ID W5UC78_ICTPU Unreviewed; 502 AA.
AC W5UC78;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN Name=LYN {ECO:0000313|EMBL:AHH39485.1};
GN Synonyms=LOC108267808 {ECO:0000313|RefSeq:XP_053537214.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH39485.1};
RN [1] {ECO:0000313|EMBL:AHH39485.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH39485.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [2] {ECO:0000313|RefSeq:XP_053537214.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_053537214.1};
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|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR EMBL; JT411549; AHH39485.1; -; mRNA.
DR RefSeq; XP_053537214.1; XM_053681239.1.
DR KEGG; ipu:108267808; -.
DR Proteomes; UP000221080; Chromosome 7.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09933; SH2_Src_family; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF42; TYROSINE-PROTEIN KINASE LYN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 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; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
FT DOMAIN 53..113
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 119..216
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 237..491
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 502 AA; 56792 MW; F0678D1BD3EA6DF6 CRC64;
MGCVSSREKG GGVKQRQNPR PPEVKRYITD PAQNSSSLLP GQVLQNVECA VSTDSKMVIA
IFSYDAENKN ELAFKKGDKL VILDENGEWW KAKSLSSGKV GLIPSNYIKL EESMDNKDWY
FKNISRITAE RNLLAPANKP GAFLIRQSET TAGSYSMSVR DVGPNRSAVV KHYKIRLLEN
GGFYISPRIT FQTIDDLIVY YQKQANGLCQ RLGKACVKPK NAVQWDEDAW EIPKESLHMT
KRLGAGQFGE VWLATYNNTT KVAVKTLKPG SMSVEAFLQE ANLMKTLRHE RLVRLYAVVT
KSQPLYIITE FMSNGSLLDF LKSPPGRRIQ FPKLVDFGAQ IAEGMAYIEK KNYIHRDLRA
ANVLVSESLL CKIADFGLAR VIEENEYSAR EGAKFPIKWT APEAINYGSF TIKSDMWSFG
ILLYEIVTYG KLPYTGLSNS EVMARVQRGY RMQCPDNCPS ELYEIMTSCW KAKPEERPTF
DFMQSVLEDY YTATEGQYQS QP
//
