ID A0A1S3QW97_SALSA Unreviewed; 1055 AA.
AC A0A1S3QW97;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=LOC106596996 {ECO:0000313|RefSeq:XP_014043709.1};
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|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014043709.1};
RN [1] {ECO:0000313|RefSeq:XP_014043709.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014043709.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_014043709.1; XM_014188234.1.
DR AlphaFoldDB; A0A1S3QW97; -.
DR STRING; 8030.ENSSSAP00000044715; -.
DR KEGG; sasa:106596996; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000087266; Chromosome ssa03.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 1.
DR CDD; cd14274; UBA_ACK1; 1.
DR CDD; cd14328; UBA_TNK1; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR030220; Ack1_UBA_dom.
DR InterPro; IPR015116; Cdc42-bd-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021619; Mig-6.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR049587; TNK-like_SAM.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR14254; GENE 33 POLYPEPTIDE; 1.
DR PANTHER; PTHR14254:SF6; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF09027; GTPase_binding; 1.
DR Pfam; PF11555; Inhibitor_Mig-6; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR630220-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_014043709.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR630220-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 152..413
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..783
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-1"
FT BINDING 158..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1055 AA; 117394 MW; 804B54314206737F CRC64;
MGETAEYQRL DETSDYQRLP SVDEEKLGSS MQSEEGTEWL LELLMEVQLQ QYLLRIRDDL
NVTLLSHFDY VKNEDLEKIG MGRPGQRRLW EAVKKRKALC KRKSWMSKVF SGKRPDGGDF
QQAAPTTSFR KLSPTPPPQQ QALSCLISEK DLVLFQKLGE GSFGVVKRGE WFTPTGKVLE
VAVKCLKTDV LSQPDALDDF ICEVNAMHSL DHQNLIRLYG VVLTRPMKMV TELAPLGSLL
DHLRCVPTQS PVLIHTLCQY AMQVACGMAY LEQRRFIHRD LAARNILLAS ADTVKIGDFG
LMRALPNNHD HYVMQEHCKV PFAWCAPESL KTRTFSHATD TWMFGVTLWE MCTHGQEPWL
GLNGSQILHK IDKEGERLPK PEDCPQDLYN VMLQCWAQKP DDRPTFLALR EFLLETMPTD
MCALQDFEEA DKLQIQVDDV ITIIEGSFPD RIDDLYLGNP MDPPDVLGLD LNAARPTQLL
GRAKKPCYDS VTEDEELTAS GLKRLSLRKA GSILKLKPAA WVSASKQGER TTGSGHTPSK
VSLIDFEEEF PPATPSPSPV AELQLPSLVK LAMEAESILD RTPPQSPWCS LPCPLHPTPV
VDWDARPLPP PPAYDDVAQD EEDMEVSSIN SLEQRQQGGM GASHSSTEVI PAGEEGKPLE
DNLFLPSQQG QGYTSFSQSA EIFQELQQEC MRRLNVPTGG VPQPPSPSPS LGLQSIDVHR
HIVLSFSEDK PQIPPRIPIP PRPVKRGDYT RWSGDLSLSP TPAPEEVQDR PPQIPPRNPL
SQPGSRTPSP MGLLVGSPQQ RTMVCPSAPP PATYGSYLST SPGKIMPTTH SFASDPKYAA
LKVIQAQAQG KDLAKGPCIL PIVRDGRKVS NTHYYLLPER PPYLDRYDRF FREAENVPIG
GGGGICEERQ QANTAMVRPM VVNQQQQSKG GDVKANFSNN NSSLGCRPGM KASLSLPRVS
SEGSASRAAG GTTTDQVKMV QEAVHGVTVE ECQTALQNHN WNMQKAVHYL KVEQLFCLGL
KTRLECLKML EMYNWNLEVA STQLLDSYSS VTQRR
//
