ID F7DKS0_XENTR Unreviewed; 1142 AA.
AC F7DKS0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
GN Name=jak1 {ECO:0000313|Ensembl:ENSXETP00000044013,
GN ECO:0000313|RefSeq:XP_002931642.1,
GN ECO:0000313|Xenbase:XB-GENE-483750};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000044013};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000044013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000044013};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000044013}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002931642.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002931642.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002931642.1};
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:PIRNR000636, ECO:0000256|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. JAK subfamily. {ECO:0000256|PIRNR:PIRNR000636}.
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DR RefSeq; XP_002931642.1; XM_002931596.5.
DR RefSeq; XP_017949056.1; XM_018093567.1.
DR Ensembl; ENSXETT00000044013; ENSXETP00000044013; ENSXETG00000020396.
DR GeneID; 100038172; -.
DR KEGG; xtr:100038172; -.
DR AGR; Xenbase:XB-GENE-483750; -.
DR CTD; 3716; -.
DR Xenbase; XB-GENE-483750; jak1.
DR eggNOG; KOG0197; Eukaryota.
DR HOGENOM; CLU_008155_1_0_1; -.
DR OMA; KDIMQGE; -.
DR OrthoDB; 1614410at2759; -.
DR TreeFam; TF327041; -.
DR Reactome; R-XTR-1059683; Interleukin-6 signaling.
DR Reactome; R-XTR-1266695; Interleukin-7 signaling.
DR Reactome; R-XTR-449836; Other interleukin signaling.
DR Reactome; R-XTR-6783783; Interleukin-10 signaling.
DR Reactome; R-XTR-6788467; IL-6-type cytokine receptor ligand interactions.
DR Reactome; R-XTR-877300; Interferon gamma signaling.
DR Reactome; R-XTR-877312; Regulation of IFNG signaling.
DR Reactome; R-XTR-8854691; Interleukin-20 family signaling.
DR Reactome; R-XTR-8983432; Interleukin-15 signaling.
DR Reactome; R-XTR-8985947; Interleukin-9 signaling.
DR Reactome; R-XTR-9020558; Interleukin-2 signaling.
DR Reactome; R-XTR-9020958; Interleukin-21 signaling.
DR Reactome; R-XTR-909733; Interferon alpha/beta signaling.
DR Reactome; R-XTR-912694; Regulation of IFNA/IFNB signaling.
DR Reactome; R-XTR-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-XTR-9732724; IFNG signaling activates MAPKs.
DR Proteomes; UP000008143; Chromosome 4.
DR Bgee; ENSXETG00000020396; Expressed in liver and 15 other cell types or tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13332; FERM_C_JAK1; 1.
DR CDD; cd05077; PTK_Jak1_rpt1; 1.
DR CDD; cd05079; PTKc_Jak1_rpt2; 1.
DR CDD; cd10378; SH2_Jak1; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR041155; FERM_F1.
DR InterPro; IPR041046; FERM_F2.
DR InterPro; IPR041381; JAK1-3/TYK2_PHL_dom.
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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
DR InterPro; IPR020776; Tyr_kinase_non-rcpt_Jak1.
DR PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
DR PANTHER; PTHR45807:SF5; TYROSINE-PROTEIN KINASE JAK1; 1.
DR Pfam; PF18379; FERM_F1; 1.
DR Pfam; PF18377; FERM_F2; 1.
DR Pfam; PF17887; Jak1_Phl; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PIRSF; PIRSF000636; TyrPK_Jak; 1.
DR PRINTS; PR01823; JANUSKINASE.
DR PRINTS; PR01824; JANUSKINASE1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW ECO:0000256|PIRSR:PIRSR000636-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000636};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000636}.
FT DOMAIN 23..405
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 424..512
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 568..842
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 862..1139
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 316..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 989
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT BINDING 868..876
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT BINDING 895
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1142 AA; 131684 MW; 8E4CB98BF279E081 CRC64;
MAFCAKMRNS KKLEVGIAAK DGLEICFYLP DKSTLYHLQG EFTAEDLCIE SALHCNISPL
CHNLFALYNE RSQSWYSPNH NFKIDSNVSL KLHYRMRFIF TNWHGTNENE PSVWRHYPKK
RDGYDKKQIQ EGTPLLDASS LDYLFAQGQY ELVKCLAPVR EPKNDQEVHE IENECLGMAV
LAISHYAIKR NIQLPDLPKD ISYKKYIPET LNRTIKQRNF LTRMRINNVF KNFLKEFNNK
TICDSSVSPH DLKVKYLSTM ETLTKNYGAE SFETNSLIIK SENEQNGFNI SDYDSMRRYE
VLVTGNSGIQ WRRKPTCTTS EKDRKLKRKK TESKSKNSDE KGKLKDEWNC FSYYPEITHI
AIKEDTVIIN NQDNKSMELK LSSQEEALSF AALIDGYFRL TADAHHYLCS DVAPPLIVNN
IKNGCHGPIC TEYAINKLRQ EGNEEGMYVL RWSCTDFNNI LMTVSCSKMS QFESKYVKQY
KNFQIEVKKG RYSLLGPDRG FDSLKDLMKH LKGQVLKTDD VSFTLKKCCP PKPREISNLL
VATKKALEWQ PVYHLSQLSF HRILKEEITQ LEHLGRGTRT QIYAGKLNYK DDNDSESYST
EKEIKVILKV LDPSHRDISL AFFETASMMR QVSHKHIVLL HGVCVRDVEN IMVEEFVDFG
PLDLFMHRKS EVLTTPWKFK VAKQLASALS YLEDKDLVHG NVCTKNILLA REGIDNDCGP
FIKLSDPGIP ITVLTRQERV ERIPWIAPEC VEDSRVLSVA ADKWSFGTTL WEICFNGEVP
LKDRTLAEKE RFYGGCFMLV APSCKELADL INQCMNYDPL RRPFFRAIMR EINKLEEQNP
DIVSEKTPSA EVDPTLFEKR FLKRVRDLGE GHFGKVELCR YDPEGDNTGE LVAVKSLKPG
TAGSHIADLK KEIEILRNLY HENIVKYKGI CEDGGSGIKL IMEYLPSGSL KEYLPRNVNK
INLKQQLKYA TQICKGMDYL GSRQYVHRDL AARNVLVENE QIIKIGDFGL TKAIETDKEY
YTVKDDLDSP VFWYAPECLL HCKFYIASDV WSFGVTLYEL LTYCNSEYSP MTMFLKMIGP
TQGQMTVTRL VRVLEEDKRL PIPANCPKQV YQLMLKCWEQ NPSHRTTFQD LIKGFEAIIN
TL
//
