ID A0A1S3LCP0_SALSA Unreviewed; 1512 AA.
AC A0A1S3LCP0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=LOC106565537 {ECO:0000313|RefSeq:XP_013988254.1};
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_013988254.1};
RN [1] {ECO:0000313|RefSeq:XP_013988254.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013988254.1};
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=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR RefSeq; XP_013988254.1; XM_014132779.1.
DR GeneID; 106565537; -.
DR KEGG; sasa:106565537; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000087266; Chromosome ssa12.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00064; FU; 3.
DR CDD; cd12095; TM_ErbB3; 1.
DR Gene3D; 6.10.250.2930; -; 1.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR044912; Egfr_JX_dom.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF88; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_013988254.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_013988254.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 711..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 779..1036
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 812
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1512 AA; 168450 MW; E2E594660EF474DC CRC64;
MSPVSRPPPP SPPSHRWPYG IQGEMPPECS TSGSGFQYLG DWEGNGPKKR CWVPAKDILD
LALITDFYRQ HPGQPGMRPG RTPGGAPRVI CSGTQNALSV TGSSQTQYTL MKDMYSGCEI
VMGNLEITMM EHWRDFTFLQ SIREVTGYIL IAINQFSRLP LDQLRIIRGT TLFEERFALA
VLVNYQKDGQ HGLEELGLTH LTEILEGGVQ IVQNKFLSYT PQVNWLDIVK DGASEVIINE
NGPEQPCDEA CAGPCWGSRN DTCQILTKTV CAPQCNGRCF GRSPSECCHM ECAGGCTGPL
DTDCFACRNF NNSGSCVPQC PQTLIYNKHT FKLEPNPSAK YQYGSICVAQ CPTNFVVDGS
SCVSSCPSYK TEVEKKGVKR CEPCGGLCPK ACQGTGTASR QTVDSQNIDS FINCTKIQGS
LHFLVTGIKG DPYNNIAALD PEKLKIFRTV REITDILSIQ SWPETLTDLS VFSNLTTIQG
RTLYRGRSKR GYSLLVMRIP SLTSLGLRSL RRINDGGVYI TGNKKLCYHH TVNWTRLFSS
SSRPQRRQKN IDVKENRLQS QCVEEGHMCD PLCSLEGCWG PGPDQCQSCK DYSRGGTCVH
QCRFLTGEGR EFAGPKGECM PCHSECEVQE GRLTCTGPGA NKCVVCASLR DGPHCVSSCP
EGVMGEKGLI FKYPNQQRRC EPCHLNCTQG CSGPGIGDCL DSSRLTTSQP IIGIVLGVLA
VVIVGISIFV MSVLYRRGLA IRRKRAMRRY LASGESLEPL DPGEKGVKVH ARILKVRELR
KIKLLGTGVF GSIHKGIWIP EGDSVKIPVA IKTIHDRTGR QTFHEITDHM LAMGSLDHQY
IVRLLGICPG ASLQLVTQLS TQGSLLEHIR HYRDSLDPQR LLNWCVQIAK GMYYLEEHRM
VHRNLAARNV LLKSDYMVQI SDYGIADLLY PDDKKYFYNE VKTPIKWMAL ESILFRRYTH
QSDVWSYGVT VWEMMSYGAE PYSTMRPQEV PDLLEKGERL SQPHICTIDV YMVMVKCWMI
DENVRPTFKE LANEFTRMAR DPPRYLVIKG DCSPSDSPSD ESHHRVTELD HMEAGLEDQD
EERLGDGMAT PPLYLSQARS FSRLSRMESH RGVHSSQAGY LPMTPGLDNS QMVWPPASRS
RLNSARTVSE SSEGRGTLVE LEMSEDLAGS LQRKRHREDS AYMSQRDSMS GVLSETPSPD
TEGEEDQNGY VLPGLGDSPE RDTLLSSSRV TLPHGRTSKV PSYPSGPSED NDSACEEYEY
MNKQAFMMTL SPRQQPGHSK DGQWLKMNKR QRSSLPSLDT EYTECTGHRT SAGENRGGQT
KNEELQDYEF PALNSDSDKI EESGSGDVEY EYMDIRSVGP EASERPDDPP TRVVPHPGAT
PKQRMRGERK VEEVDNEYVE EDDYHYTNRQ PKLRQALRSR EGLRMQRGGE GEVDEYEDMD
SLAAPGAGDP VEYENLQGEG EGVVRAIGGQ RTGMGAFVKV RAGVGVGEPG GDCSFDNPDY
WQSRLFLKPV ST
//
