KSYK_CHICK
ID KSYK_CHICK Reviewed; 613 AA.
AC F1N9Y5; Q5ZJ91;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Tyrosine-protein kinase SYK;
DE EC=2.7.10.2;
GN Name=SYK; ORFNames=RCJMB04_19o18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3]
RP FUNCTION IN B-CELL RECEPTOR SIGNALING PATHWAY, AND FUNCTION IN
RP PHOSPHORYLATION OF BLNK.
RX PubMed=9697839; DOI=10.1016/s1074-7613(00)80591-9;
RA Fu C., Turck C.W., Kurosaki T., Chan A.C.;
RT "BLNK: a central linker protein in B cell activation.";
RL Immunity 9:93-103(1998).
CC -!- FUNCTION: Non-receptor tyrosine kinase which mediates signal
CC transduction downstream of a variety of transmembrane receptors
CC including classical immunoreceptors like the B-cell receptor (BCR).
CC Regulates several biological processes including innate and adaptive
CC immunity, cell adhesion, osteoclast maturation, platelet activation and
CC vascular development. Assembles into signaling complexes with activated
CC receptors at the plasma membrane via interaction between its SH2
CC domains and the receptor tyrosine-phosphorylated ITAM domains. The
CC association with the receptor can also be indirect and mediated by
CC adapter proteins containing ITAM or partial hemITAM domains. The
CC phosphorylation of the ITAM domains is generally mediated by SRC
CC subfamily kinases upon engagement of the receptor. More rarely signal
CC transduction via SYK could be ITAM-independent. Direct downstream
CC effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2
CC and BLNK. Initially identified as essential in B-cell receptor (BCR)
CC signaling, it is necessary for the maturation of B-cells most probably
CC at the pro-B to pre-B transition. Activated upon BCR engagement, it
CC phosphorylates and activates BLNK an adapter linking the activated BCR
CC to downstream signaling adapters and effectors.
CC {ECO:0000269|PubMed:9697839}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- ACTIVITY REGULATION: Autoinhibited. Intramolecular binding of the
CC interdomains A and B (also called linker region) to parts of the
CC catalytic domain keep the catalytic center in an inactive conformation.
CC The phosphorylation of the interdomains or the binding of the SH2
CC domains with dually phosphorylated ITAM domains on transmembrane
CC proteins disrupt those intramolecular interactions allowing the kinase
CC domain to adopt an active conformation. The phosphorylation of SYK and
CC of the ITAM domains which is responsible for SYK activation is
CC essentially mediated by SRC subfamily kinases, like LYN, upon
CC transmembrane receptors engagement. Downstream signaling adapters and
CC intermediates may mediate positive and/or negative feedback regulation
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}. Cytoplasm, cytosol
CC {ECO:0000305}.
CC -!- DOMAIN: The SH2 domains mediate the interaction of SYK with the
CC phosphorylated ITAM domains of transmembrane proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SYK/ZAP-70 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AJ720543; CAG32202.1; -; mRNA.
DR EMBL; AADN02069860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02069869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001026601.1; NM_001031430.1.
DR AlphaFoldDB; F1N9Y5; -.
DR SMR; F1N9Y5; -.
DR BioGRID; 686612; 97.
DR STRING; 9031.ENSGALP00000024509; -.
DR PaxDb; F1N9Y5; -.
DR PRIDE; F1N9Y5; -.
DR Ensembl; ENSGALT00000032807; ENSGALP00000032170; ENSGALG00000015216.
DR GeneID; 427272; -.
DR KEGG; gga:427272; -.
DR CTD; 6850; -.
DR VEuPathDB; HostDB:geneid_427272; -.
DR eggNOG; ENOG502QT06; Eukaryota.
DR GeneTree; ENSGT00940000159053; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; F1N9Y5; -.
DR Reactome; R-GGA-114604; GPVI-mediated activation cascade.
DR Reactome; R-GGA-2029481; FCGR activation.
DR Reactome; R-GGA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-GGA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-GGA-2424491; DAP12 signaling.
DR Reactome; R-GGA-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-GGA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-GGA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-GGA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-GGA-354192; Integrin signaling.
DR Reactome; R-GGA-912631; Regulation of signaling by CBL.
DR Reactome; R-GGA-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-GGA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-GGA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:F1N9Y5; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000015216; Expressed in spleen and 7 other tissues.
DR ExpressionAtlas; F1N9Y5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IMP:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IMP:AgBase.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IMP:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:AgBase.
DR GO; GO:0071226; P:cellular response to molecule of fungal origin; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0002366; P:leukocyte activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0001945; P:lymph vessel development; ISS:UniProtKB.
DR GO; GO:0002281; P:macrophage activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0002283; P:neutrophil activation involved in immune response; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
DR GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IBA:GO_Central.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IBA:GO_Central.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISS:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IBA:GO_Central.
DR GO; GO:0090237; P:regulation of arachidonic acid secretion; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0043313; P:regulation of neutrophil degranulation; ISS:UniProtKB.
DR GO; GO:0050764; P:regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0010543; P:regulation of platelet activation; ISS:UniProtKB.
DR GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0032928; P:regulation of superoxide anion generation; ISS:UniProtKB.
DR GO; GO:0002554; P:serotonin secretion by platelet; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd09938; SH2_N-SH2_Zap70_Syk_like; 1.
DR Gene3D; 1.10.930.10; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023420; Kinase_SYK/ZAP-70_inter-SH2_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035838; SYK/ZAP-70_N_SH2.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR012234; Tyr_kinase_non-rcpt_SYK/ZAP70.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 2.
DR PIRSF; PIRSF000604; TyrPK_SYK; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Immunity; Innate immunity; Kinase;
KW Membrane; Nucleotide-binding; Reference proteome; Repeat; SH2 domain;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..613
FT /note="Tyrosine-protein kinase SYK"
FT /id="PRO_0000415332"
FT DOMAIN 14..106
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 167..258
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 349..613
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 107..166
FT /note="Interdomain A"
FT REGION 259..348
FT /note="Interdomain B"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 355..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 188
FT /note="N -> D (in Ref. 1; CAG32202)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="E -> G (in Ref. 1; CAG32202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 69901 MW; 32783B7D0C8EBC82 CRC64;
MASNMANPAN HLPYFFGNIT REEAEEYLMQ GGMSDGLYLL RQSRNYLGGF ALSLAYGRKV
HHYTIERELS GTYAIAGGKS HASPAELINY HSEEADGLIC LLRKSFNRPP GVEPKTGPFE
DLKENLIREY VKQTWNLQGH ALEQAIISQK PQLEKLIATT AHEKMPWFHG RISREESEHR
ILIGSRNNGK FLIRERDSNG SYALCLLNDG KVLHYRIDRD KTGKLSIPDG KRFDTLWQLV
EHYSYKPDGL LRVLSIPCPR HGSESDNVVF DTRPLPGTPS KLQTPIGAPS DDQTPFNPYV
LQRARGLIGA EKGDQREALP MDTEVYESPY ADPDEIKPKN VTLDRKLLTL EEGELGSGNF
GTVKKGFYKM KKGAKPVAVK ILKNESNDPA IKDELLREAN VMQQLDNPYI VRMIGICEAE
AWMLVMEMAE LGPLNKFLQK NRHVTEKNIT ELVHQVSMGM KYLEENNFVH RDLAARNVLL
VTQHYAKISD FGLSKALSAD ENYYKAQSHG KWPVKWYAPE CMNFYKFSSK SDVWSFGVLM
WEAFSYGQKP YKGMKGGEVA QMIERGERME CPEACPVEVY DLMKLCWTYN VDDRPGFVAV
ELRLRNYYYD ISH
