ID A0A0V0YIY5_TRIPS Unreviewed; 530 AA.
AC A0A0V0YIY5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN Name=ACVR2A {ECO:0000313|EMBL:KRY00008.1};
GN ORFNames=T4E_190 {ECO:0000313|EMBL:KRY00008.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRY00008.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRY00008.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRY00008.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361271};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU361271};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU361271};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605, ECO:0000256|RuleBase:RU361271}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY00008.1}.
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DR EMBL; JYDU01000011; KRY00008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0YIY5; -.
DR STRING; 6337.A0A0V0YIY5; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR PANTHER; PTHR23255:SF98; SERINE_THREONINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037393; TGFRII; 2.
DR PRINTS; PR00653; ACTIVIN2R.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 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|PIRSR:PIRSR037393-
KW 2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
KW Kinase {ECO:0000256|RuleBase:RU361271};
KW Magnesium {ECO:0000256|RuleBase:RU361271};
KW Manganese {ECO:0000256|RuleBase:RU361271};
KW Membrane {ECO:0000256|RuleBase:RU361271};
KW Metal-binding {ECO:0000256|RuleBase:RU361271};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR037393-2};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361271};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361271}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|RuleBase:RU361271};
KW Transmembrane {ECO:0000256|RuleBase:RU361271};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361271}.
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361271"
FT DOMAIN 210..503
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-1"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-2"
FT DISULFID 32..63
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 93..112
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 114..119
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
SQ SEQUENCE 530 AA; 60046 MW; 37A51B0B81007D40 CRC64;
MNVNCDYSFV PLFRQCSVFT DMRSENYDDF SCAYFNSDVC NGTAENCPTP ETCEKLGNSS
QGCYAVWKYV GEQAEVMYKG CWTNEMDCDF DRCIAEEPSV DSPVRSIEVY FCCCNKPMCN
REFQVGSKSF SETFSKIDRT NTTILTVDDS LRNVIFSLVS VLLAAVLILI GFYFVRRYRL
RFLLKSLESH STVLPKRLPL SLSNLPQRQI RLKEKISRGH YGCVYKAAMG AQQVVVAVKV
FSANNSDSWV QEQEIYAVPG LKSHPNILRF LGAEAHGTGP NYDYWLITEY HQRGSLHDHI
KIHSISFQQL LSIGISMLRG LSFLHEEVVG TDKYKPTIVH RDFKSRNVLL KDDFTACVAD
FGLALKCEHG RTPNDTHGQV GTRRYMAPEV LEGATEFSAF AFRQIDVYAA ALVLWELMSR
CSLHGEEPDE YKLPFEVEVG LRPTLQVIQD TVATKKRRPI IKDSWRVDSH SKVVCATIEE
MWDGEPEARI SVGCAAERLN ALWHVGEELG NDSKDELAPL MIAEQQHCDA
//
