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Database: UniProt
Entry: Q9YH35_TETFL
LinkDB: Q9YH35_TETFL
Original site: Q9YH35_TETFL 
ID   Q9YH35_TETFL            Unreviewed;      1106 AA.
AC   Q9YH35;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Proto-oncogene tyrosine-protein kinase receptor Ret {ECO:0000256|PIRNR:PIRNR000631};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000631};
GN   Name=RET {ECO:0000313|EMBL:AAD10845.1};
OS   Tetraodon fluviatilis (Green pufferfish) (Chelonodon fluviatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=47145 {ECO:0000313|EMBL:AAD10845.1};
RN   [1] {ECO:0000313|EMBL:AAD10845.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Leu J.H., Huang C.J.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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   EMBL; U58673; AAD10845.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9YH35; -.
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; 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; 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; PR00205; CADHERIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00112; CA; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 2.
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, ECO:0000313|EMBL:AAD10845.1};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000631};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000631, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:AAD10845.1};
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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1106
FT                   /note="Proto-oncogene tyrosine-protein kinase receptor Ret"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004337048"
FT   DOMAIN          193..266
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          716..1008
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        866
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000631-1"
FT   BINDING         750
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1106 AA;  124995 MW;  EC4045464974D56A CRC64;
     MGSSYGFSRG NVILMLLLLL LDGVRGLYFS QSEYIETVYV GQPAGTPVLQ VHALRDNVSQ
     LPHFYLCWVK FLRRPAYISW FSLDVNTGVL YLNKTLEESD FASVYQSNQA VKKLSLHVMA
     SPGFTKKPLC NSRNYPRITL DFVNALMPQC GETDLKELCF PRKDTSNPHI TENRFPGGLR
     QLRRLSWLNV CPNYTISYSV ETESPAPFAV NENTTELVVT APLDREESES YRLLLVCTVR
     TEAVITKVET SLDVFVDDED DNAPYMNGTD TSDIVISFNR TAGGSFGTLS VFDRDLTPII
     DRTHNKYVGT LLNIDPWVKE TFDIKGTFSE KKAAQGGIRE TVHDYHLVLK RNLYVTENRT
     LQLDYLVNDT TYPGLEGTVL LHFNVTILPV HIFFSNITHT FPLTRRASSY AQVGKVCVEN
     CRQFDGFRIA YRLELPDKNV SADVLSCHSA VSIAQAPDEM WGLLYVNDTE ELRRPECQDL
     QYLVVVKEQH TQMETSVQIQ IILDNEVGQE SQPLLSCAEN RRRGDCESAR GLGTTTGRCQ
     WRQGSDKGIS KNYSTCSPDL RTCPDSVCDA VESKDASICP QDCTKKTVIG GHEPGLRNGI
     QAGHGTCYCY SEKCFCEKED IDETMCDDMC KTIIATALLL SFIVSILLSS YFIHRYHKNS
     PKPPIASAEM TFRRPAQAYP ISFPANNLRR GSQESIETDT FKIPEDPKWE FPRKNLVLGK
     TLGEGEFGKV VKATAFRLKG KAGYTTVAVK MLKENASHSG LRSLLSEFTL LKQVNHPHVI
     KMYGACSQDG PLYLIVEYAK YGSLRNFLRE SRKVGPSYMG RDANRNSSYL ENPDDRALTM
     GDLISFAWQI SRGMQYLAEM KLVHRDLAAR NVLVAEGRKM KISDFGLSRD VYEEDSYVKR
     SKGRIPVKWM AIESLFDHIY TTQSDVWSFG VLLWEIVMLG GNPYPGIAPE RLFNLLKTGY
     RMERPENCSE EMYNLMLRCW KQEADKRPTF SDISKELEKM MVKSRDYLDL AASTPADALL
     YDDALSEEDT PLVDCNNAPL PRTLPSTWIE NKLYGMSYPN WPEKSPVPLS RHDATNPVFT
     RYANDSVYAN WMALPSPAKA VDKVDS
//
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