ID A0A091PKT8_APAVI Unreviewed; 350 AA.
AC A0A091PKT8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Activin receptor type-1 {ECO:0000256|ARBA:ARBA00039914};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
DE AltName: Full=Activin receptor type I {ECO:0000256|ARBA:ARBA00041365};
DE Flags: Fragment;
GN ORFNames=N311_07704 {ECO:0000313|EMBL:KFP92110.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP92110.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP92110.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP92110.1};
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-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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {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}.
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DR EMBL; KL392462; KFP92110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PKT8; -.
DR Proteomes; UP000054244; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0009888; P:tissue development; IEA:UniProt.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255:SF69; ACTIVIN 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; PF07714; PK_Tyr_Ser-Thr; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
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};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFP92110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..350
FT /note="Activin receptor type-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001877917"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..201
FT /note="GS"
FT /evidence="ECO:0000259|PROSITE:PS51256"
FT DOMAIN 202..350
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 229
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:KFP92110.1"
FT NON_TER 350
FT /evidence="ECO:0000313|EMBL:KFP92110.1"
SQ SEQUENCE 350 AA; 38627 MW; 89EBB54D3505FAD6 CRC64;
VVDGVMILPV LMVMAFPSPS WQGDELKLNT VHYECVCEGM SCGNGDRCQG QQCFASLSIN
DGAKVYQKGC FQVYEQGKMT CKTPPSPDQA VECCQGYLCN MNITAQLPSS KGYSMETLII
VILAPVIVLI VFSAVAVLII RRIQKNHMER LNSRDAEYGT IEGLIASNVG DSTLADLLDH
SCTSGSGSGL PFLVQRTVAR QITLVECVGK GRYGEVWRGQ WQGENVAVKI FSSRDEKSWF
RETELYNTVL LRHENILGFI ASDMTSRNSS TQLWLITHYH EMGSLYDYLQ LTTLDTVSCL
RIVLSIASGL AHLHIEIFGT QGKPAISHRD LKSKNILVKK NGQCCIADLG
//
