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P0CAN6

- CD79A_CANFA

UniProt

P0CAN6 - CD79A_CANFA

Protein

B-cell antigen receptor complex-associated protein alpha chain

Gene

CD79A

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (05 May 2009)
      Previous versions | rss
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    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

    1. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. B cell differentiation Source: Ensembl
    2. B cell proliferation Source: Ensembl
    3. B cell receptor signaling pathway Source: Ensembl

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_174255. 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: 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

    GO - Cellular componenti

    1. B cell receptor complex Source: Ensembl
    2. external side of plasma membrane Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane raft Source: Ensembl
    5. multivesicular body Source: Ensembl

    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...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei152 – 17221HelicalSequence AnalysisAdd
    BLAST

    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.
    KOiK06506.
    OMAiRKRWQNE.
    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

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    MPGGPGLLQA LCATTFLLFL ISAGGLGPGS QALWVDGGPP SMTVSLGETA    50
    RLQCLHNRSR LSSKLNITWW RVLQGNATWP DIFLSYGKGP NGELTIDTVN 100
    KSHMGMYRCQ VEEKDLNQKI LSSQQSCGTY LRVRERLPRP FLDMGEGTKN 150
    NIITAEGIIL LFCAVVPGTL LLFRKRWQNM KFGVDAQDDY EDENLYEGLN 200
    LDDCSMYEDI SRGLQGTYQD VGSLHIGDGD VQLEKP 236
    Length:236
    Mass (Da):26,120
    Last modified:May 5, 2009 - v1
    Checksum:iE24C3DDF97119B7E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DN272794 mRNA. No translation available.
    DN352654 mRNA. No translation available.
    AAEX02033438 Genomic DNA. No translation available.
    RefSeqi XP_541597.2. XM_541597.4.

    3D structure databases

    ProteinModelPortali P0CAN6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000007407.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSCAFT00000008000 ; ENSCAFP00000007407 ; ENSCAFG00000004980 .
    GeneIDi 484483.
    KEGGi cfa:484483.

    Organism-specific databases

    CTDi 973.

    Phylogenomic databases

    eggNOGi NOG41728.
    GeneTreei ENSGT00510000049127.
    HOGENOMi HOG000074307.
    KOi K06506.
    OMAi RKRWQNE.
    OrthoDBi EOG7J70GM.
    TreeFami TF336032.

    Enzyme and pathway databases

    Reactomei REACT_174255. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

    Miscellaneous databases

    NextBioi 20858616.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    [Graphical view ]
    Pfami PF00047. ig. 1 hit.
    PF02189. ITAM. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    SM00077. ITAM. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS51055. ITAM_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 41 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