[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8400359 [NCBI, ExPASy, EBI, Israel, Japan] Yamazaki Y., Saito T., Nohno T.; "A new receptor protein kinase from chick embryo related to type II receptor for TGF-beta."; DNA Seq. 3:297-302(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 (By similarity).
CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
COFACTOR: Magnesium or manganese (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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

D13432; BAA02694.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A56683; A56683.

NP_990463.1; -.

3D structure databases

HSSP

P36897; 1IAS. [HSSP ENTRY / PDB]

ModBase

Q05438.

Protein-protein interaction databases

DIP

DIP:5822N; -.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000333; Activin_II_recpt.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR003605; TGF_beta_rcpt_GS.
Graphical view of domain structure.

Pfam

PF01064; Activin_recp; 1.
PF00069; Pkinase; 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).

Genome annotation databases

Ensembl

ENSGALG00000012216; Gallus gallus. [Contig view]

GeneID

396030; -.

KEGG

gga:396030; -.

Phylogenomic databases

HOGENOM

Q05438; -.

HOVERGEN

Q05438; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 13`	`13`	`Potential.`
`CHAIN`	`14 502`	`489`	`Bone morphogenetic protein receptor type-1B.`	`PRO_0000024414`
`TOPO_DOM`	`14 126`	`113`	`Extracellular (Potential).`
`TRANSMEM`	`127 148`	`22`	`Potential.`
`TOPO_DOM`	`149 502`	`354`	`Cytoplasmic (Potential).`
`DOMAIN`	`174 203`	`30`	`GS.`
`DOMAIN`	`204 494`	`291`	`Protein kinase.`
`NP_BIND`	`210 218`	`9`	`ATP (By similarity).`
`ACT_SITE`	`332 332`		`Proton acceptor (By similarity).`
`BINDING`	`231 231`		`ATP (By similarity).`
`CARBOHYD`	`44 44`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 502 AA [This is the length of the unprocessed precursor]

Molecular weight: 56766 Da [This is the MW of the unprocessed precursor]

CRC64: D5D93CCEBF2A0680 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPLLSSSKLS MESRKEDSEG TAPAPPQKKL SCQCHHHCPE DSVNSTCSTD GYCFTIIEED 

        70         80         90        100        110        120 
DSGGHLVTKG CLGLEGSDFQ CRDTPIPHQR RSIECCTGQD YCNKHLHPTL PPLKNRDFAE 

       130        140        150        160        170        180 
GNIHHKALLI SVTVCSILLV LIIIFCYFRY KRQEARPRYS IGLEQDETYI PPGESLKDLI 

       190        200        210        220        230        240 
EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS 

       250        260        270        280        290        300 
WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDTKG 

       310        320        330        340        350        360 
MLKLAYSSVS GLCHLHTGIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD 

       370        380        390        400        410        420 
TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEI ARRCVSGGIV 

       430        440        450        460        470        480 
EEYQLPYHDL VPSDPSYEDM REIVCIKRLR PSFPNRWSSD ECLRQMGKLM MECWAHNPAS 

       490        500 
RLTALRVKKT LAKMSESQDI KL

Q05438 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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