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Database: UniProt
Entry: A0A0B2V048_TOXCA
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ID   A0A0B2V048_TOXCA        Unreviewed;       553 AA.
AC   A0A0B2V048;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   08-MAY-2019, entry version 24.
DE   RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132};
DE            EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132};
GN   Name=Tgfbr1 {ECO:0000313|EMBL:KHN74717.1};
GN   ORFNames=Tcan_14687 {ECO:0000313|EMBL:KHN74717.1};
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:KHN74717.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN74717.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN74717.1};
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.,
RA   Yang Y., Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W.,
RA   Jex A.R., 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=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
CC         phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
CC         COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|SAAS:SAAS01128400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-threonine + ATP = [receptor-
CC         protein]-O-phospho-L-threonine + ADP + H(+);
CC         Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-
CC         COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30; Evidence={ECO:0000256|SAAS:SAAS01128404};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|SAAS:SAAS00595019}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KHN74717.1}.
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DR   EMBL; JPKZ01002830; KHN74717.1; -; Genomic_DNA.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043235; C:receptor complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:InterPro.
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; IPR000333; TGFB_receptor.
DR   InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PIRSF; PIRSF037393; TGFRII; 2.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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|PIRSR:PIRSR037393-2,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031036};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
KW   Kinase {ECO:0000256|SAAS:SAAS00138139};
KW   Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR037393-2,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:KHN74717.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00138186};
KW   Transferase {ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00138220,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00488859,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    117    141       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      223    252       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      253    541       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   ACT_SITE    381    381       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037393-1}.
FT   BINDING     280    280       ATP. {ECO:0000256|PIRSR:PIRSR037393-2}.
FT   DISULFID     75     89       {ECO:0000256|PIRSR:PIRSR037393-3}.
SQ   SEQUENCE   553 AA;  61213 MW;  78D32DD2492C6A85 CRC64;
     MRRFEANLKY PVNLETDIMC NCTHAGCDVE VTRFLGKNFT HICRATGGAC YKRIALDGTT
     IHACLGLDAV PDLFCSTKQP MPDGSVMACC SNQSFCNGAL NLKLPVQPES DSTPWRVVAI
     VAVVLIAVAL VSGILLTLAV VNKPLKQCIF YWLFRRPNAS STQGVGTEEM LLGSPSDDLA
     HLSDLLGNLD DSDTTGSGSG YKKRVGTEEM LLGSPSDDLA HLSDLLGNLD DSDTTGSGSG
     LPLLVQRTIA RQIELHTEIG KGRFGEVWLG SWKGDPVAVK IFSSRDERSW NREVEVFQTN
     MLRHSNILRF IASDNKDTGT SMQLWLVTEY HAHGSLFDYL SENTISGPVM LQMLRSIANG
     LAFLHAEVPG MHSKPAIAHR DLKTKNILVK SNLTCVIADL GLAVRYINGE LNLPDNNKCG
     TIRYLSPEVL SDSYPIHQFD AYKMSDMYAI GLIIWELATR CDANGDMQAY EPPYAEWVTR
     DPSIEEMREC VCVHKHRPTV RGSWKSDKVM SDIERMMMEC WAESPPNRLT AMNVRIAVDR
     LANSLDWKLQ TSS
//
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