ID G3SSY6_LOXAF Unreviewed; 1154 AA.
AC G3SSY6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:ENSLAFP00000003110.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000003110.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000003110.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003110.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000003110.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003110.4};
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 AlphaFoldDB; G3SSY6; -.
DR Ensembl; ENSLAFT00000003730.4; ENSLAFP00000003110.4; ENSLAFG00000003730.4.
DR GeneTree; ENSGT00940000157092; -.
DR HOGENOM; CLU_008155_1_0_1; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; 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; 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:UP000007646};
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..417
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 436..525
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 579..853
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 875..1153
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 1003
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT BINDING 879..889
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT BINDING 908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
SQ SEQUENCE 1154 AA; 133134 MW; 16292AB87694122F CRC64;
LQYLNIKEDC NAMAFCAKMR SSKKTEVNLE APEPGVEVIF YLPDREPLRL SSGEYTAEDL
CIKAAQECCI SPLCHNLFAL YDENTKLWYA PNRTITVDDK TSLRLHYRMR RFYFTNWHGT
NDREHFLGSF MPSFVEKQFG ARGTVNLINL IAVLLFLVGQ YDLVKCLAPI RDPKTEQDGH
DIENECLGMA VLAISHYAMM KKMQLPELPK DISYKRYIPE TLNKSIRQRN LLTRMRINNV
FKDFLKEFNN KTICDSSVST HDLKVKYLAT LETLTKHYGA EIFETSMLLI SSENEMNRFH
SNDSGNILYY EVMVTGNLGI QWRQKPNVLP VEKEKNKLKR KKLENKHKKD EEKNKIREEW
NNFSYFPEIT HIVIKESVVS INKQDNKKME LKLSSHEEAL SFVSLVDGYF RLTADAHHYL
CTDVAPPLIV HNIENGCHGP ICTEYAINKL RQEGSEEGMY VLRWSCTDFD NILMTVTCFE
KTEVLGGQKQ FKNFQIEVQK GHYSLHGSDR SFPTLGELMG HLKKQILRTD NISFVLKRCC
QPKPREISNL LVATKKAQEW QPVYTMSQLS FDRILKKDIM QGEHLGRGTR THIYSGTLMD
YKDDEGTSEE KRIKVILKVL DPSHRDISLA SAFFEAASMM RQVSHKHIVY LYGVCVRDVE
NIMVEEFVEG GPLDLFMHRR SDALTTPWKF KVAKQLASAL SYLEDKDLVH GNVCTKNLLL
AREGIDSECG PFIKLSDPGI PITVLTRQEC IERIPWIAPE CVEDSKNLSV AADKWSFGTT
LWEICYNGEI PLKDKTLIEK ERFYESRCRP VTPSCKELAD LMTHCMNYDP NQRPFFRAIM
RDINKLEEQN PDIVSERKPA TEVDPTHFEK RFLKRIRDLG EARGHFGKVE LCRYDPEGDN
TGEQVAVKSL KPESGGNHIA DLKKEIEILR NLYHENIVKY KGICTEDGGN GIKLIMEFLP
SGSLKEYLPK NKNKINLKQQ LKYAVQICKG MDYLGSRQYV HRDLAARNVL VESEHQVKIG
DFGLTKAIET DKEYYTVKDD RDSPVFWYAP ECLIQCKFYI ASDVWSFGVT LHELLTYCDS
DSSPMALFLK MIGPTHGQMT VTRLVNTLKE GKRLPCPPNC PDEVYHLMRK CWEFQPSNRT
TFQNLIEGFE ALLK
//
