ID K7GL93_PIG Unreviewed; 567 AA.
AC K7GL93; A0A5K1VMN1; K9IVL4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=TGF-beta receptor type-2 {ECO:0000256|PIRNR:PIRNR037393};
DE Short=TGFR-2 {ECO:0000256|PIRNR:PIRNR037393};
DE EC=2.7.11.30 {ECO:0000256|PIRNR:PIRNR037393};
DE AltName: Full=TGF-beta type II receptor {ECO:0000256|PIRNR:PIRNR037393};
DE AltName: Full=Transforming growth factor-beta receptor type II {ECO:0000256|PIRNR:PIRNR037393};
GN Name=TGFBR2 {ECO:0000313|Ensembl:ENSSSCP00000028622.4,
GN ECO:0000313|VGNC:VGNC:93931};
GN Synonyms=TGFBR2_tv2 {ECO:0000313|EMBL:JAA53698.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000028622.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000028622.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000028622.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAA53698.1}
RP NUCLEOTIDE SEQUENCE.
RA Dawson H.D., Chen C.T.;
RT "Global Gene Expression Profiling of Alveolar Macrophages by Deep
RT Sequencing.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000028622.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-
CC beta type I serine/threonine kinase receptor, TGFBR1, the non-
CC promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3.
CC Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to
CC the cytoplasm and is thus regulating a plethora of physiological and
CC pathological processes including cell cycle arrest in epithelial and
CC hematopoietic cells, control of mesenchymal cell proliferation and
CC differentiation, wound healing, extracellular matrix production,
CC immunosuppression and carcinogenesis. The formation of the receptor
CC complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound
CC to the cytokine dimer results in the phosphorylation and the activation
CC of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1
CC phosphorylates SMAD2 which dissociates from the receptor and interacts
CC with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the
CC nucleus where it modulates the transcription of the TGF-beta-regulated
CC genes. This constitutes the canonical SMAD-dependent TGF-beta signaling
CC cascade. Also involved in non-canonical, SMAD-independent TGF-beta
CC signaling pathways. {ECO:0000256|PIRNR:PIRNR037393}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC Evidence={ECO:0000256|PIRNR:PIRNR037393,
CC ECO:0000256|RuleBase:RU361271};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR037393,
CC ECO:0000256|RuleBase:RU361271};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR037393,
CC ECO:0000256|RuleBase:RU361271};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479,
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|ARBA:ARBA00009605, ECO:0000256|PIRNR:PIRNR037393,
CC ECO:0000256|RuleBase:RU361271}.
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DR EMBL; GACC01000109; JAA53698.1; -; mRNA.
DR Ensembl; ENSSSCT00000035130.4; ENSSSCP00000028622.4; ENSSSCG00000011226.6.
DR VGNC; VGNC:93931; TGFBR2.
DR GeneTree; ENSGT00940000157527; -.
DR OMA; WTSHAGI; -.
DR OrthoDB; 3900892at2759; -.
DR TreeFam; TF314724; -.
DR Reactome; R-SSC-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-SSC-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-SSC-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000011226; Expressed in subcutaneous adipose tissue and 41 other cell types or tissues.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR GO; GO:0050431; F:transforming growth factor beta binding; IBA:GO_Central.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; IBA:GO_Central.
DR GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:UniProtKB-UniRule.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR CDD; cd14055; STKc_TGFbR2_like; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
DR PANTHER; PTHR23255:SF55; TGF-BETA RECEPTOR TYPE-2; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF08917; ecTbetaR2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF037393; TGFRII; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|PIRNR:PIRNR037393};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037393};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR037393};
KW Differentiation {ECO:0000256|PIRNR:PIRNR037393};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604,
KW ECO:0000256|PIRNR:PIRNR037393};
KW Kinase {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
KW Magnesium {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR037393};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037393};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR037393,
KW ECO:0000256|RuleBase:RU361271};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037393};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR037393};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR037393};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..567
FT /note="TGF-beta receptor type-2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014580475"
FT DOMAIN 244..544
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 545..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-1"
FT BINDING 250..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-2"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 51..84
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 54..71
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 61..67
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 77..101
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 121..136
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 138..143
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
SQ SEQUENCE 567 AA; 63931 MW; 177101142CEC726C CRC64;
MGRGLLGGLW PLHVVLWTRI ASTIPPHVPK SVNSDMMVTD SNGAVKLPQL CKFCDVRSST
CDNQKSCLSN CSITAICEKP QEVCVAVWRK NDENITIETV CHDPKIAYHG FVLDDAASSK
CIMKERKGSG ETFFMCSCSS DECNDHIIFS EEYATNNPDL LLVIFQVTGV SLLPPLGIAI
AVIITFYCYR VHRQQKLSPS WDSGKPRKLM EFSEHLAIIL EDDRSDISST CANNINHNTE
LLPIELDTLV GKGRFAEVYK AKLRQNTSEQ FETVAVKIFP YEEYASWKTE KDIFSDINLK
HENILQFLTA EERKTELGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRRL GGSLARGIAH
LHSDHTLCGR PKMPIVHRDL KSSNILVKGD LTCCLCDFGL SLRLDPTLSV DDLANSGQVG
TARYMAPEVL ESRMNLENVE SFKQTDVYSM ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE
HPCVESMKDN VLRDRGRPEI PSSWLNHQGI QTVCETLAEC WDHDPEARLT AQCVAERFSE
LEHLDRLSGR SSSEEKIPEH GSLNTTK
//
