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Protein

Activin receptor type-2B

Gene

Acvr2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei217ATPPROSITE-ProRule annotation1
Active sitei322Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi196 – 204ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • activin binding Source: RGD
  • ATP binding Source: UniProtKB-KW
  • inhibin binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • receptor signaling protein serine/threonine kinase activity Source: InterPro
  • transmembrane receptor protein serine/threonine kinase activity Source: RGD

GO - Biological processi

  • protein phosphorylation Source: RGD
  • sexual reproduction Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Activin receptor type-2B (EC:2.7.11.30)
Alternative name(s):
Activin receptor type IIB
Short name:
ACTR-IIB
Gene namesi
Name:Acvr2b
Synonyms:Actriib
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2028. Acvr2b.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 137ExtracellularSequence analysisAdd BLAST119
Transmembranei138 – 158HelicalSequence analysisAdd BLAST21
Topological domaini159 – 513CytoplasmicSequence analysisAdd BLAST355

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000002440619 – 513Activin receptor type-2BAdd BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi29 ↔ 59Combined sources1 Publication
Glycosylationi42N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi49 ↔ 77Combined sources1 Publication
Glycosylationi65N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi84 ↔ 103Combined sources1 Publication
Disulfide bondi90 ↔ 102Combined sources1 Publication
Disulfide bondi104 ↔ 109Combined sources1 Publication

Post-translational modificationi

Phosphorylated. Constitutive phosphorylation is in part catalyzed by its own kinase activity (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP38445.
PRIDEiP38445.

PTM databases

PhosphoSitePlusiP38445.

Expressioni

Gene expression databases

BgeeiENSRNOG00000014477.

Interactioni

Subunit structurei

Forms an activin receptor complex with activin type II receptors such as ACVR1B. Interacts with VPS39.By similarity

GO - Molecular functioni

  • activin binding Source: RGD
  • inhibin binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019777.

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 33Combined sources6
Turni34 – 40Combined sources7
Beta strandi43 – 48Combined sources6
Beta strandi57 – 65Combined sources9
Beta strandi70 – 79Combined sources10
Helixi82 – 84Combined sources3
Beta strandi89 – 92Combined sources4
Beta strandi98 – 104Combined sources7
Helixi109 – 111Combined sources3
Beta strandi112 – 115Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NYSX-ray3.05A/C19-119[»]
1NYUX-ray3.10A/C19-119[»]
ProteinModelPortaliP38445.
SMRiP38445.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38445.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini190 – 481Protein kinasePROSITE-ProRule annotationAdd BLAST292

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3653. Eukaryota.
ENOG410XS2Z. LUCA.
HOGENOMiHOG000231495.
HOVERGENiHBG054502.
InParanoidiP38445.
KOiK13596.

Family and domain databases

InterProiIPR000472. Activin_recp.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00653. ACTIVIN2R.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38445-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE
60 70 80 90 100
GEQDKRLHCY ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY
110 120 130 140 150
FCCCEGNFCN ERFTHLPEPG GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS
160 170 180 190 200
LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP PSPLVGLKPL QLLEIKARGR
210 220 230 240 250
FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK HENLLQFIAA
260 270 280 290 300
EKRGCSNLEV ELWLITAFHD KGSLTDYLKG NIITWNELCH VAETMSRGLS
310 320 330 340 350
YLHEDVPWCR GEGHKPSIAH RDFKSKNVLL KSDLTAVLAD FGLAVRFEPG
360 370 380 390 400
KPPGDTHGQV GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELVSR
410 420 430 440 450
CKAADGPVDE YMLPFEEEIG QHPSLEELQE VVVHKKMRPT IKDHWLKHPG
460 470 480 490 500
LAQLCVTIEE CWDHDAEARL SAGCVEERVS LIRRSVNSST SDCLVSLVTS
510
VTNVDLLPKE SSI
Length:513
Mass (Da):57,857
Last modified:November 13, 2007 - v3
Checksum:i765DB33F11C64CA7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64R → P in AAA40772 (PubMed:1312838).Curated1
Sequence conflicti64R → P (PubMed:7916681).Curated1
Sequence conflicti255Missing (PubMed:7916681).Curated1
Sequence conflicti255Missing in AAH97358 (PubMed:15489334).Curated1
Sequence conflicti488S → G in AAA40772 (PubMed:1312838).Curated1
Sequence conflicti488S → G (PubMed:7916681).Curated1
Sequence conflicti501V → S in AAA40772 (PubMed:1312838).Curated1
Sequence conflicti501V → S (PubMed:7916681).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10640 mRNA. Translation: AAA40772.1.
BC097358 mRNA. Translation: AAH97358.1.
PIRiB49193.
JQ1484.
RefSeqiNP_113742.1. NM_031554.1.
UniGeneiRn.24240.

Genome annotation databases

GeneIDi25366.
KEGGirno:25366.
UCSCiRGD:2028. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10640 mRNA. Translation: AAA40772.1.
BC097358 mRNA. Translation: AAH97358.1.
PIRiB49193.
JQ1484.
RefSeqiNP_113742.1. NM_031554.1.
UniGeneiRn.24240.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NYSX-ray3.05A/C19-119[»]
1NYUX-ray3.10A/C19-119[»]
ProteinModelPortaliP38445.
SMRiP38445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019777.

PTM databases

PhosphoSitePlusiP38445.

Proteomic databases

PaxDbiP38445.
PRIDEiP38445.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25366.
KEGGirno:25366.
UCSCiRGD:2028. rat.

Organism-specific databases

CTDi93.
RGDi2028. Acvr2b.

Phylogenomic databases

eggNOGiKOG3653. Eukaryota.
ENOG410XS2Z. LUCA.
HOGENOMiHOG000231495.
HOVERGENiHBG054502.
InParanoidiP38445.
KOiK13596.

Miscellaneous databases

EvolutionaryTraceiP38445.
PROiP38445.

Gene expression databases

BgeeiENSRNOG00000014477.

Family and domain databases

InterProiIPR000472. Activin_recp.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00653. ACTIVIN2R.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAVR2B_RAT
AccessioniPrimary (citable) accession number: P38445
Secondary accession number(s): Q4V8J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 13, 2007
Last modified: November 2, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.