CD79A_CANLF
ID CD79A_CANLF Reviewed; 236 AA.
AC P0CAN6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=B-cell antigen receptor complex-associated protein alpha chain;
DE AltName: Full=Ig-alpha;
DE AltName: CD_antigen=CD79a;
DE Flags: Precursor;
GN Name=CD79A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph node, and Thymus;
RA Staten N.R.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
CC -!- FUNCTION: Required in cooperation with CD79B for initiation of the
CC signal transduction cascade activated by binding of antigen to the B-
CC cell antigen receptor complex (BCR) which leads to internalization of
CC the complex, trafficking to late endosomes and antigen presentation.
CC Also required for BCR surface expression and for efficient
CC differentiation of pro- and pre-B-cells. Stimulates SYK
CC autophosphorylation and activation. Binds to BLNK, bringing BLNK into
CC proximity with SYK and allowing SYK to phosphorylate BLNK. Also
CC interacts with and increases activity of some Src-family tyrosine
CC kinases. Represses BCR signaling during development of immature B-cells
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of alpha and beta chains; disulfide-linked. Part
CC of the B-cell antigen receptor complex where the alpha/beta chain
CC heterodimer is non-covalently associated with an antigen-specific
CC membrane-bound surface immunoglobulin of two heavy chains and two light
CC chains. Interacts through its phosphorylated ITAM domain with the SH2
CC domains of SYK which stimulates SYK autophosphorylation and activation.
CC Also interacts, when phosphorylated on Tyr-207, with the SH2 domain of
CC BLNK/SLP65, bringing BLNK into proximity with SYK and allowing SYK to
CC phosphorylate BLNK which is necessary for trafficking of the BCR to
CC late endosomes. Interacts with Src-family tyrosine kinases including
CC FYN and LYN, increasing their activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=Following antigen binding, the BCR
CC has been shown to translocate from detergent-soluble regions of the
CC cell membrane to lipid rafts although signal transduction through the
CC complex can also occur outside lipid rafts. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine, serine and threonine residues upon B-
CC cell activation. Phosphorylation of tyrosine residues by Src-family
CC kinases, including LYN, is an early and essential feature of the BCR
CC signaling cascade. The phosphorylated tyrosines serve as docking sites
CC for SH2-domain containing kinases, leading to their activation which in
CC turn leads to phosphorylation of downstream targets. Phosphorylation of
CC serine and threonine residues may prevent subsequent tyrosine
CC phosphorylation (By similarity). {ECO:0000250}.
CC -!- PTM: Arginine methylation in the ITAM domain may interfere with the
CC binding of SYK. It promotes signals leading to B-cell differentiation
CC (By similarity). {ECO:0000250}.
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DR EMBL; DN272794; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DN352654; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AAEX02033438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001300763.1; NM_001313834.1.
DR AlphaFoldDB; P0CAN6; -.
DR SMR; P0CAN6; -.
DR STRING; 9612.ENSCAFP00000007407; -.
DR PaxDb; P0CAN6; -.
DR Ensembl; ENSCAFT00040014193; ENSCAFP00040012276; ENSCAFG00040007622.
DR GeneID; 484483; -.
DR KEGG; cfa:484483; -.
DR CTD; 973; -.
DR eggNOG; ENOG502S1DI; Eukaryota.
DR HOGENOM; CLU_106774_0_0_1; -.
DR InParanoid; P0CAN6; -.
DR OMA; RWQNEKF; -.
DR OrthoDB; 1165385at2759; -.
DR TreeFam; TF336032; -.
DR Reactome; R-CFA-5690714; CD22 mediated BCR regulation.
DR Reactome; R-CFA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000004980; Expressed in ovary and 48 other tissues.
DR GO; GO:0019815; C:B cell receptor complex; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR039695; CD79a/CD79b.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR PANTHER; PTHR14334; PTHR14334; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF02189; ITAM; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00077; ITAM; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51055; ITAM_1; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..236
FT /note="B-cell antigen receptor complex-associated protein
FT alpha chain"
FT /id="PRO_0000373777"
FT TOPO_DOM 33..151
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..122
FT /note="Ig-like C2-type"
FT DOMAIN 185..213
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT SITE 218
FT /note="Required for binding to BLNK"
FT /evidence="ECO:0000250"
FT MOD_RES 196
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P11911,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 207
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11911,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 212
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P11911"
FT MOD_RES 218
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P11911,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 127
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 236 AA; 26120 MW; E24C3DDF97119B7E CRC64;
MPGGPGLLQA LCATTFLLFL ISAGGLGPGS QALWVDGGPP SMTVSLGETA RLQCLHNRSR
LSSKLNITWW RVLQGNATWP DIFLSYGKGP NGELTIDTVN KSHMGMYRCQ VEEKDLNQKI
LSSQQSCGTY LRVRERLPRP FLDMGEGTKN NIITAEGIIL LFCAVVPGTL LLFRKRWQNM
KFGVDAQDDY EDENLYEGLN LDDCSMYEDI SRGLQGTYQD VGSLHIGDGD VQLEKP
