ID A0A1L8HYI7_XENLA Unreviewed; 605 AA.
AC A0A1L8HYI7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000604};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000604};
GN Name=syk.L {ECO:0000313|RefSeq:XP_018101865.1,
GN ECO:0000313|Xenbase:XB-GENE-978187};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018101865.1};
RN [1] {ECO:0000313|RefSeq:XP_018101865.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018101865.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018101865.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001149,
CC ECO:0000256|PIRNR:PIRNR000604};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SYK/ZAP-70 subfamily. {ECO:0000256|PIRNR:PIRNR000604}.
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DR RefSeq; XP_018101865.1; XM_018246376.2.
DR AlphaFoldDB; A0A1L8HYI7; -.
DR STRING; 8355.A0A1L8HYI7; -.
DR PaxDb; 8355-A0A1L8HYI7; -.
DR GeneID; 446500; -.
DR KEGG; xla:446500; -.
DR AGR; Xenbase:XB-GENE-978187; -.
DR CTD; 446500; -.
DR Xenbase; XB-GENE-978187; syk.L.
DR OMA; ICEGASW; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 446500; Expressed in spleen and 11 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd10401; SH2_C-SH2_Syk_like; 1.
DR CDD; cd09938; SH2_N-SH2_Zap70_Syk_like; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF231; TYROSINE-PROTEIN KINASE SYK; 1.
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; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000604};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000604};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000604};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000604};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000604}.
FT ACT_SITE 464
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-1"
FT BINDING 347..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2"
FT BINDING 372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 605 AA; 69084 MW; B11A87C3AD623341 CRC64;
MADIAQNLPY FFGNITREES EDYLRQAGAS DGLYLLRQSR SYLGGYALSV AHGRHFYHYT
IERELNGTYA ISGGISHNSP AELCHYHTLE SSGLVCLLKK PCNLPPGVQP KTGPFEDLKE
HLIREYVQQT WNLQGEALEQ AIISQKPQLE KLIATTAHEK MPWFHGRISR EDSEQLLISG
VKPNGSFLIR ERDDNGSYAL CLLHDRKISH YRIDRDKTGK LSIPDGKKFD TLWQLVEHYS
YKPDGLLRVL TEPCSRATGR KESFIFNRTV CPEPPPHHKM SSAEAMKRNR SSSSMKVLSC
RPNVEVTKDS MPMDTDVYRG IYEDPDEFRP MDGKIAPEQL TLLETELGSG NFGNVKKGML
KTSKSEKPVA VKILKNDSND ESMKDELLKE ARVMQLLNNP YIVRMLGICE GASWMLVMEL
AGLGPLNKFL ARNKNVTEHN VTELVHQVSM GMKYLEETNF VHRDLAARNV LLVTQHYAKI
SDFGLSKALG TDENYYQAKT TGKWPMKWYA PESLNYHKFS SKSDVWSFGI LMWEGYSYGL
KPYPGMKGNE VTVFIESGKR LESPRRCPPE MYNLMKLCWT YSTDERPSFA VVELKLRSYY
YDSSH
//
