EC 2.7.11.30
Transforming growth factor-beta receptor type I
TGF-beta receptor type I
TGF-beta type I receptor
TbetaR-I
TGFR-1
Serine/threonine-protein kinase receptor R4
SKR4

Gene name

Name:

Tgfbr1

From

Rattus norvegicus (Rat)

[TaxID: 10116]

Taxonomy

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

Protein existence

2: Evidence at transcript level;

References

[1]

NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Urogenital ridge;
PubMed=8395914 [NCBI, ExPASy, EBI, Israel, Japan]
He W.-W., Gustafson M.L., Hirobe S., Donahoe P.K.;
"Developmental expression of four novel serine/threonine kinase receptors homologous to the activin/transforming growth factor-beta type II receptor family.";
Dev. Dyn. 196:133-142(1993).

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: Interacts with CD109. The unphosphorylated protein interacts with FKBP1A and is stabilized the inactive conformation. Phosphorylation of the GS region abrogates FKBP1A binding. Interacts with SMAD2 when phosphorylated on several residues in the GS region (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
TISSUE SPECIFICITY: Urogenital ridge, testis, ovary, brain and lungs.
PTM: Phosphorylated at basal levels in the absence of ligand binding. Activated by multiple phosphorylation, mainly in the GS region (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
SIMILARITY: Contains 1 GS domain.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L26110; AAA83216.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Rn.44402

3D structure databases

HSSP

P36897; 1IAS. [HSSP ENTRY / PDB]

SMR

P80204; 199-501.

ModBase

P80204.

Organism-specific databases

RGD

3852; Tgfbr1.

GeneLynx

Tgfbr1; Rattus norvegicus.

Gene expression databases

ArrayExpress

P80204; -.

GermOnline

ENSRNOG00000007036; Rattus norvegicus.

Family and domain databases

InterPro

IPR000333; Activin_II_recpt.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR008271; Ser_thr_pkin_AS.
IPR003605; TGF_beta_rcpt_GS.
Graphical view of domain structure.

Pfam

PF01064; Activin_recp; 1.
PF08515; TGF_beta_GS; 1.
Pfam graphical view of domain structure.

PRINTS

PR00653; ACTIVIN2R.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00467; GS; 1.
SMART graphical view of domain structure.

PROSITE

PS51256; GS; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P80204.

Genome annotation databases

Ensembl

ENSRNOG00000007036; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P80204; -.

Other

ProtoNet

P80204.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`CHAIN`	`23 501`	`479`	`TGF-beta receptor type-1.`	`PRO_0000024425`
`TOPO_DOM`	`23 123`	`101`	`Extracellular (Potential).`
`TRANSMEM`	`124 146`	`23`	`Potential.`
`TOPO_DOM`	`147 501`	`355`	`Cytoplasmic (Potential).`
`DOMAIN`	`173 202`	`30`	`GS.`
`DOMAIN`	`203 493`	`291`	`Protein kinase.`
`NP_BIND`	`209 217`	`9`	`ATP (By similarity).`
`ACT_SITE`	`331 331`		`Proton acceptor (By similarity).`
`BINDING`	`230 230`		`ATP (By similarity).`
`MOD_RES`	`183 183`		`Phosphothreonine (By similarity).`
`MOD_RES`	`184 184`		`Phosphothreonine (By similarity).`
`MOD_RES`	`185 185`		`Phosphoserine (By similarity).`
`MOD_RES`	`187 187`		`Phosphoserine (By similarity).`
`MOD_RES`	`189 189`		`Phosphoserine (By similarity).`
`CARBOHYD`	`41 41`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`32 50`		`By similarity.`
`DISULFID`	`34 37`		`By similarity.`
`DISULFID`	`44 67`		`By similarity.`
`DISULFID`	`82 94`		`By similarity.`
`DISULFID`	`95 100`		`By similarity.`

Sequence information

Length: 501 AA [This is the length of the unprocessed precursor]

Molecular weight: 56000 Da [This is the MW of the unprocessed precursor]

CRC64: EAD7F8D37E456102 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEAASAALRR CLLLIVLVAA ATLLPGAKAL QCFCHLCTKD NFTCETDGLC FVSVTETTDK 

        70         80         90        100        110        120 
VIHNSMCIAE IDLIPRDRPF VCAPSSKTGA VTYCCNQDHC NKIELPTTGP FSEKQSAGLG 

       130        140        150        160        170        180 
PVELAAVIAG PVCFVCIALM LMVYICHNRT VIHHRVPNEE DPSLDRPFIS EGTTLKDLIY 

       190        200        210        220        230        240 
DMTTSGSGSG LPLLVQRTIA RTIVLQESIG KGRFGEVWRG KWRGEEVAVK IFSSREERSW 

       250        260        270        280        290        300 
FREAEIYQTV MLRHENILGF IAADNKDNGT WTQLWLVSDY HEHGSLFDYL NRYTVTVEGM 

       310        320        330        340        350        360 
IKLALSTASG LAHLHMEIVG TQGKPAIAHR DLKSKNILVK KNGTCCIADL GLAVRHDSAT 

       370        380        390        400        410        420 
DTIDIAPNHR VGTKRYMAPE VLDDSINMKH FESFKRADIY AMGLVFWEIA RRCSIGGIHE 

       430        440        450        460        470        480 
DYQLPYYDLV PSDPSVEEMR KVVCEQKLRP NIPNRWQSCE ALRVMAKIMR ECWYANGAAR 

       490        500 
LTALRIKKTL SQLSQQEGIK M

P80204 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools