ID A0A093PPB0_9PASS Unreviewed; 472 AA.
AC A0A093PPB0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=TGF-beta receptor type-1 {ECO:0000256|ARBA:ARBA00040150};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
DE AltName: Full=Transforming growth factor-beta receptor type I {ECO:0000256|ARBA:ARBA00043075};
DE Flags: Fragment;
GN ORFNames=N305_01762 {ECO:0000313|EMBL:KFW78276.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW78276.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW78276.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW78276.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30; Evidence={ECO:0000256|ARBA:ARBA00023945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC Evidence={ECO:0000256|ARBA:ARBA00023948};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL670090; KFW78276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093PPB0; -.
DR STRING; 328815.ENSMVIP00005022567; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009888; P:tissue development; IEA:UniProt.
DR CDD; cd14143; STKc_TGFbR1_ACVR1b_ACVR1c; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR003605; GS_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255:SF61; TGF-BETA RECEPTOR TYPE-1; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 1.
DR PROSITE; PS51256; GS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Kinase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFW78276.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..173
FT /note="GS"
FT /evidence="ECO:0000259|PROSITE:PS51256"
FT DOMAIN 174..464
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW78276.1"
FT NON_TER 472
FT /evidence="ECO:0000313|EMBL:KFW78276.1"
SQ SEQUENCE 472 AA; 53120 MW; CEEBE8B9AC0E3203 CRC64;
LECYCHLCTK DNFTCVTDGV CFASVTRTAD KIIHNSMCIA EVDLIPRDRP FVCSSSTRDG
VFTVPHCCNT PLCNKIELPI PTPEKPASNL GPVELAAVIA GPVCFVCISL MLILYICHNR
TVIHHRVPSE EDPSLDRPFI SEGTTLKDLI YDMTTSGSGS GLPLLVQRTI ARTIVLQESI
GKGRFGEVWR GKWRGEEVAV KIFSSREERS WFREAEIYQT VMLRHENILG FIAADNKDNG
TWTQLWLVSD YHEHGSLFDY LNRYTVTVEG MIKLALSTAS GLAHLHMEIV GTQGKPAIAH
RDLKSKNILV KKNGTCCIAD LGLAVRHDSA TDTIDIAPNH RVGTKRYMAP EVLDDSINMK
HFESFKRADI YAMGLVFWEI ARRCSIGGIH EDYQLPYYDL VPSDPSVEEM RKVVCEQKLR
PNIPNRWQSC EALRVMAKIM RECWYANGAA RLTALRIKKT LSQLSQQEGI KM
//