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TGF-beta receptor type-2 (TGFR-2) (EC 2 7 11 30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II)

 F7CFN3_MONDO            Unreviewed;       564 AA.
F7CFN3;
27-JUL-2011, integrated into UniProtKB/TrEMBL.
09-JAN-2013, sequence version 2.
26-FEB-2020, entry version 61.
RecName: Full=TGF-beta receptor type-2 {ECO:0000256|PIRNR:PIRNR037393};
Short=TGFR-2 {ECO:0000256|PIRNR:PIRNR037393};
EC=2.7.11.30 {ECO:0000256|PIRNR:PIRNR037393};
AltName: Full=TGF-beta type II receptor {ECO:0000256|PIRNR:PIRNR037393};
AltName: Full=Transforming growth factor-beta receptor type II {ECO:0000256|PIRNR:PIRNR037393};
Name=TGFBR2 {ECO:0000313|Ensembl:ENSMODP00000018937};
Monodelphis domestica (Gray short-tailed opossum).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000018937, ECO:0000313|Proteomes:UP000002280};
[1] {ECO:0000313|Ensembl:ENSMODP00000018937, ECO:0000313|Proteomes:UP000002280}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=17495919; DOI=10.1038/nature05805;
Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
Samollow P.B., Lander E.S., Lindblad-Toh K.;
"Genome of the marsupial Monodelphis domestica reveals innovation in non-
coding sequences.";
Nature 447:167-177(2007).
[2] {ECO:0000313|Ensembl:ENSMODP00000018937}
IDENTIFICATION.
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-
beta type I serine/threonine kinase receptor, TGFBR1, the non-
promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3.
Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to
the cytoplasm and is thus regulating a plethora of physiological and
pathological processes including cell cycle arrest in epithelial and
hematopoietic cells, control of mesenchymal cell proliferation and
differentiation, wound healing, extracellular matrix production,
immunosuppression and carcinogenesis. The formation of the receptor
complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound
to the cytokine dimer results in the phosphorylation and the activation
of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1
phosphorylates SMAD2 which dissociates from the receptor and interacts
with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the
nucleus where it modulates the transcription of the TGF-beta-regulated
genes. This constitutes the canonical SMAD-dependent TGF-beta signaling
cascade. Also involved in non-canonical, SMAD-independent TGF-beta
signaling pathways. {ECO:0000256|PIRNR:PIRNR037393}.
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.11.30;
Evidence={ECO:0000256|SAAS:SAAS01128400};
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-threonine + ATP = [receptor-protein]-O-
phospho-L-threonine + ADP + H(+); Xref=Rhea:RHEA:44880, Rhea:RHEA-
COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
ChEBI:CHEBI:456216; EC=2.7.11.30;
Evidence={ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS01128404};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR037393}.
Membrane {ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane
protein {ECO:0000256|RuleBase:RU361271}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily.
{ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00595019}.
---------------------------------------------------------------------------
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---------------------------------------------------------------------------
RefSeq; XP_007505277.1; XM_007505215.2.
STRING; 13616.ENSMODP00000018937; -.
Ensembl; ENSMODT00000019279; ENSMODP00000018937; ENSMODG00000015155.
GeneID; 100031897; -.
KEGG; mdo:100031897; -.
CTD; 7048; -.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00940000157527; -.
HOGENOM; CLU_000288_8_3_1; -.
InParanoid; F7CFN3; -.
KO; K04388; -.
OMA; HQGIQTV; -.
OrthoDB; 426838at2759; -.
TreeFam; TF314724; -.
Proteomes; UP000002280; Chromosome 8.
Bgee; ENSMODG00000015155; Expressed in heart and 7 other tissues.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0048185; F:activin binding; IBA:GO_Central.
GO; GO:0017002; F:activin-activated receptor activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
GO; GO:0050431; F:transforming growth factor beta binding; IBA:GO_Central.
GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:UniProtKB-UniRule.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IBA:GO_Central.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0060434; P:bronchus morphogenesis; IEA:Ensembl.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
GO; GO:0003274; P:endocardial cushion fusion; IEA:Ensembl.
GO; GO:0007369; P:gastrulation; IEA:Ensembl.
GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IEA:Ensembl.
GO; GO:0007507; P:heart development; IBA:GO_Central.
GO; GO:0001947; P:heart looping; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:1905317; P:inferior endocardial cushion morphogenesis; IEA:Ensembl.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:1990086; P:lens fiber cell apoptotic process; IEA:Ensembl.
GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
GO; GO:0060443; P:mammary gland morphogenesis; IEA:Ensembl.
GO; GO:0003149; P:membranous septum morphogenesis; IEA:Ensembl.
GO; GO:1990428; P:miRNA transport; IEA:Ensembl.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0002663; P:positive regulation of B cell tolerance induction; IEA:Ensembl.
GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0002666; P:positive regulation of T cell tolerance induction; IEA:Ensembl.
GO; GO:0002651; P:positive regulation of tolerance induction to self antigen; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0062009; P:secondary palate development; IEA:Ensembl.
GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
GO; GO:0060440; P:trachea formation; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
GO; GO:0003186; P:tricuspid valve morphogenesis; IEA:Ensembl.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
InterPro; IPR017194; Transform_growth_fac-b_typ-2.
InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF08917; ecTbetaR2; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF037393; TGFRII; 1.
PRINTS; PR00653; ACTIVIN2R.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
3: Inferred from homology;
Apoptosis {ECO:0000256|PIRNR:PIRNR037393};
ATP-binding {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|PIRSR:PIRSR037393-
2, ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138218};
Cell membrane {ECO:0000256|PIRNR:PIRNR037393};
Differentiation {ECO:0000256|PIRNR:PIRNR037393};
Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
Growth regulation {ECO:0000256|PIRNR:PIRNR037393};
Kinase {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00138186};
Magnesium {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
Manganese {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
Membrane {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00488859};
Metal-binding {ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|PIRSR:PIRSR037393-2, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00138218};
Receptor {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00138179};
Reference proteome {ECO:0000313|Proteomes:UP000002280};
Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037393,
ECO:0000256|RuleBase:RU361271, ECO:0000256|SAAS:SAAS00138186};
Signal {ECO:0000256|SAM:SignalP};
Transferase {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00138186};
Transmembrane {ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00488859};
Transmembrane helix {ECO:0000256|RuleBase:RU361271,
ECO:0000256|SAAS:SAAS00488859}.
SIGNAL 1..23
/evidence="ECO:0000256|SAM:SignalP"
CHAIN 24..564
/note="TGF-beta receptor type-2"
/evidence="ECO:0000256|SAM:SignalP"
/id="PRO_5003349482"
TRANSMEM 161..187
/note="Helical"
/evidence="ECO:0000256|RuleBase:RU361271"
DOMAIN 241..538
/note="Protein kinase"
/evidence="ECO:0000259|PROSITE:PS50011"
NP_BIND 247..255
/note="ATP"
/evidence="ECO:0000256|PIRSR:PIRSR037393-2"
ACT_SITE 376
/note="Proton acceptor"
/evidence="ECO:0000256|PIRSR:PIRSR037393-1"
BINDING 274
/note="ATP"
/evidence="ECO:0000256|PIRSR:PIRSR037393-2"
DISULFID 50..83
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 53..70
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 60..66
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 76..100
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 120..135
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
DISULFID 137..142
/evidence="ECO:0000256|PIRSR:PIRSR037393-3"
SEQUENCE 564 AA; 64128 MW; BCFFF375CE7D6025 CRC64;
MSRALLWSPG LLLLFLWTRN ASTIPPHVQK IVDGVPVTEE NGAIKSSLLC KFCDIQPSNC
TNDRSCPSYC GITSICEKAH EICVAVWRKN DKNITIETLC HDPSLEVHGF PLEDSNSDKC
IMREKKVPGE TFFMCSCRKE ECNDILFFSE DVLDNFDLMA IIFKVTVISL LPPLGIAIAV
IIIFYCYRVH RRRKLSTAWE TSKPGKPDYS EGCAMMLDDD RSDISSTCAN NLNHNTELLP
IELDTLVGKG RFAEVYKAKL KQNTSEQFET VAVKIFPYEE YASWKTEKEI FSDINLKHEN
ILQFLTAEER KMDLGKQYWL ITAFHARGNL QEYLTRHVIS WEDLWKLGSS LARGIAHLHS
DHTPCGRPKT AIVHRDLKSS NILVKNDLTC CLCDFGLSLR LDPTLSVDDL ANSGQVGTAR
YMAPEVLESR MNLENMESFK QTDVYSMALV LWEMTSRCNE IGEVKEYEPP FGSKVREHPC
VESMKDNVLR DRGRPEIPNT WLSHRGIQMV CETLAECWDH DPEARLTAQC VAERFDQLGD
LDRLSGRSCS EEKIPEDCSL SPTK


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