JAK1_CYPCA
ID JAK1_CYPCA Reviewed; 1156 AA.
AC Q09178;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8892755; DOI=10.1089/dna.1996.15.827;
RA Chang M.S., Chang G.D., Leu J.H., Huang F.L., Chou C.K., Huang C.J.,
RA Lo T.B.;
RT "Expression, characterization, and genomic structure of carp JAK1 kinase
RT gene.";
RL DNA Cell Biol. 15:827-844(1996).
CC -!- FUNCTION: Tyrosine kinase of the non-receptor type.
CC {ECO:0000250|UniProtKB:O12990}.
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 -!- 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; L24895; AAB38157.1; -; mRNA.
DR EMBL; U53694; AAB38256.1; -; Genomic_DNA.
DR EMBL; U53686; AAB38256.1; JOINED; Genomic_DNA.
DR EMBL; U53687; AAB38256.1; JOINED; Genomic_DNA.
DR EMBL; U53688; AAB38256.1; JOINED; Genomic_DNA.
DR EMBL; U53689; AAB38256.1; JOINED; Genomic_DNA.
DR EMBL; U53690; AAB38256.1; JOINED; Genomic_DNA.
DR EMBL; U53691; AAB38256.1; JOINED; Genomic_DNA.
DR EMBL; U53692; AAB38256.1; JOINED; Genomic_DNA.
DR EMBL; U53693; AAB38256.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q09178; -.
DR SMR; Q09178; -.
DR BRENDA; 2.7.10.2; 1195.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; SH2 domain;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..1156
FT /note="Tyrosine-protein kinase JAK1"
FT /id="PRO_0000088111"
FT DOMAIN 32..419
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 438..543
FT /note="SH2; atypical"
FT DOMAIN 583..857
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 875..1153
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1003
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 881..889
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1034
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1035
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1156 AA; 132246 MW; FF54BDDD2F9666F5 CRC64;
MPELAVMELG RQLCGKMKKQ RKAEMTVLTV MKGLEIHFYL PDTHQLEYFK DCHTAEDLCV
EGCQEDATSH LCADNLFALS EESQDLWYAP NHAFKITEET SIKLHYRMRF YFTNWHAPVR
TESPVWRHSL FKHKGVSVSP KGPEGTPLLD AASLEYLFAQ GQYDFLRGLA PVRAPQNEAE
KHEIENECLG MAVLAITHHA KSNDLPLSGV GAETSYKRFI PDSLNRTIKQ RNFSHVYVYN
NVFKNFLNEF NSKTIQDSNI TLYDLKVKYL STLETLTQGL GRETIEPKIL KVSGESDGSP
ALTLPSGDDG LGYEVQVSGT TGISWRRKPV PNILIVKDKT KSKKNKADKQ SKKEMTKRKT
VMTIFSDFFE ITHIVIKESC ATIYSQDNKT MELDLFYRDA ALSFAALVDG YFRLTVDAHH
YLCTEVAPSS VVQNLENGCH GPICTEYAIH KLRQEGNEEG TYVLRWSCTD YNYIIMTVVC
IEMDLCESRP VPQYKNFQIE TSPQGYRLYG TDTFRPTLKE LLEHLQGQNL RTENLRFQPV
LVGLGQPRKI SNLLVMTRDR EPDSQRQPQV SQLSFHRILK EEIVQGEHLG RGTRTNIYSG
VLKLKSEDDD DMGGYSQEVK VILKVLGSGH RDISLAFFET ASMMRQISHK HIALLYGVCV
RHQENIMVEE FVQYGPLDLF MRRQSIPLST AWKFQVAKQL AGALSYLEDK KLVHGNVCSK
NILVARDGLD GEGGPFIKLS DPGIPITVLS REECVDRLPW IAPECVQDTA NLSIAADKWG
FGTTLWEICY NGEIPLKDKK LTEKERFYAA QCQLASPDCE ELAKLMTHCM TYDPRQRLFF
RAIVRDIDMV EKQNPSIQPV PMLEVDPTVF EKRFLKKIRD LGEGHFGKVE LCRYDPRGDR
TGELVAVKSL KPENREEQSS NLWREIHILR ELYHENIVKY KGIWHEEGGR SIKLIMEFLP
AGSLKEYLPR NKAHIDLKTL LNYAVQICQG MDLLASRNYI HRDLAARNVL VENENTVKIG
DFGLTKSIKD NEGYYTVKDD LDSPVFWYAP ECLIHCKFYR ASDVWSFGVT MYELLTYCDI
SCSPMSVFLT MIGPTHGQMT VTRLVKVLEE GKRLPKPDGC SDRLYCLMRR CWEATPEKRI
DFKGLIANFQ QMIDNQ
