ID A0A3B1K5V3_ASTMX Unreviewed; 1071 AA.
AC A0A3B1K5V3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000048994.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000048994.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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 AlphaFoldDB; A0A3B1K5V3; -.
DR Ensembl; ENSAMXT00000053220.1; ENSAMXP00000048994.1; ENSAMXG00000004705.2.
DR GeneTree; ENSGT00940000158499; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000004705; Expressed in bone element and 9 other cell types or tissues.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11304; Cadherin_repeat; 1.
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; PF00028; Cadherin; 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; 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:UP000018467};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1071
FT /note="Proto-oncogene tyrosine-protein kinase receptor Ret"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017321695"
FT DOMAIN 168..264
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 723..1015
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 873
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-1"
FT BINDING 757
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-4"
SQ SEQUENCE 1071 AA; 121459 MW; 28E83CB120B90568 CRC64;
MGTARGTLRG DVVVVLLLLC EGSSGLYFPQ NLYSETIYVG QPAGAPLLQV HSMRETSSER
PYFSLCWRNV QKPPLIAAWF HIDPVSGVLY MNKTLEWTDF DSLSSSAFGH AKKLILKVVA
APGNQRSICL HHTKVDVSLT FLNTTAPSCG QIKLEKLCYP VRDINPHIKE NRLPGALRQL
RRFTQADICP NYTITYNVEA ESPGPFAVND SSSELVVTAP VDREEKEFYR LIIVCNVRTP
DMVHKLETPL HINIYDEDDT APYVNGTDSE DVLIEFSRSE GTVFGHLFVY DRDTTPSYPK
DQTENRFVGT LMTNDSWIKD TFTILHEFRE EKAMFGNVRG TVHEYRLNLS RNLTVEEKRS
FQLDYLVNDT TYPGTEGTVM LHFNITILPV PIQFSNITYV SLSRKSTLYS QIGKVCVDNC
LKFKGIDIAY EIEIADRNVS ADVLSCYSAV SVARSLEEMS GVLYVNDTKP FQRQECFQDL
EFVLIAKEQQ RHLEAKTQLL IRFEGEVVVP RSEKQQSLAC AEKRQRGDCE AFRGLGASTG
RCQWRQGTDK VISENYSTCS PDLRTCPDGY CDVIESKNIS ICPQDCTREP IIGGHERGLM
LGIKAGHGTC YCYSEKCFCE QDEMEEAICD DMCKTIIATA VLLSFIVSIL LSSYFIHRYH
KNTPKPPIAS AEMTFRRPAQ SYPISYSANN VRRGSLDSME NQVAIDTFKI PEDPKWEFPR
KNLVLGKTLG EGEFGKVVKA TAFRLKGKAG YTTVAVKMLK ENASHSELRD LLSEFTLLKQ
VNHPHVIKMY GACSQDGPLY LIVEYAKYGS LRNFLRESRK VGPSYMGSDA NRNSSYLENP
DERALTMGDL ISFAWQISRG MQYLAEMKLV HRDLAARNVL VAEGRKMKIS DFGLSRDVYE
EDSYVKRSKG RIPVKWMAIE SLFDHIYTTQ SDVWSFGVLL WEIVTLGGNP YPGIAPERLF
NLLKTGYRME KPENCTEEMY SLMLRCWKQE PDKRPTFSEI SKELEKMMVK SRDYLDLAAS
TPADALLYDD ALSEEDTPLV DCNNAPLPRT LPSTWIENKL YGRISHAFTR F
//
