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Database: UniProt
Entry: I3LWQ4_ICTTR
LinkDB: I3LWQ4_ICTTR
Original site: I3LWQ4_ICTTR 
ID   I3LWQ4_ICTTR            Unreviewed;       512 AA.
AC   I3LWQ4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   08-MAY-2019, entry version 49.
DE   RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132};
DE            EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132};
GN   Name=ACVR1B {ECO:0000313|Ensembl:ENSSTOP00000000433};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel)
OS   (Spermophilus tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
OC   Sciuridae; Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000000433, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Ensembl:ENSSTOP00000000433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000000433}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-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|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}.
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DR   EMBL; AGTP01037400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 43179.ENSSTOP00000000433; -.
DR   Ensembl; ENSSTOT00000000482; ENSSTOP00000000433; ENSSTOG00000000480.
DR   eggNOG; KOG2052; Eukaryota.
DR   eggNOG; ENOG410XQT0; LUCA.
DR   GeneTree; ENSGT00940000157032; -.
DR   InParanoid; I3LWQ4; -.
DR   TreeFam; TF314724; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0048179; C:activin receptor complex; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0048185; F:activin binding; IEA:Ensembl.
DR   GO; GO:0016361; F:activin receptor activity, type I; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR   GO; GO:0034711; F:inhibin binding; IEA:Ensembl.
DR   GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0038092; P:nodal signaling pathway; IEA:Ensembl.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:1901165; P:positive regulation of trophoblast cell migration; IEA:Ensembl.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
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|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005215};
KW   Kinase {ECO:0000256|SAAS:SAAS00138139};
KW   Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|SAAS:SAAS00138179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
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    134    158       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      184    213       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      214    504       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   512 AA;  58160 MW;  0D62A33A9A70D667 CRC64;
     KILLFGRHSF WDYILNLEKD LEKTSLLLSM STPKSPAALL CACTSCLQAN YTCETDGACM
     VSIFNLDGME HHVRTCIPKV ELVPAGKPFY CLSSEDLRNT HCCYTDFCNK IDLRVPSGHL
     KEPEHPSVWG PVELVGIIAG PVFLLFLIII IVFLVINYHQ RVYHNRQRLD MEDPSCEMCL
     SKDKTLQDLV YDLSTSGSGS GLPLFVQRTV ARTIVLQEII GKGRFGEVWR GRWRGGDVAV
     KIFSSREERS WFREAEIYQT VMLRHENILG FIAADNKDNG TWTQLWLVSD YHEHGSLFDY
     LNRYTVTIEG MIKLALSAAS GLAHLHMEIV GTQGKPGIAH RDLKSKNILV KKNGMCAIAD
     LGLAVRHDAV TDTIDIAPNQ RVGTKRYMAP EVLDETINMK HFDSFKCADI YALGLVYWEI
     ARRCNSGGVH EEYQLPYYDL VPSDPSIEEM RKVVCDQKLR PNIPNWWQSY EALRVMGKMM
     RECWYANGAA RLTALRIKKT LSQLSVQEDV KI
//
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