NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS SER-8 AND VAL-417.
TISSUE=Testis;
DOI=10.1007/s10528-005-8165-0; PubMed=16341765 [NCBI, ExPASy, EBI, Israel, Japan]
Shimanuki S., Mikawa A., Miyake Y., Hamasima N., Mikawa S., Awata T.;
"Structure and polymorphism analysis of transforming growth factor beta receptor 1 (TGFBR1) in pigs.";
Biochem. Genet. 43:491-500(2005).

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 (By similarity).
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).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q5CD18-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q5CD18-2
Note: May be due to a competing donnor splice site.
Features which should be applied to build the isoform sequence: VSP_021594.

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

AB182259; BAD91022.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB182260; BAD91023.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001033728.1; -.

UniGene

Ssc.23794

3D structure databases

SMR

Q5CD18; 201-503.

ModBase

Q5CD18.

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

Q5CD18.

Genome annotation databases

GeneID

396665; -.

KEGG

ssc:396665; -.

Phylogenomic databases

HOVERGEN

Q5CD18; -.

Other

ProtoNet

Q5CD18.

UniRef

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

Keywords

Alternative splicing; ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; 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`	`30 503`	`474`	`TGF-beta receptor type-1.`	`PRO_0000260305`
`TOPO_DOM`	`30 126`	`97`	`Extracellular (Potential).`
`TRANSMEM`	`127 147`	`21`	`Potential.`
`TOPO_DOM`	`148 503`	`356`	`Cytoplasmic (Potential).`
`DOMAIN`	`175 204`	`30`	`GS.`
`DOMAIN`	`205 495`	`291`	`Protein kinase.`
`NP_BIND`	`211 219`	`9`	`ATP (By similarity).`
`ACT_SITE`	`333 333`		`Proton acceptor (By similarity).`
`BINDING`	`232 232`		`ATP (By similarity).`
`MOD_RES`	`185 185`		`Phosphothreonine (By similarity).`
`MOD_RES`	`186 186`		`Phosphothreonine (By similarity).`
`MOD_RES`	`187 187`		`Phosphoserine (By similarity).`
`MOD_RES`	`189 189`		`Phosphoserine (By similarity).`
`MOD_RES`	`191 191`		`Phosphoserine (By similarity).`
`CARBOHYD`	`41 41`		`N-linked (GlcNAc...) (Potential).`
`VAR_SEQ`	`111 114`		`Missing (in isoform 2).`	`VSP_021594`
`VARIANT`	`8 8`	`1`	`P -> S.`
`VARIANT`	`417 417`	`1`	`I -> V.`

Sequence information

Length: 503 AA [This is the length of the unprocessed precursor]

Molecular weight: 56174 Da [This is the MW of the unprocessed precursor]

CRC64: CFA1EEC793401A4A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEVAAGAPRS RLLLFVLAAT ATLAPEATAF QCFCHLCTKD NFTCVTDGLC FVSVTETTDK 

        70         80         90        100        110        120 
VIHNSMCIAE IDLIPRDRPF VCAPSSKTGS VTTTYCCNQD HCNKIELPTV GPFPGKPPSG 

       130        140        150        160        170        180 
LGPVELAAVI AGPVCFVCIS LMLMVYICHN RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL 

       190        200        210        220        230        240 
IYDMTTSGSG SGLPLLVQRT IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER 

       250        260        270        280        290        300 
SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE 

       310        320        330        340        350        360 
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA DLGLAVRHDS 

       370        380        390        400        410        420 
ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD IYAMGLVFWE IARRCSIGGI 

       430        440        450        460        470        480 
HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL RPNIPNRWQS CEALRVMAKI MRECWYANGA 

       490        500 
ARLTALRIKK TLSQLSQQEG IKM

Q5CD18 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