JAK1_DANRE
ID JAK1_DANRE Reviewed; 1153 AA.
AC O12990; O73880;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Tyrosine-protein kinase JAK1;
DE EC=2.7.10.2;
DE AltName: Full=Janus kinase 1;
DE Short=JAK-1;
GN Name=jak1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, MUTAGENESIS OF LYS-905,
RP AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=9096349; DOI=10.1073/pnas.94.7.3082;
RA Conway G., Margoliath A., Wong-Madden S., Roberts R.J., Gilbert W.;
RT "Jak1 kinase is required for cell migrations and anterior specification in
RT zebrafish embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3082-3087(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 443-1153.
RC TISSUE=Embryo;
RX PubMed=10515866;
RA Oates A.C., Brownlie A., Pratt S.J., Irvine D.V., Liao E.C., Paw B.H.,
RA Dorian K.J., Johnson S.L., Postlethwait J.H., Zon L.I., Wilks A.F.;
RT "Gene duplication of zebrafish JAK2 homologs is accompanied by divergent
RT embryonic expression patterns: only jak2a is expressed during
RT erythropoiesis.";
RL Blood 94:2622-2636(1999).
CC -!- FUNCTION: Tyrosine kinase of the non-receptor type. Appears to be
CC required in early development for specific cell migrations (epiboly),
CC expression of homeobox protein goosecoid and formation of anterior
CC structures. {ECO:0000269|PubMed:9096349}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely
CC to be the in vivo cofactor. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Wholly intracellular, possibly
CC membrane associated. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Present in the unfertilized egg through to the
CC blastula stage where it is distributed uniformly. Levels drop rapidly
CC at four hours development, remain very low until 10 hours, then
CC gradually increase from 12 hours with a rapid increase at 48 hours. At
CC 48 hours it is concentrated in the region of the gill arches. Also
CC present in the adult. {ECO:0000269|PubMed:9096349}.
CC -!- DOMAIN: Possesses two phosphotransferase domains. The second one
CC probably contains the catalytic domain, while the presence of slight
CC differences suggest a different role for domain 1.
CC -!- DOMAIN: The protein kinase 1 domain is also called the pseudokinase
CC domain and has a regulatory role through the transactivation of other
CC JAK kinases associated with signaling receptors.
CC {ECO:0000250|UniProtKB:P23458}.
CC -!- DOMAIN: The protein kinase 2 domain is the catalytically active domain.
CC {ECO:0000250|UniProtKB:P23458}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. JAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U82980; AAB54114.1; -; mRNA.
DR EMBL; AJ005689; CAA06673.1; -; mRNA.
DR AlphaFoldDB; O12990; -.
DR SMR; O12990; -.
DR STRING; 7955.ENSDARP00000037399; -.
DR PaxDb; O12990; -.
DR PRIDE; O12990; -.
DR ZFIN; ZDB-GENE-980526-142; jak1.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; O12990; -.
DR BRENDA; 2.7.10.2; 928.
DR Reactome; R-DRE-1059683; Interleukin-6 signaling.
DR Reactome; R-DRE-110056; MAPK3 (ERK1) activation.
DR Reactome; R-DRE-112411; MAPK1 (ERK2) activation.
DR Reactome; R-DRE-1266695; Interleukin-7 signaling.
DR Reactome; R-DRE-6783783; Interleukin-10 signaling.
DR Reactome; R-DRE-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-DRE-6788467; IL-6-type cytokine receptor ligand interactions.
DR Reactome; R-DRE-877300; Interferon gamma signaling.
DR Reactome; R-DRE-877312; Regulation of IFNG signaling.
DR Reactome; R-DRE-8854691; Interleukin-20 family signaling.
DR Reactome; R-DRE-8983432; Interleukin-15 signaling.
DR Reactome; R-DRE-8984722; Interleukin-35 Signalling.
DR Reactome; R-DRE-8985947; Interleukin-9 signaling.
DR Reactome; R-DRE-9020558; Interleukin-2 signaling.
DR Reactome; R-DRE-9020591; Interleukin-12 signaling.
DR Reactome; R-DRE-9020956; Interleukin-27 signaling.
DR Reactome; R-DRE-9020958; Interleukin-21 signaling.
DR Reactome; R-DRE-909733; Interferon alpha/beta signaling.
DR Reactome; R-DRE-912526; Interleukin receptor SHC signaling.
DR Reactome; R-DRE-912694; Regulation of IFNA/IFNB signaling.
DR Reactome; R-DRE-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-DRE-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR SignaLink; O12990; -.
DR ChiTaRS; jak1; zebrafish.
DR PRO; PR:O12990; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005126; F:cytokine receptor binding; IBA:GO_Central.
DR GO; GO:0005131; F:growth hormone receptor binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:ZFIN.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IBA:GO_Central.
DR Gene3D; 3.30.505.10; -; 1.
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 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; SH2 domain; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..1153
FT /note="Tyrosine-protein kinase JAK1"
FT /id="PRO_0000088110"
FT DOMAIN 32..416
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 435..540
FT /note="SH2; atypical"
FT DOMAIN 580..846
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 872..1150
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1000
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 878..886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 905
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 1031
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1032
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MUTAGEN 905
FT /note="K->E: Loss of autophosphorylation and defects in
FT early development."
FT /evidence="ECO:0000269|PubMed:9096349"
FT CONFLICT 649
FT /note="T -> I (in Ref. 2; CAA06673)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="T -> S (in Ref. 2; CAA06673)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="S -> T (in Ref. 2; CAA06673)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="H -> L (in Ref. 2; CAA06673)"
FT /evidence="ECO:0000305"
FT CONFLICT 1111
FT /note="L -> I (in Ref. 2; CAA06673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1153 AA; 132481 MW; 736D5263D03E7450 CRC64;
MPELAVMDLG RQLCVKMKKQ RKAEMTIPTA MKGLEIHFYL ADTHQLEFFK ACYTAEDLCV
EAAKRCRISP LCHNLFALYE ESQDLWYAPN HVFKVTDETS IKLHYRMRFY FTNWHGTSEI
ESPVWRHTLS KQKSVLNSQK TTEGTPLLDA ASLDYLFAQG QYDFLRGLSP VRPTQTDEEH
HEIENECLGM AVLAITHHAK SNNLPLSGAG AETSYKRFIP DSLNRTIKQR NFLTRIRISN
VFKNFLNEFN SKTIQDSNIG LYDLKVKYLS TLETLTQGVG REIFKPKNLK VTGESEGSPA
QMLPLGDNGM GYEVQVYGTT GISWRRKPAP NQLILKDKPK SKKIKGDKQW NDKKKDSGWT
LFSDFHEITH IVIKDCCVTI YRQDNKTMEL DLFYRDAALS FAALVDGYFR LTVDAHHYLC
TDVAPSSVVQ NLENGCHGPI CTEYAIHKLR QEGNEEGTYV LRWSCTEYNF IIMTVVCIEL
DLCESRPVPQ YKNFQIETSP QGYRLYGTDT FRPTLKELLE HLQGQLLRTD NLRFQLRRCC
PPQPREISNL LVMTTDREPV PQKKTQVSQL SFDRILKEEI VQGEHLGRGT RTNIYAGILK
PKSDDEDDLG GYSQEVKVVL KVLGSGHRDI SLAFFETASM MRQISHKHTA LLYGVCVRHQ
ENIMVEEFVQ YGPLDLFMRR QTTPLSTAWK FQVAKQLASA LSYLEDKKMV HGYVCSKNIL
VARDGLDGEG GPFIKLSDPG IPITVLSREE CVDRIPWIAP ECVKDTANLT IAADKWSFGT
TLWEICYNGE IPLKDKKLSE KERFYAAQCQ LATPDCDELA KLMTHCMTYD PRQRLFFRAI
VRDIVMVEKQ NPSIQPVPML EVDPTVFEKR FLKKIRDLGE GHFGKVELCR YDPRGDRTGE
LVAVKSLKPE NREEQSNNLW REIHILRELY HENIVKYKGI CNEEGGRSIK LIMEFLPAGS
LKEYLPRNKA HINLKTLHNY SVQICQGMDY LGSRNYIHRD LAARNVLVEN EGTVKIGDFG
LTKSIKDNEG YYTVKDDLDS PVFWYAPECL IHCKFYRASD VWSFGVTMYE LLTYCDASCS
PMSVFLKLIG PTHGQMTVTR LVKVLEEGKR LPRPDDCSEQ LYNLMRRCWE ATPEKRIDFK
SLIANFQQML DNL
