Reviewed, UniProtKB/Swiss-Prot P38438 (TGFR2_RAT)

Names and origin

Protein names

Recommended name:
    TGF-beta receptor type-2
    EC=2.7.11.30
Alternative name(s):
    Transforming growth factor-beta receptor type II
      Short name=TGF-beta receptor type II
    TGF-beta type II receptor
    TbetaR-II
    TGFR-2

Gene names

Name:

Tgfbr2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for TGF-beta.
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Binds to DAXX. Interacts with TCTEX1D4 By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Post-translational modification	Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal Transmembrane
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	aging Inferred from expression pattern. Source: RGD common-partner SMAD protein phosphorylation Inferred from direct assay. Source: RGD embryo implantation Inferred from expression pattern. Source: RGD embryonic development Inferred from expression pattern. Source: RGD gut development Inferred from expression pattern. Source: RGD lung development Inferred from expression pattern. Source: RGD negative regulation of cardiac muscle cell proliferation Inferred from mutant phenotype. Source: RGD organ regeneration Inferred from expression pattern. Source: RGD positive regulation of skeletal muscle regeneration Inferred from expression pattern. Source: RGD positive regulation of smooth muscle cell proliferation Inferred from mutant phenotype. Source: RGD receptor-mediated endocytosis Inferred from direct assay. Source: RGD response to estrogen stimulus Inferred from expression pattern. Source: RGD response to glucose stimulus Inferred from expression pattern. Source: RGD response to hypoxia Inferred from expression pattern. Source: RGD response to mechanical stimulus Inferred from expression pattern. Source: RGD response to nutrient Inferred from expression pattern. Source: RGD response to organic cyclic substance Inferred from expression pattern. Source: RGD vasculogenesis Inferred from expression pattern. Source: RGD wound healing Inferred from expression pattern. Source: RGD
Cellular component	caveola Inferred from mutant phenotype. Source: RGD cell surface Inferred from direct assay. Source: RGD cytosol Inferred from direct assay. Source: RGD transforming growth factor beta receptor complex Inferred by curator. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW mitogen-activated protein kinase kinase kinase binding Inferred from physical interaction. Source: RGD protein heterodimerization activity Traceable author statement. Source: RGD protein homodimerization activity Traceable author statement. Source: RGD transforming growth factor beta receptor activity, type II Inferred from mutant phenotype. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 567	544	TGF-beta receptor type-2		PRO_0000024429
Regions
	Topological domain	24 – 166	143	Extracellular Potential
	Transmembrane	167 – 187	21	Potential
	Topological domain	188 – 567	380	Cytoplasmic Potential
	Domain	244 – 546	303	Protein kinase
	Nucleotide binding	250 – 258	9	ATP By similarity
Sites
	Active site	379	1	Proton acceptor By similarity
	Binding site	277	1	ATP By similarity
Amino acid modifications
	Modified residue	548	1	Phosphoserine By similarity
	Glycosylation	70	1	N-linked (GlcNAc...) Potential
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 84		By similarity
	Disulfide bond	54 ↔ 71		By similarity
	Disulfide bond	61 ↔ 67		By similarity
	Disulfide bond	77 ↔ 101		By similarity
	Disulfide bond	121 ↔ 136		By similarity
	Disulfide bond	138 ↔ 143		By similarity
Experimental info
	Sequence conflict	388 – 389	2	KN → RS in AAB29352. Ref.2
	Sequence conflict	403	1	R → G Ref.2
	Sequence conflict	405	1	D → S Ref.2
	Sequence conflict	477	1	K → R in AAB29352. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P38438-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: EC1D7642A51A3B75	FASTA	567	64,241
	10 20 30 40 50 60 MGRGLLRGLW PLHIVLWTRI ASTIPPHVPK SVNSDLMAGD NSGAVKLPQL CKFCDVTLST 70 80 90 100 110 120 CDNQKSCMSN CSVTSICEKP QEVCVAVWRK NDKNITLETV CHDPKFTYHG FTLEDATSPT 130 140 150 160 170 180 CVMKEKKRAG ETFFMCSCNT EECNDYIIFN EEYTTSSPDL LLVIIQVTGV SLLPPLGIAI 190 200 210 220 230 240 AVIAIFYCYR VHRQQKLSPS WESSKPRKLM DFSDNCAIIL EDDRSDISST CANNINHNTE 250 260 270 280 290 300 LLPIELDTLV GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYSSWKTE KDIFSDINLK 310 320 330 340 350 360 HENILQFLTA EERKTEMGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL GSSLARGIAH 370 380 390 400 410 420 LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPTLSV DDLANSGQVG 430 440 450 460 470 480 TARYMAPEVL ESRMNLENME SFKQTDVYSM ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE 490 500 510 520 530 540 HPCVESMKDN VLRDRGRPEI PSFWLNHQGI QIVCETLTEC WDHDPEARLT AQCVAERFSE 550 560 LEHPDRLSGR SCSQEKIPED GSLNTTK

References

[1]	"Molecular characterization of rat transforming growth factor-beta type II receptor." Tsuchida K., Lewis K.A., Mathews L.S., Vale W.W. Biochem. Biophys. Res. Commun. 191:790-795(1993) [PubMed: 8385453] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Pituitary.
[2]	"Rat mesangial cell hypertrophy in response to transforming growth factor-beta 1." Choi M.E., Kim E.G., Huang Q., Ballermann B.J. Kidney Int. 44:948-958(1993) [PubMed: 8264154] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L09653 mRNA. Translation: AAA42237.1. S67770 mRNA. Translation: AAB29352.2.
IPI	IPI00327360.
PIR	JN0459.
RefSeq	NP_112394.3.
UniGene	Rn.9954
3D structure databases
HSSP	HSSP built from PDB template 1M9Z based on UniProtKB P37173.
SMR	P38438. Positions 40-159.
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000013265. Rattus norvegicus. [Contig view]
GeneID	81810.
KEGG	rno:81810.
Organism-specific databases
RGD	69651. Tgfbr2.
Phylogenomic databases
HOVERGEN	P38438.
Enzyme and pathway databases
BRENDA	2.7.10.2. 248. 2.7.11.30. 248.
Gene expression databases
ArrayExpress	P38438.
GermOnline	ENSRNOG00000013265. Rattus norvegicus.
Family and domain databases
InterPro	IPR000333. Activin_II_recpt. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR015769. TGF-beta-2_rcpt_C. IPR017194. Transform_growth_fac-b_typ-2. IPR015013. Transforming_GF_b_rcpt_2_ecto. [Graphical view]
PANTHER	PTHR23255:SF11. TGF-beta_II_C. 1 hit.
Pfam	PF08917. ecTbetaR2. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
PIRSF	PIRSF037393. TGFRII. 1 hit.
PRINTS	PR00653. ACTIVIN2R.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	615691.

Entry information

Entry name

TGFR2_RAT

Accession

Primary (citable) accession number: P38438

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)