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Database: UniProt
Entry: H3CUH8_TETNG
LinkDB: H3CUH8_TETNG
Original site: H3CUH8_TETNG 
ID   H3CUH8_TETNG            Unreviewed;       510 AA.
AC   H3CUH8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   31-JUL-2019, entry version 48.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000011912, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Ensembl:ENSTNIP00000011912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A.,
RA   Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B.,
RA   Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S.,
RA   Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B.,
RA   Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V.,
RA   Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J.,
RA   Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S.,
RA   Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J.,
RA   Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M.,
RA   Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C.,
RA   Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals
RT   the early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000011912}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
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}.
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DR   Ensembl; ENSTNIT00000012102; ENSTNIP00000011912; ENSTNIG00000009054.
DR   eggNOG; KOG2052; Eukaryota.
DR   eggNOG; ENOG410XQT0; LUCA.
DR   GeneTree; ENSGT00940000155919; -.
DR   OMA; QCRDTWN; -.
DR   TreeFam; TF314724; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0042078; P:germ-line stem cell division; IEA:Ensembl.
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   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 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|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007303};
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|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361271,
KW   ECO:0000256|SAAS:SAAS00138186};
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   TRANSMEM    131    154       Helical. {ECO:0000256|RuleBase:RU361271}.
FT   DOMAIN      180    211       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      212    503       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   510 AA;  57617 MW;  45165367598CA920 CRC64;
     ANMLDAMLLR NGGKSASERQ AQESSSAVPV AAPSMLWCHC YHHCPEDSAN NTCMTDGYCF
     TMVEEEEGGQ PVLTAGCLGL AGSEFQCRDT WNARSRRALE CCTDQDYCNR NLHPTLPPLV
     SSDFGDSSIQ YMALSISIIV CSVILALILL FCYVRYKRQE SQPHYSIDLE QEETYIPPGE
     SLKDLIEHSR SVGSGSGSGL PLLVQRTIAK QIQMVKQIGK GRYGEVWMGK WRGERVAVKV
     FFTTEEESWF RETEIYQTFL MRHDNILGFI AADIKGTGSW TQLYLITDYH ENGSLYDYLK
     SNTLDVKALL KVAYSSISGL CHLHTEIYGT QGKPAIAHRD LKSKNILVKK NGYCCIADLG
     LAVKFNSDTN EVDIPPNLRV GTKRYMPPEV LDESLNRSYF QSFIMADMYS FGLIMWEMAR
     RCISGGIVEE YQLPYHDLVP TDPSYEDMQE VVCIKKQRPS FPNRWSSDEC LRQMGKVMSE
     CWAHSPASRL TALRVKKTLA KMLESQDIKL
//
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