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Database: UniProt
Entry: A0A1S3WAF8_ERIEU
LinkDB: A0A1S3WAF8_ERIEU
Original site: A0A1S3WAF8_ERIEU 
ID   A0A1S3WAF8_ERIEU        Unreviewed;      1153 AA.
AC   A0A1S3WAF8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
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|RefSeq:XP_016043381.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016043381.1};
RN   [1] {ECO:0000313|RefSeq:XP_016043381.1}
RP   IDENTIFICATION.
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   -!- 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   RefSeq; XP_016043381.1; XM_016187895.1.
DR   AlphaFoldDB; A0A1S3WAF8; -.
DR   STRING; 9365.ENSEEUP00000010416; -.
DR   CTD; 3716; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   InParanoid; A0A1S3WAF8; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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:0019221; P:cytokine-mediated signaling pathway; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:UP000079721};
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..528
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          582..854
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          874..1152
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          335..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1002
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT   BINDING         880..888
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         907
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1153 AA;  132804 MW;  6F2DCBA54E1EA9F5 CRC64;
     MQYLNIKEDC NAMAFCAKMR SSKKTEVNPE APEPGVEVFF YLPDKEPLRL GNGDYTAEEL
     CVKAAQKCSI SPLCHNLFAL YDDSTKLWYA PNRTITVDDK TCLRLHYRMR FYFTNWHGTN
     ENEQSVWRHS PKKQKNGYEK KKVPDATPLL DASSLEYLFA QGQYDLVKCL APIRDPKTEQ
     DGHDIENECL GMAVLAISHY AMIKKVQLPE LPKDISYKRY IPETLNKSIR QRNLLTRMRI
     NNVFKDFLKE FNNKTICDSS VSTHDLKVKY LATLETLTKH YGAEIFETSM LLISAENEMS
     RLYPSDSGST LCYEVMVTGN LGIQWRQKQN VVPVEKEKNK LKRKKQEGKH KKDEEKNKAR
     EEWNNFSYFP EITHIVIKES LVSINKQDQK KMELKLSSHE EALSFVSLVD GYFRLTADAH
     HYLCTDVAPP LIVHNIQNGC HGPICTEYAI NKLRQEGSEE GLYVLRWSCT DFDNILMTVT
     CFEKPEVLGG QKQFKNFQIE VQKGHYSLHG SERSFPSLGD LMDHLKKQIL RTDNISFVLK
     RCCQPKPREI SNLLVATKKA QEWQPVYPMS QLSFCRILKK DIIQGEHLGR GTRTHIYSGT
     LLDYKDDEGM AEEKRIKVIL KVLDPSHRDI SLAFFEAASM MRQVSHKHIV YLYGVCVRDV
     ENIMVEEFVE GGPLDLFMHR KSDALTTPWK FKVAKQLASA LSYLEDKDLV HGNVCTKNLL
     LARAGIDSEC GPFIKLSDPG IPITVLSRQE CLERIPWIAP ECVEDSKNLS VAADKWSFGT
     TLWEICYNGE IPLKDKTLIE KERFYESRCR PVTPSCKELA DLMTRCMNYD PNQRPFFRAI
     MRDINKLEEQ NPDIVSEKKP ATEVDPTHFE KRFLKRIRDL GEGHFGKVEL CRYDPEGDNT
     GEQVAVKSLK PESGGNHIAD LKKEIEILRN LYHENIVKYK GICTEDGGNG IKLIMEFLPS
     GSLKEYLPKN KNKINLKQQL KYAVQICKGM DYLGSRQYVH RDLAARNVLV ESEHQVKIGD
     FGLTKAIETD KEYYTVKDDR DSPVFWYAPE CLIQCKFYIA SDVWSFGVTL HELLTYCDSD
     SSPMALFLKM IGPTHGQMTV TRLVNTLREG KRLPCPPNCP DEVYQLMRNC WDFQPSSRTT
     FQNLIERFEA LLK
//
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