Activin receptor type-2B precursor - Rattus norvegicus (Rat)

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P38445 (AVR2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Activin receptor type-2B
EC=2.7.11.30

Alternative name(s):
Activin receptor type IIB
Short name=ACTR-IIB

Gene names

Name:	Acvr2b
Synonyms:	Actriib

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor By similarity.
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Forms an activin receptor complex with activin type II receptors such as ACVR1B By similarity. Interacts with VPS39 By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity.
Post-translational modification	Phosphorylated. Constitutive phosphorylation is in part catalyzed by its own kinase activity By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from electronic annotation. Source: Compara activation of protein kinase activity Inferred from electronic annotation. Source: Compara anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara artery development Inferred from electronic annotation. Source: Compara blood vessel remodeling Inferred from electronic annotation. Source: Compara determination of left/right symmetry Inferred from electronic annotation. Source: Compara embryonic foregut morphogenesis Inferred from electronic annotation. Source: Compara gastrulation with mouth forming second Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara insulin secretion Inferred from electronic annotation. Source: Compara kidney development Inferred from electronic annotation. Source: Compara lung development Inferred from electronic annotation. Source: Compara lymphangiogenesis Inferred from electronic annotation. Source: Compara lymphatic endothelial cell differentiation Inferred from electronic annotation. Source: Compara mesoderm development Inferred from electronic annotation. Source: Compara odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara organ growth Inferred from electronic annotation. Source: Compara palate development Inferred from electronic annotation. Source: Compara pancreas development Inferred from electronic annotation. Source: Compara positive regulation of activin receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of bone mineralization Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara retina vasculature development in camera-type eye Inferred from electronic annotation. Source: Compara sexual reproduction Non-traceable author statement Ref.2. Source: RGD signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC skeletal system morphogenesis Inferred from electronic annotation. Source: Compara venous blood vessel development Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW activin binding Inferred from direct assay PubMed 12385827. Source: RGD activin-activated receptor activity Inferred from electronic annotation. Source: InterPro inhibin binding Inferred from direct assay PubMed 12385827. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: Compara receptor signaling protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro transforming growth factor beta-activated receptor activity Inferred from electronic annotation. Source: InterPro transmembrane receptor protein serine/threonine kinase activity Traceable author statement PubMed 12770730. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Potential

Chain

19 – 513

495

Activin receptor type-2B

PRO_0000024406

Regions

Topological domain

19 – 137

119

Extracellular Potential

Transmembrane

138 – 158

Helical; Potential

Topological domain

159 – 513

355

Cytoplasmic Potential

Domain

190 – 481

292

Protein kinase

Nucleotide binding

196 – 204

ATP By similarity

Sites

Active site

322

Proton acceptor By similarity

Binding site

217

ATP By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

29 ↔ 59

By similarity

Disulfide bond

49 ↔ 77

By similarity

Disulfide bond

84 ↔ 103

By similarity

Disulfide bond

90 ↔ 102

By similarity

Disulfide bond

104 ↔ 109

By similarity

Experimental info

Sequence conflict

R → P in AAA40772. Ref.1

Sequence conflict

R → P Ref.2

Sequence conflict

255

Missing Ref.2

Sequence conflict

255

Missing in AAH97358. Ref.3

Sequence conflict

488

S → G in AAA40772. Ref.1

Sequence conflict

488

S → G Ref.2

Sequence conflict

501

V → S in AAA40772. Ref.1

Sequence conflict

501

V → S Ref.2

Secondary structure

513

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P38445 [UniParc].

Last modified November 13, 2007. Version 3.
Checksum: 765DB33F11C64CA7
Show »

FASTA

513

57,857

        10         20         30         40         50         60 
MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY 

        70         80         90        100        110        120 
ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEPG 

       130        140        150        160        170        180 
GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP 

       190        200        210        220        230        240 
PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK 

       250        260        270        280        290        300 
HENLLQFIAA EKRGCSNLEV ELWLITAFHD KGSLTDYLKG NIITWNELCH VAETMSRGLS 

       310        320        330        340        350        360 
YLHEDVPWCR GEGHKPSIAH RDFKSKNVLL KSDLTAVLAD FGLAVRFEPG KPPGDTHGQV 

       370        380        390        400        410        420 
GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELVSR CKAADGPVDE YMLPFEEEIG 

       430        440        450        460        470        480 
QHPSLEELQE VVVHKKMRPT IKDHWLKHPG LAQLCVTIEE CWDHDAEARL SAGCVEERVS 

       490        500        510 
LIRRSVNSST SDCLVSLVTS VTNVDLLPKE SSI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a novel rat activin receptor." Legerski R., Zhou X., Dresback J., Eberspaecher H., McKinney S., Segarini P., de Crombrugghe B. Biochem. Biophys. Res. Commun. 183:672-679(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Expression of type II activin receptor genes in the male and female reproductive tissues of the rat." Feng Z.M., Madigan M.B., Chen C.L.C. Endocrinology 132:2593-2600(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[4]	"Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions." Thompson T.B., Woodruff T.K., Jardetzky T.S. EMBO J. 22:1555-1566(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 19-119 IN COMPLEX WITH HUMAN INHBA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L10640 mRNA. Translation: AAA40772.1.
BC097358 mRNA. Translation: AAH97358.1.

IPI

IPI00231510.

PIR

B49193.
JQ1484.

RefSeq

NP_113742.1. NM_031554.1.

UniGene

Rn.24240.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NYS	X-ray	3.05	A/C	19-119	[»]
1NYU	X-ray	3.10	A/C	19-119	[»]

ProteinModelPortal

P38445.

SMR

P38445. Positions 26-120, 190-485.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000049841.

Proteomic databases

PaxDb

P38445.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000019777; ENSRNOP00000019777; ENSRNOG00000014477.

GeneID

25366.

KEGG

rno:25366.

UCSC

RGD:2028. rat.

Organism-specific databases

CTD

93.

RGD

2028. Acvr2b.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00560000076906.

HOGENOM

HOG000231495.

HOVERGEN

HBG054502.

K13596.

Gene expression databases

ArrayExpress

P38445.

Genevestigator

P38445.

GermOnline

ENSRNOG00000014477. Rattus norvegicus.

Family and domain databases

InterPro

IPR000333. Activin_II/TGFBeta-II_recpt.
IPR015768. Activin_II_recpt.
IPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

PANTHER

PTHR23255:SF10. PTHR23255:SF10. 1 hit.

Pfam

PF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR00653. ACTIVIN2R.

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P38445.

NextBio

606365.

Entry information

Entry name

AVR2B_RAT

Accession

Primary (citable) accession number: P38445
Secondary accession number(s): Q4V8J8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 13, 2007
Last modified:	April 3, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents