ID A0A3P9N1G7_POERE Unreviewed; 1118 AA.
AC A0A3P9N1G7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Proto-oncogene tyrosine-protein kinase receptor Ret {ECO:0000256|PIRNR:PIRNR000631};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000631};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000003385.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000003385.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000003385.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Receptor tyrosine-protein kinase involved in numerous
CC cellular mechanisms including cell proliferation, neuronal navigation,
CC cell migration, and cell differentiation upon binding with glial cell
CC derived neurotrophic factor family ligands.
CC {ECO:0000256|PIRNR:PIRNR000631}.
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 ECO:0000256|PIRNR:PIRNR000631};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR000631}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000631}.
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DR RefSeq; XP_008428251.1; XM_008430029.2.
DR RefSeq; XP_017164479.1; XM_017308990.1.
DR RefSeq; XP_017164480.1; XM_017308991.1.
DR RefSeq; XP_017164481.1; XM_017308992.1.
DR AlphaFoldDB; A0A3P9N1G7; -.
DR STRING; 8081.ENSPREP00000003385; -.
DR Ensembl; ENSPRET00000003439.1; ENSPREP00000003385.1; ENSPREG00000002410.1.
DR GeneID; 103477116; -.
DR KEGG; pret:103477116; -.
DR CTD; 5979; -.
DR GeneTree; ENSGT00940000158499; -.
DR OMA; CDVVENQ; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000002410; Expressed in head.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0014707; P:branchiomeric skeletal muscle development; IEA:Ensembl.
DR GO; GO:0048484; P:enteric nervous system development; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0072114; P:pronephros morphogenesis; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR CDD; cd11304; Cadherin_repeat; 2.
DR CDD; cd05045; PTKc_RET; 1.
DR Gene3D; 2.60.40.60; Cadherins; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR041163; Ret_CLD1.
DR InterPro; IPR040667; Ret_CLD3.
DR InterPro; IPR041317; RET_CLD4.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016249; Tyr_kinase_Ret_rcpt.
DR PANTHER; PTHR24416:SF485; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF17756; RET_CLD1; 1.
DR Pfam; PF17812; RET_CLD3; 1.
DR Pfam; PF17813; RET_CLD4; 1.
DR PIRSF; PIRSF000631; TyrPK_receptor_Ret; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00112; CA; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50268; CADHERIN_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000631};
KW Calcium {ECO:0000256|PROSITE-ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|PIRNR:PIRNR000631};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR000631};
KW Kinase {ECO:0000256|PIRNR:PIRNR000631};
KW Membrane {ECO:0000256|PIRNR:PIRNR000631};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000631, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|PIRNR:PIRNR000631};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000631}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1118
FT /note="Proto-oncogene tyrosine-protein kinase receptor Ret"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018136797"
FT DOMAIN 191..263
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 728..1020
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 878
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-1"
FT BINDING 762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-4"
SQ SEQUENCE 1118 AA; 125273 MW; 1F475F430A0FB435 CRC64;
MEPSCGFSPG NVAALQLLLL LFGGVAGLYF PQREYTETVY VGQEAGTPVL QVHAMLDGRS
ERPHFYLCGS RRPPYALWFQ MDVQTGELSL SKTLEETDFA SLYQNSWPAK RLTLQVMALN
SVSKRAPCSR NSAHITLDFV NGSMPRCAQT DMKELCFPHR DTSNPHIIEN RFPGVLRQLR
RLTRLAVCPN YTITYGVESE TPAPFAVNGN TSELVVTAPL DREESENYRL LLVCTVQTES
VVTKVETPLD VFVDDEDDNA PYVNGTDTAE VVISFNRTKG AAFGTLFVFD RDLTTLFPKD
LSQNRYVGTL LSSESWIKDT FDIKATFSER RASPGGIRES VYDYQLILKR NLDITENRTV
FLDYLVNDTT YPGLEGTVLL HFNVTILPVQ IRFANITHVF TLPRKASVYA QVGRICVENC
LEFDGFSVSY QLEVPDKNMS SELLSCFSAI SITQAPDRML GLLYVNNSGA LSRPGCQDLD
YTVVAQEEHS QLVASTQIRI LLHGEAANVS QESQQLLSCA ENRQRDDCEA SQGLGATTGA
CQWRQGSEKG ISENYSTCSP DLRTCPDSVC DAVESRDTSI CPQDCTTESV TGGHERGLSG
SGIRAGYGTC YCFSEKCFCE NADAEAVVSK NRFPDVICDD MCKTIVATAL LCCFIISVLL
SSYFIHRYHK NSPKAPIAFA EMTFRRPAQS YPISFPANNV RRGSQESIEA DAFKIPEDPK
WEFPRKNLVL GKTLGEGEFG KVVKATAFRL KGKAGYTTVA VKMLKENASH TELRDLLSEF
TLLKQVNHPH VIKMYGACSQ DGPLYLIVEY AKFGSLRNFL RESRKVGPSY MGRDANRNSS
YLENPDDRAL TMGDLISFAW QISRGMQYLA EMKLVHRDLA ARNVLVAEGR KMKISDFGLS
RDVYEEDSYV KRSKGRIPVK WMAIESLFDH IYTTQSDVWS FGVLLWEIVT LGGNPYPGIA
PERLFNLLKT GYRMERPENC SEEMYNLMLR CWKQEPDKRP TFSDISKELE KMMVKSRDYL
DLAASTPADA LLYDDALSEE DTPLVDCNNA PLPRTLPSTW IENKLYGMSY PSWPETSPVP
LNRHDATNPV FTRYANDSVY ANWMALPSPA KAVDKLDS
//
