NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1002/(SICI)1098-2795(199801)49:1<1::AID-MRD1>3.3.CO;2-N; PubMed=9406190 [NCBI, ExPASy, EBI, Israel, Japan]
Roelen B.A.J., Van Eijk M.J.T., Van Rooijen M.A., Bevers M.M., Larson J.H., Lewin H.A., Mummery C.L.;
"Molecular cloning, genetic mapping, and developmental expression of a bovine transforming growth factor beta (TGF-beta) type I receptor.";
Mol. Reprod. Dev. 49:1-9(1998).

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 (By similarity).
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

U97485; AAC02717.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_777046.1; -.

UniGene

Bt.91785

3D structure databases

HSSP

P36897; 1IAS. [HSSP ENTRY / PDB]

SMR

O46680; 197-499.

ModBase

O46680.

Ontologies

GO:0005025;	Molecular function: transforming growth factor beta receptor activity, type I (inferred from sequence or structural similarity from AgBase).
GO:0007179;	Biological process: transforming growth factor beta receptor signaling pathway (inferred from sequence or structural similarity from AgBase).
QuickGo view.

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

O46680.

Genome annotation databases

Ensembl

ENSBTAG00000018035; Bos taurus. [Contig view]

GeneID

282382; -.

KEGG

bta:282382; -.

Phylogenomic databases

HOVERGEN

O46680; -.

Other

ProtoNet

O46680.

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 29`	`29`	`Potential.`
`CHAIN`	`30 499`	`470`	`TGF-beta receptor type-1.`	`PRO_0000254657`
`TOPO_DOM`	`30 122`	`93`	`Extracellular (Potential).`
`TRANSMEM`	`123 143`	`21`	`Potential.`
`TOPO_DOM`	`144 499`	`356`	`Cytoplasmic (Potential).`
`DOMAIN`	`171 200`	`30`	`GS.`
`DOMAIN`	`201 491`	`291`	`Protein kinase.`
`NP_BIND`	`207 215`	`9`	`ATP (By similarity).`
`ACT_SITE`	`329 329`		`Proton acceptor (By similarity).`
`BINDING`	`228 228`		`ATP (By similarity).`
`MOD_RES`	`181 181`		`Phosphothreonine (By similarity).`
`MOD_RES`	`182 182`		`Phosphothreonine (By similarity).`
`MOD_RES`	`183 183`		`Phosphoserine (By similarity).`
`MOD_RES`	`185 185`		`Phosphoserine (By similarity).`
`MOD_RES`	`187 187`		`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 96`		`By similarity.`
`DISULFID`	`97 102`		`By similarity.`

Sequence information

Length: 499 AA [This is the length of the unprocessed precursor]

Molecular weight: 55814 Da [This is the MW of the unprocessed precursor]

CRC64: 7FA311693CA938CD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEAAAATPRP RLFLLMLAAA ATLVPEATPL QCFCHLCTKD NFTCVTDGLC FVSVTETTDK 

        70         80         90        100        110        120 
VIHNSMCIAE IDLIPRDRPF VCAPSSKTGS ITTTYCCNQD HCNKIELPTV GKPSSGLGPV 

       130        140        150        160        170        180 
ELAAVIAGPV CFVCISLMLM VYICHNRTVI HHRVPNEEDP SLDRPFISEG TTLKDLIYDM 

       190        200        210        220        230        240 
TTSGSGSGLP LLVQRTIART IVLQESIGKG RFGEVWRGKW RGEEVAVKIF SSREERSWFR 

       250        260        270        280        290        300 
EAEIYQTVML RHENILGFIA ADNKDNGTWT QLWLVSDYHE HGSLFDYLNR YTVTVEGMIK 

       310        320        330        340        350        360 
LALSTASGLA HLHMEIVGTQ GKPAIAHRDL KSKNILVKKN GTCCIADLGL AVRHDSATDT 

       370        380        390        400        410        420 
IDIAPNHRVG TKRYMAPEVL DDSINMKHFE SFKRADIYAM GLVFWEVARR CSIGGIHEDY 

       430        440        450        460        470        480 
QLPYYDLVPS DPSVEEMRKV VCEQKLRPNI PNRWQSCEAL RVMAKIMREC WYANGAARLT 

       490 
ALRIKKTLSQ LSQQEGIKM

O46680 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