SRC-type Tyr-kinases By similarity
Modified residue2071Phosphotyrosine By similarity
Modified residue2121Asymmetric dimethylarginine; by PRMT1 By similarity
Modified residue2181Phosphotyrosine; by Tyr-kinases By similarity
Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation761N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 109 By similarity
Disulfide bond127Interchain (with beta chain) Potential

Sequences

Sequence LengthMass (Da)Tools
P0CAN6 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: E24C3DDF97119B7E

FASTA23626,120
        10         20         30         40         50         60 
MPGGPGLLQA LCATTFLLFL ISAGGLGPGS QALWVDGGPP SMTVSLGETA RLQCLHNRSR 

        70         80         90        100        110        120 
LSSKLNITWW RVLQGNATWP DIFLSYGKGP NGELTIDTVN KSHMGMYRCQ VEEKDLNQKI 

       130        140        150        160        170        180 
LSSQQSCGTY LRVRERLPRP FLDMGEGTKN NIITAEGIIL LFCAVVPGTL LLFRKRWQNM 

       190        200        210        220        230 
KFGVDAQDDY EDENLYEGLN LDDCSMYEDI SRGLQGTYQD VGSLHIGDGD VQLEKP 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DN272794 mRNA. No translation available.
DN352654 mRNA. No translation available.
AAEX02033438 Genomic DNA. No translation available.
RefSeqXP_541597.2. XM_541597.4.

3D structure databases

ProteinModelPortalP0CAN6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000007407.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000008000; ENSCAFP00000007407; ENSCAFG00000004980.
GeneID484483.
KEGGcfa:484483.

Organism-specific databases

CTD973.

Phylogenomic databases

eggNOGNOG41728.
GeneTreeENSGT00510000049127.
HOGENOMHOG000074307.
KOK06506.
OMAPFLDMGE.
OrthoDBEOG7J70GM.
TreeFamTF336032.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
IPR003110. Phos_immunorcpt_sig_ITAM.
[Graphical view]
PfamPF00047. ig. 1 hit.
PF02189. ITAM. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00077. ITAM. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS51055. ITAM_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20858616.

Entry information

Entry nameCD79A_CANFA
AccessionPrimary (citable) accession number: P0CAN6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families