ID A0A337S4G8_FELCA Unreviewed; 1116 AA.
AC A0A337S4G8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
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};
GN Name=RET {ECO:0000313|Ensembl:ENSFCAP00000043172.2,
GN ECO:0000313|VGNC:VGNC:69292};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000043172.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000043172.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000043172.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000043172.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000043172.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000043172.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000043172.2};
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 EMBL; AANG04000273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A337S4G8; -.
DR GlyCosmos; A0A337S4G8; 1 site, No reported glycans.
DR PaxDb; 9685-ENSFCAP00000012057; -.
DR Ensembl; ENSFCAT00000061821.2; ENSFCAP00000043172.2; ENSFCAG00000012999.6.
DR VGNC; VGNC:69292; RET.
DR GeneTree; ENSGT00940000158499; -.
DR Proteomes; UP000011712; Chromosome D2.
DR Bgee; ENSFCAG00000012999; Expressed in prefrontal cortex and 7 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; 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:UP000011712};
KW Transferase {ECO:0000256|PIRNR:PIRNR000631};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000631}.
FT DOMAIN 168..273
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 726..1018
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 876
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-1"
FT BINDING 760
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-4"
FT DISULFID 137..142
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-3"
SQ SEQUENCE 1116 AA; 124784 MW; 37A0AB827DE8DCDF CRC64;
MPDSCGGRPD GPAEESRPGV PLPAPLGLYF ARDAYWEKLY VDQPAGMPLL YVHALRDMPE
EVPTFRLGQH LYGIAYRARL HENEWIRIEE DTGLLYLNRS LDHSTWDKLS IRNGGFPVLT
IYLQVFLSPT SLREGECQWP SCARVYFSFV NTSFPACGSL KPRELCFPET GVSFRIRENR
PPGTFHQFRL LPVQFLCPNI SVAYRLLEGE NLPFHCAPDS LEVSTRWPLD RELREKYELV
AACTVRVGAR KEEVVMVPFP VTVYDEDDSA PTFLGGIDTA SAVVEFKRKE GTVVAKIRVF
DADVVPASGE LLKRYTNTLL SGDAWVLQTF RIEHSPNETL AQANGSFVRA TVHDYRLVLN
RSLPISENRS LQLTVLVNDS DFQGPGEGTL FLHFNVSVLP VSLHLPSTYT FTVSRRARRF
AQIGKVCVEN CQEFSGIHVQ YRLQLSSTNC SVLGVVTSAE DTTGNLFVND TEALQRPDCS
QLRYTVVAAD RPTRKQTQAL LVVTVEGTYV AEEPGCPLSC AVSKRRPECE ECGGLGSLTG
RCEWRQGDGK GITRNFSTCS PSIKTCPDGH CDAVESRNVN ICPQDCLRGG SIIGGHEPGE
RWGIKAGFGI CNCFPEEKKC FCEPEDSQEP LCDELCRTVI AAAVLFSFVV SMLLSTFCIH
RYHKNAHKPP IASAEMTFRR PAQAFPVSYS SSGARRPSMD SMENQVSVDA FKIPEDPKWE
FPRKNLVLGK TLGEGEFGKV VKATAFRLKG KAGYTTVAVK MLKENASPSE LRDLLSEFNL
LKQVNHPHVI KLYGACSQDG PLFLIVEYAK YGSLRGFLRE SRKAGPGYVG SGGSRSSSYL
DNPEERALTM GDLISFAWQI SRGMRYLAEM KLVHRDLAAR NVLVAEGRKM KISDFGLSRD
VYEEDSYVKR SKGRIPVKWM AIESLFDHIY TTQSDVWSFG VLLWEIVTLG GNPYPGIPPE
RLFNLLKTGY RMERPDNCSE EMYGLMLQCW KQEPDKRPVF ADISKDLEKM MVKNRDYLDL
AASTPSDSLL YDDGLSEEET PLVDCNNAPL PRALPSTWIE NKLYGMSDPN WPEESPVPLT
RADGTNTVCP RYANDSVYAN WMVSPSAAQL MDAFDS
//
