ID A0A093HZ58_STRCA Unreviewed; 1076 AA.
AC A0A093HZ58;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Proto-oncogene tyrosine-protein kinase receptor Ret {ECO:0000313|EMBL:KFV88048.1};
DE Flags: Fragment;
GN ORFNames=N308_15416 {ECO:0000313|EMBL:KFV88048.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV88048.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV88048.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV88048.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KL206988; KFV88048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HZ58; -.
DR STRING; 441894.ENSSCUP00000020040; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Calcium {ECO:0000256|PROSITE-ProRule:PRU00043};
KW Kinase {ECO:0000313|EMBL:KFV88048.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000313|EMBL:KFV88048.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 142..246
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 700..992
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 850
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-1"
FT BINDING 734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000631-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV88048.1"
FT NON_TER 1076
FT /evidence="ECO:0000313|EMBL:KFV88048.1"
SQ SEQUENCE 1076 AA; 121775 MW; A6DF472E0C6334F0 CRC64;
AAFGLYFPRK EYSENVYIDQ AAGTPLLHIH ALRDSHGEAA HFHLCQNLII SRARSHENHW
FQIREKTGLL YLSKSLDRED FNMLSVGNWM SLSKVMLYVF LSSHPFQEKE CDSATRATVY
LSLINATAPA CSTLTARQLC FTEMDLSFHI KENKPPGTFH QLQLPSVHHL CQNVSVSYKL
LAAEGLPFRY NENTTGVSVI QRLDREERER YELIAKCTVR EGFREMQVEV PFLVNVLDED
DSAPFLPNGT NTADAVVEFN RKEGTVLAML TVCDADTTPI YPLESSRKKY TGTIITNDPW
INETFRVEHI FHEIHFSPNG SQVRGTLHEY KLVLNKSISV TEHRSFQLDV LVNDTEYHGP
ERSVMLHFNV SILPVSIQFP NVTYQFTVNR NAERFAQIGK ICIENCMKFC GVNITYKLLS
PNVSCYAVSI LQGREDKYGS LYVNDSSVLR RPECKEIQYT IQATDRQSRK HAKTLLTVVL
EGTLLKKEED CPDSCAVSKH HAECEECGGL GVLTGRCQWR QGSGKGITTN YSTCTPSIKT
CPDGICDVIE SRDPAVCPQD CTSGNIIGGH GKGIGNLGIK SGHGICYCFP RQNCYCEKAD
IKEQLCDDVC KTVIAGAVLL SFIISVLLSS YFIHRYHKNS PKPPIASAEM TFRRPAQSYP
ISYSSTNVRR PSLDSMENQV SVDTFKIPED PKWEFPRKNL VLGKTLGEGE FGKVVKATAF
RLKGRAGYTT VAVKMLKENA SQSELRDLLS EFNLLKQVNH PHVIKLYGAC SQDGPLYLIV
EYAKYGSLRS FLRESRKVGP SYVGSDGNRN SSYLDNPDER ALTMGDLISF AWQISRGMQY
LAEMKLVHRD LAARNVLVAE GRKMKISDFG LSRDVYEEDS YVKRSKGRIP VKWMAIESLF
DHIYTTQSDV WSFGVLLWEI VTLGGNPYPG IAPERLFNLL KTGYRMERPE NCSEEMYNLM
LRCWKQEPDK RPTFAEISKE LEKMMVKSRD YLDLAASTPS DSLLYDDGLS EEETPLVDCN
NAPLPRTLPS TWIENKLYGM SYPNWPEESP VPLTRFDGTN SVFSRYANDS VYANWM
//
