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Database: UniProt
Entry: H2UDY0_TAKRU
LinkDB: H2UDY0_TAKRU
Original site: H2UDY0_TAKRU 
ID   H2UDY0_TAKRU            Unreviewed;       540 AA.
AC   H2UDY0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   08-MAY-2019, entry version 46.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN   Name=LOC101061264 {ECO:0000313|Ensembl:ENSTRUP00000035149};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000035149, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000035149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A.,
RA   Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu
RT   facilitates insights into distinct features of genome evolution in
RT   teleosts and mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000035149}
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   STRING; 31033.ENSTRUP00000035149; -.
DR   Ensembl; ENSTRUT00000035277; ENSTRUP00000035149; ENSTRUG00000013761.
DR   eggNOG; KOG2052; Eukaryota.
DR   eggNOG; ENOG410XQT0; LUCA.
DR   GeneTree; ENSGT00940000155919; -.
DR   OMA; QCRDTWN; -.
DR   TreeFam; TF314724; -.
DR   Proteomes; UP000005226; Chromosome 6.
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; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PIRSF; PIRSF037393; TGFRII; 2.
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:UP000005226};
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:UP000005226};
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     21     44       Helical. {ECO:0000256|RuleBase:RU361271}.
FT   DOMAIN      210    241       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      242    533       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   ACT_SITE    370    370       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037393-1}.
FT   BINDING     269    269       ATP. {ECO:0000256|PIRSR:PIRSR037393-2}.
FT   DISULFID     79     85       {ECO:0000256|PIRSR:PIRSR037393-3}.
FT   DISULFID    128    142       {ECO:0000256|PIRSR:PIRSR037393-3}.
SQ   SEQUENCE   540 AA;  60830 MW;  832B765598026CE0 CRC64;
     MPHSSGFIWR RTSTASTFRS LLLILPIITS GTCVSVSVST ANMLDAMLLR NGGKGGSERW
     PEDSSGGTVT VLAPRMLWCH CYHHCPEDSV NNTCVTDGYC FTMVEEEEGG QAVLTAGCLG
     LAGSEFQCRD TWNVRSRRAL ECCTDQDYCN QNLHPTLPPL VSSGKNHRWH ASVPPVSANT
     LSCDRYKRQE SRPHYSIDLE QEETYIPPGE SLKDLIEHSR SIGSGSGSGL PLLVQRTIAK
     QIQMVKQIGK GRYGEVWMGK WRGERVAVKV FFTTEEESWF RETEIYQTFL MRHDNILGFI
     AADIKGTGSW TQLYLITDYH ENGSLYDYLK SNTLDVKALL KLAYSSISGL CHLHTEIYGT
     QGKPAIAHRD LKSKNILVKK NGSCCIADLG LAVKFNSDSN EVDIPPNLRV GTKRYMPPEV
     LDESLNRSYF QSFIMADMYS FGLIMWEMAR RSTFGGIVEE YQLPYHDLVP TDPSYEDMQE
     VVCIKKQRPS FANRWSSDEC LRQMGKLMSE CWAHSPASRL TALRVKKTLA KMLESQDIKL
//
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