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Database: UniProt
Entry: A0A2A4JZJ2_HELVI
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ID   A0A2A4JZJ2_HELVI        Unreviewed;       539 AA.
AC   A0A2A4JZJ2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   08-MAY-2019, entry version 8.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   ORFNames=B5V51_7357 {ECO:0000313|EMBL:PCG77431.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
OC   Noctuoidea; Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG77431.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG77431.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG77431.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG77431.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis
RT   virescens, in response to modern agricultural practices.";
RL   Submitted (SEP-2017) 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|RuleBase:RU361271,
CC         ECO:0000256|SAAS:SAAS01128404};
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|RuleBase:RU361271};
CC       Single-pass type I membrane protein
CC       {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|RuleBase:RU361271, 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:PCG77431.1}.
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DR   EMBL; NWSH01000326; PCG77431.1; -; Genomic_DNA.
DR   Proteomes; UP000218220; 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-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:InterPro.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:InterPro.
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; IPR000333; TGFB_receptor.
DR   InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 2.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PIRSF; PIRSF037393; TGFRII; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
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|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000218220};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
KW   Kinase {ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138139};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|RuleBase:RU361271};
KW   Membrane {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138203};
KW   Metal-binding {ECO:0000256|RuleBase:RU361271};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR037393-2,
KW   ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138186}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138220};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00488859}.
FT   SIGNAL        1     34       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        35    539       Serine/threonine-protein kinase receptor.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012201436.
FT   TRANSMEM    131    152       Helical. {ECO:0000256|RuleBase:RU361271}.
FT   DOMAIN      185    213       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      214    528       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   ACT_SITE    362    362       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037393-1}.
FT   BINDING     241    241       ATP. {ECO:0000256|PIRSR:PIRSR037393-2}.
FT   DISULFID     87    101       {ECO:0000256|PIRSR:PIRSR037393-3}.
SQ   SEQUENCE   539 AA;  61446 MW;  69892DEF9A22BF11 CRC64;
     MFSSRNVIMN SFQWRKWFLF LIFAVYRRLD TVDGLKCYCN SERCPNSTCE TDGFCFASTS
     LENKVQKFTY HCIELKSLIP IEHPFSCSTT KTKNESVVIK CCKSHDMCNE GLRLDLQPKP
     ETGTTATAWK VLPWVMGLMV LGVCAAISFW WAKRSHGPKK RVPSRTPYPT DDSVCEARHP
     MMRTTTIRDM IELTTSGSGS GLPLLVQRSI ARQIQLVDII GKGRFGEVWR GRWRGENVAV
     KIFSSREESS WFREAEIYQT VMLRHENILG FIAADNKDNG TWTQLWLITD YHENGSLFDF
     LSARTIDSIT LVKMSLSIAT GLAHLHMDIV GTKGQPGVLF SNTDQTECWR NIGGKPAIAH
     RDLKSKNILV KSNLTCVIGD LGLAVRHNVA SDSVDVPTTN RVGTKRYMAP EVLDETMDTR
     QFDPYKRSDV YSFGLVLWEM ARRCGVMPDE YQPPYYDCVP PDPALEDMRR VVCTEKRRPN
     VPNRWHSDHV LSSISKVMKE CWYQNPAARL TALRIKKTLA NIGTPDYIKL EVELDEIRV
//
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