ID S5RRC4_SALSA Unreviewed; 1176 AA.
AC S5RRC4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=LOC106601287 {ECO:0000313|RefSeq:XP_014048861.1,
GN ECO:0000313|RefSeq:XP_014048862.1};
GN Synonyms=LOC106597276 {ECO:0000313|RefSeq:XP_014043958.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:AGS07433.1};
RN [1] {ECO:0000313|EMBL:AGS07433.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23872231; DOI=10.1016/j.dci.2013.07.008;
RA Sobhkhez M., Hansen T., Iliev D.B., Skjesol A., Jorgensen J.B.;
RT "The Atlantic salmon protein tyrosine kinase Tyk2: molecular cloning,
RT modulation of expression and function.";
RL Dev. Comp. Immunol. 41:553-563(2013).
RN [2] {ECO:0000313|RefSeq:XP_014043958.1, ECO:0000313|RefSeq:XP_014048861.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014048861.1,
RC ECO:0000313|RefSeq:XP_014048862.1};
RG RefSeq;
RL Submitted (SEP-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; KF021282; AGS07433.1; -; mRNA.
DR RefSeq; XP_014043958.1; XM_014188483.1.
DR RefSeq; XP_014048861.1; XM_014193386.1.
DR RefSeq; XP_014048862.1; XM_014193387.1.
DR STRING; 8030.ENSSSAP00000032281; -.
DR PaxDb; 8030-ENSSSAP00000032281; -.
DR GeneID; 106601287; -.
DR KEGG; sasa:106597276; -.
DR KEGG; sasa:106601287; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000087266; Chromosome ssa03.
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:0097677; F:STAT family protein binding; IPI:AgBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IMP:AgBase.
DR CDD; cd14473; FERM_B-lobe; 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; IPR016045; Tyr_kinase_non-rcpt_TYK2_N.
DR PANTHER; PTHR45807:SF6; NON-RECEPTOR TYROSINE-PROTEIN KINASE TYK2; 1.
DR PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 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; PR00109; TYRKINASE.
DR PRINTS; PR01827; YKINASETYK2.
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.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW ECO:0000256|PIRSR:PIRSR000636-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|EMBL:AGS07433.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999};
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 26..421
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 584..865
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 884..1169
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1010
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT BINDING 890..898
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT BINDING 917
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1176 AA; 133455 MW; 7C2ADCA4180BEA9C CRC64;
MMSRSGRFKS TRTGSSTGQC EPPQGPGVHV YLFWTKGGER YLTHTEGKVT AEELSISAAQ
TVGITPLCHV LFSLYDPESH CWYSPNHFFN SEEQTRLTLH YRMRFYFRNW HGLSEKEPSV
VRYAPRSGTE HGGSPLLEMT SLEYLFCQAK FDFVNDVTPM EDAQGKEELS RFKNESLGMA
VLHLSHQALR SGCTLQEVAK SVSFLRCIPR SFAKHIARDN FLTKIRIRRV FADFVRTFQE
HTVDVGRLGS QEVMYKYLST LEHLAPRFGT ETFLAAHLEL RTDGGDGSGS YLNTSRAHGA
SDPENVGPQV MHEVMVSGTK GIQWRKMTVQ KPQANSYFGN DYLGNRKSVK QSPLQQEPTS
SDTWTSFCDF PEISHITITG ANVSIIKQDN FSMEVQMNSS LEALSFVSLL DGYFRLTADA
HHYLCHEVAP PRVVLSATNG LHGPMNDDFV LQRLRKEAVE EGAFLVRWSV LDYHRIILAV
LNKSQNGQAA IHKQFRILHS GSVFALEGWD REFSSVKELT DSLKAFVLKS GTDNFTVKKC
CLPRPAELSN LLVMRQGVDQ CVQPDSVALC LTQLKFHQIK DKEITQEQHL GRGTRTNIYS
GRLLVWGGAE EDEEDKWNNN LTDRKEIRVV LKILDQSHKD IALAFFETAS LMSQVSHSHL
VFVHGVSVKG SENIMVEEFV EFGPLDVFLR RERALVTPQW KFTVAKQLAS ALSYLETKQL
VHGNVCGKNI LVARRGLEEG TFPFVKLSDP GIALNVLSRE ERVERIPWIA PECVPSSAPF
GRAADQWSFG ATLLEICNNG DLPMSGSTLT EKERFYETRS RLTEPSSQEL ASFISMCLTY
EPRERPSFRT VLRELTELQL KNPDISPLES LPDADPNVFL KRYLKKIRDL GEGHFGKVML
YVYDPANDGT GDYVAVKALK HEGGSHLHEG WMKEIEILKS LYHSNIVKYK GCCSELGGQT
VQLIMEFLPL GSLREYLVKH RLGVAHSLLF AQQICQGMDY LHSKRYIHRD LAARNVLVEN
EHLVKIGDFG LTKYIPEGDV YYRVREDGDS PVYWYAIECL KESKFSFSSD IWSFGVTLYE
VLTHGDHRQS PPVKFTQMMG NVHGQMTVMV LVKLLEKHNR LPCPRDCPSE VHMLMQHCWD
FDPARRPSFK SLIESIGAIR KTYERQPNMR LAQISQ
//