ID A0A087YEX2_POEFO Unreviewed; 1374 AA.
AC A0A087YEX2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016575.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016575.2}
RP IDENTIFICATION.
RG Ensembl;
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=2.7.10.1;
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}.
CC -!- SIMILARITY: Belongs to the plexin family.
CC {ECO:0000256|ARBA:ARBA00010297}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR EMBL; AYCK01000411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007550970.1; XM_007550908.2.
DR STRING; 48698.ENSPFOP00000016575; -.
DR Ensembl; ENSPFOT00000016597.2; ENSPFOP00000016575.2; ENSPFOG00000016463.2.
DR GeneID; 103137246; -.
DR KEGG; pfor:103137246; -.
DR eggNOG; KOG1095; Eukaryota.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT00940000157842; -.
DR OMA; WIQTQTA; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0007411; P:axon guidance; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00603; IPT_PCSR; 1.
DR CDD; cd01179; IPT_plexin_repeat2; 1.
DR CDD; cd05058; PTKc_Met_Ron; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR24416:SF614; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF81296; E set domains; 3.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF101912; Sema domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000617-
KW 2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000617-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000617-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1374
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001834403"
FT TRANSMEM 942..968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..505
FT /note="Sema"
FT /evidence="ECO:0000259|PROSITE:PS51004"
FT DOMAIN 1064..1327
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1351..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1190
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-1"
FT BINDING 1070..1078
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1096
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1143..1146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT BINDING 1194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT MOD_RES 1220
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1221
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1335
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT MOD_RES 1342
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT DISULFID 98..101
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 133..141
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 167..170
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 293..358
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 510..528
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 516..550
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 519..535
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT DISULFID 531..541
FT /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
SQ SEQUENCE 1374 AA; 153183 MW; 77BA160BDDE6875B CRC64;
MVTATALLAI CIWIQAQIAS GQETCPPLHR GLVNFSVEYS LPTFQTNTVI QNIVVNKELE
ETEVYLGCQN AIVAVNDSMG EKWELKTGPI GSPDCETCPV CDIETDPEDP VDTDNTVLVL
DPAAYLYPYL YICGSTQYGI CYRIDFSQPK LRPTCFYKRK QNSVTDCPDC IGSPLGTKVT
VVEDSDAALL FVAASVNDKV VEKYPRRSIS VLRPLSTEDG FLKIMDGLTV LPTLRNSYKI
DYIYSFSTEE FVYFLSLQRE DPFRNNSAFQ THLGRLPIST PEVWMYREVV LECRYEPKRR
KRSDYKDVVY NGLQAAHFGH AGKDFAEELR VDKNDNILYG VFTEVKVQGE RQATSALCAF
PLKKINDAID MGVEACCTSG PEQLSRGLCH FQPCESCLHE KSEGNYTCKH QATLVSKPHY
RLDIFNRRMR DVLFTSVLVS VIENHTIGHF GTSDGRILQM ILTLHNPIVF ANYSLGEVAI
SRTAAVYSED SLIFTAGNKM FKVPTTGPGC DHFLTCPVCL TAPRFMNCGW CSGKCSRKSE
CTSGWNKDSC APILTQFFPK TAPAGGETEV TLCGSEFLSR QSAIISGGIH VVRVDSGALC
AVLPNKSNIT VLVCQINEKI PHQNMNITLE IHKKEEEGYY SIEGTVQMSG FSVVEPSITD
IKPSHGPMFG GTTVTVLGKH LYSGNQRHVL FADRKCTLVP SDPKETGDLS PIICNTPPAE
SVGEVPVKVI IDNLEVTTAK TFFYKENPVI TSIYPHCSFR SGSNLVIRGQ NLDSGHKVVV
QYTPKNSQFS LQQDCNSSRN ATYLECQTPA FSAQTAEDKF NAGTISILID GQNIFNKTKF
NYHADANIIP LEKEDNVSLL KPGGHEVSLH HDKLQSVNKC MKIIMSIGNE PCKHIVLLNE
LTCRIPNGLD FPSNGLPLKV SVNGKDLYVG RVIYDKTNNS TVIAGIVLGI ITALVVGAGL
ALFVMRYLRK KDRAIIDRNL TMVPRNRMNN QTDPFPTSDY RYSHPVSQTS GSGGMAFQGL
TYASSYDHLA IPLMSRDNVS VVSSNPELLE EVKDVLIPAD RLRIEEGQII GKGHFGTVYH
GYLLDSSKQE IHCAVKSLNR ITDLGEVDQF LREGIIMKAF HHPNILSLLG IMLPKEGLPL
VVLPYMKHGD LRHFIRSEQR NPTVKDLIGF GLQVAMGMEY LTQKKFVHRD LAARNCMLDE
TFTVKVADFG MARDVYDKEY YSIQNHKRAK LPVKWMAIES LQTQKFTTKS DVWSYGILMW
ELITRGASPY PDVDPYDITH YLMKGRRLPQ PQYCPDPLYS IMLACWDPEP ECRPSFHSLV
AEVDEILSGL EGEHYINLKV TYINLDQPRP YPPLSGSADE AEASDLDSDD HSAS
//
