ID A0A0B2VYD1_TOXCA Unreviewed; 909 AA.
AC A0A0B2VYD1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:KHN86439.1};
GN ORFNames=Tcan_18418 {ECO:0000313|EMBL:KHN86439.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN86439.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN86439.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN86439.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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:KHN86439.1}.
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DR EMBL; JPKZ01000620; KHN86439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2VYD1; -.
DR STRING; 6265.A0A0B2VYD1; -.
DR Proteomes; UP000031036; 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: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; 2.
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 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; 2.
DR PRINTS; PR00653; ACTIVIN2R.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
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|RuleBase:RU361271};
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|RuleBase:RU361271};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361271};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361271};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU361271};
KW Transmembrane {ECO:0000256|RuleBase:RU361271};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361271}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..909
FT /note="Serine/threonine-protein kinase receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002095650"
FT TRANSMEM 205..228
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361271"
FT DOMAIN 269..558
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 825..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 101262 MW; D2C947DE5FB09D49 CRC64;
MRAVPPRTHF LLTITLLLSP INAVLFERKA HSGLFNDELV DLKEVAGAVK VELPARPVFL
EKHGTEGINY SLDNRSRPFI YCDYYDVNAC DPAVRNCPTT KMCYAAASDH RLGCMAALVN
NSSSRQITLK GCWMHDGNLG NCDNEACVAE ERPTGHGNAA LFCCCSTHHC NRHIRFPAYS
QPTVAPSTLA PAESDDPGLF SSDSWVAAVI IFGIFIACLL VLVCYWTYRE FRSSQHIKAK
AVNDYSMPRM GSAANPLLGS SKDDGCRNVT ALELVARGRF GQVSRGLFDG TVVAVKEFPS
VDANSWIVEQ EIYALPALRK HDNILRYIGA EVHGDRYWLI TEYHENGSLH DYLKPHVLTL
REALKVIATM LRGLSFLHEE KTVDGELKPC VVHRDFKSRN VLLKSDLTAV IADFGLALKC
ENGQMPAEDH HGQVGTRRYM SPEVLEGATE FTAFAFRQID VYAAALVIWE VLSRTTFLEG
DIVDEYRQPY EEETGLQPSL HDLRRIVAVQ KTRPRIRRAV KEHNIGSVLW KTVEDMWDME
PDGRITSGCA YERANTLFMS YAVESPAEGA QTRNSHSLSE DFKSRNVLLK SDLTAVIADF
GLALKCENGQ MPAEDHHGQV GTRRYMSPEV LEGATEFTAF AFRQIDVYAA ALVIWEVLSR
TTFLEGDIVD EYRQPYEEET GLQPSLHDLR RIVAVQKTRP RIRRAVKEHN IGSVLWKTVE
DMWDMEPDGR ITSGCAYERA NTLFMSYAVE SPAEGAQTHG PPPPYSQVHA SDDMALRPAL
MIKDGSLGSN GFNATMDEYA QACTAPPNVR FVGDDYRRPA TTHSVIQMDP PCGRTSDSDR
GEADGRIPPP LLSTCCAQES SSSQMVGVAQ NGYVVHKRSI EGVPLARRTV WKMDDKGMGK
MRGTLMCIE
//
