NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=NIH Swiss;
TISSUE=Placenta;
DOI=10.1016/0925-4773(95)00395-H; PubMed=7577669 [NCBI, ExPASy, EBI, Israel, Japan]
Verschuern K., Dewulf N., Goumans M.J., Lonnoy O., Freijen A., Grimsby S., Vande Spiegle K., ten Dijke P., Moren A., Vanscheeuwijck P., Heldin C.H., Miyazono K., Mummery C., Van Den Eijnden-Van Raaij J., Huylebroeck D.;
"Expression of type I and type IB receptors for activin in midgestation mouse embryos suggests distinct functions in organogensis.";
Mech. Dev. 52:109-123(1995).

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.
CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
COFACTOR: Magnesium or manganese (By similarity).
SUBUNIT: Interacts with AIP1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (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

Z31663; CAA83483.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_031421.1; -.

UniGene

Mm.308467

3D structure databases

HSSP

P36897; 1B6C. [HSSP ENTRY / PDB]

SMR

Q61271; 178-501.

ModBase

Q61271.

Organism-specific databases

MGI

MGI:1338944; Acvr1b.

Gene expression databases

ArrayExpress

Q61271; -.

CleanEx

MM_ACVR1B; -.

GermOnline

ENSMUSG00000000532; Mus musculus.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from MGI).
GO:0048185;	Molecular function: activin binding (inferred from physical interaction from MGI).
GO:0007166;	Biological process: cell surface receptor linked signal transduction (traceable author statement from MGI).
GO:0001942;	Biological process: hair follicle development (inferred from mutant phenotype from MGI).
GO:0001701;	Biological process: in utero embryonic development (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

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.

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

Q61271.

Genome annotation databases

Ensembl

ENSMUSG00000000532; Mus musculus. [Contig view]

GeneID

11479; -.

KEGG

mmu:11479; -.

Phylogenomic databases

HOGENOM

Q61271; -.

HOVERGEN

Q61271; -.

Other

SOURCE

Acvr1b; Mus musculus.

ProtoNet

Q61271.

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 23`	`23`	`Potential.`
`CHAIN`	`24 505`	`482`	`Activin receptor type-1B.`	`PRO_0000024418`
`TOPO_DOM`	`24 126`	`103`	`Extracellular (Potential).`
`TRANSMEM`	`127 149`	`23`	`Potential.`
`TOPO_DOM`	`150 505`	`356`	`Cytoplasmic (Potential).`
`DOMAIN`	`177 206`	`30`	`GS.`
`DOMAIN`	`207 497`	`291`	`Protein kinase.`
`NP_BIND`	`213 221`	`9`	`ATP (By similarity).`
`ACT_SITE`	`335 335`		`Proton acceptor (By similarity).`
`BINDING`	`234 234`		`ATP (By similarity).`
`MOD_RES`	`380 380`		`Phosphotyrosine (By similarity).`
`CARBOHYD`	`43 43`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 505 AA [This is the length of the unprocessed precursor]

Molecular weight: 56700 Da [This is the MW of the unprocessed precursor]

CRC64: 56E9EEF1607A2517 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAESAGASSF FPLVVLLLAG SGGSGPRGIQ ALLCACTSCL QTNYTCETDG ACMVSIFNLD 

        70         80         90        100        110        120 
GVEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYIDF CNKIDLRVPS GHLKEPAHPS 

       130        140        150        160        170        180 
MWGPVELVGI IAGPVFLLFL IIIIVFLVIN YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ 

       190        200        210        220        230        240 
DLVYDLSTSG SGSGLPLFVQ RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE 

       250        260        270        280        290        300 
ERSWFREAEI YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT 

       310        320        330        340        350        360 
IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA IADLGLAVRH 

       370        380        390        400        410        420 
DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC ADIYALGLVY WEIARRCNSG 

       430        440        450        460        470        480 
GVHEDYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNVPNWW QSYEALRVMG KMMRECWYAN 

       490        500 
GAARLTALRI KKTLSQLSVQ EDVKI

Q61271 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