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Database: UniProt
Entry: G1SQL4_RABIT
LinkDB: G1SQL4_RABIT
Original site: G1SQL4_RABIT 
ID   G1SQL4_RABIT            Unreviewed;      1151 AA.
AC   G1SQL4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   27-MAR-2024, entry version 77.
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:ENSOCUP00000005398.3};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000005398.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000005398.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000005398.3,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000005398.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000005398.3};
RG   Ensembl;
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   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004184}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. JAK subfamily. {ECO:0000256|PIRNR:PIRNR000636}.
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DR   EMBL; AAGW02002362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008263345.1; XM_008265123.2.
DR   AlphaFoldDB; G1SQL4; -.
DR   SMR; G1SQL4; -.
DR   STRING; 9986.ENSOCUP00000005398; -.
DR   PaxDb; 9986-ENSOCUP00000005398; -.
DR   Ensembl; ENSOCUT00000006236.4; ENSOCUP00000005398.3; ENSOCUG00000006227.4.
DR   GeneID; 100352594; -.
DR   KEGG; ocu:100352594; -.
DR   CTD; 3716; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000157092; -.
DR   HOGENOM; CLU_008155_1_0_1; -.
DR   InParanoid; G1SQL4; -.
DR   OMA; KDIMQGE; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF327041; -.
DR   Proteomes; UP000001811; Chromosome 13.
DR   Bgee; ENSOCUG00000006227; Expressed in upper lobe of left lung and 15 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
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:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0038154; P:interleukin-11-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0038110; P:interleukin-2-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0035771; P:interleukin-4-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0038113; P:interleukin-9-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0150105; P:protein localization to cell-cell junction; IEA:Ensembl.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0060337; P:type I interferon-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0060333; P:type II interferon-mediated signaling pathway; IEA:Ensembl.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13332; FERM_C_JAK1; 1.
DR   CDD; cd05077; PTK_Jak1_rpt1; 1.
DR   CDD; cd05079; PTKc_Jak1_rpt2; 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; IPR019748; FERM_central.
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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW   ECO:0000256|PIRSR:PIRSR000636-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
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          34..420
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          439..523
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          577..849
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          869..1151
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        997
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT   BINDING         875..883
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         902
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1151 AA;  133203 MW;  085351F4BF4B4D56 CRC64;
     MQYLNIKEDC NAMAFCAKMR SSKKTEVDLE APEPGVEVVF YLSDREPLRL GSGEYTAEEV
     CIRAAQECRI SPLCHNLFAL YDESTKLWYA PNRTITVDDK TSLRLHYRMR FYFTNWHGTN
     DSEQSVWRHS PKKQKNGYEK KKVPDATPLL DANSLEYLFA QGQYDLVKCL APIRDPKTEQ
     DGHDIENECL GMAVLAISHY AMMRKMQLPE LPKDISYKRY IPETLNKSIR QRNLLTRMRI
     NNVFKDFLKE FNNKTICDSS VSTHDLKVKY LATLETLTKH YGAEIFETSM LLISSENEMN
     WFHSSDSGIV LYYEVMVTGN LGIQWRQKPN VVPVEKEKSK LKRKKLENKL RKDEERNKTR
     EEWNNFSYFP EITHIVIKES VVSINKQDNK KMELKLSSHE EALSFVSLVD GYFRLTADAH
     HYLCTDVAPP LIVHNIQNGC HGPICTEYAI NKLRQEGNEE GMYVLRWSCT DFDNILMTVT
     CFEKSERQFK NFQIEVRKGC YSLHGSDRSF PSLGELMSHL KKQILRTDNI SFVLKRCCQP
     KPREISNLLV ATKKAQEWQP VYPMSQLSFD RILKKDIMQG EHLGRGTRTH IYAGTLVDHK
     DDEGTSEEKR IKVILKVLDP SHRDISLAFF EAASMMRQVS HKHIVYLYGV CVRDVENIMV
     EEFVEGGPLD LFMHRKSDLL TTPWKFKVAK QLASALSYLE DKDMVHGNVC TKNLLLAREG
     IDSECGPFIK LSDPGIPITV LSRQECIERI PWIAPECVED SKNLSVAADK WSFGTTLWEI
     CYNGEIPLKD KTLIEKERFY ESRCRPVTPS CKELADLMTR CMNYDPNQRP FFRAIMRDIN
     KLEEQNPDIV SERKPATEVD PTHFEKRFLK RIRDLGEGHF GKVELCRYDP EGDNTGEQVA
     VKSLKPESGG NHIADLKKEI EILRNLYHEN IVKYKGICTE DGGNGIKLIM EFLPSGSLKE
     YLPKNKNKIN LKQQLKYAVQ ICKGMDYLGS RQYVHRDLAA RNVLVESEHQ VKIGDFGLTK
     AIETDKEYYT VKDDRDSPVF WYAPECLIQC KFYIASDVWS FGVTLHELLT YCDSEYSPMA
     LFLKMIGPTH GQMTVTRLVN TLKEGKRLPC PPNCPDQVYQ LMRKCWEFQP SNRTTFQNLI
     EGFEAILKKH E
//
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