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Protein

Activin receptor type-2B

Gene

ACVR2B

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activin A, activin B and inhibin A. May modulate neuropeptide expression in dorsal root ganglia (DRG) neurons and ovarian follicle development.4 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei217 – 2171ATPPROSITE-ProRule annotation
Active sitei321 – 3211Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2049ATPPROSITE-ProRule annotation

GO - Molecular functioni

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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 137113ExtracellularSequence AnalysisAdd
BLAST
Transmembranei138 – 15821HelicalSequence AnalysisAdd
BLAST
Topological domaini159 – 512354CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 512488Activin receptor type-2BPRO_0000269546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 59By similarity
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi49 ↔ 77By similarity
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi84 ↔ 103By similarity
Disulfide bondi90 ↔ 102By similarity
Disulfide bondi104 ↔ 109By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ90670.

Expressioni

Tissue specificityi

Not expressed in hen anterior pituitary during the ovulatory cycle but expressed in the ovarian follicle.2 Publications

Developmental stagei

Expressed during the differentiation of neuroepithelium, of myotomes to muscle and of surface extoderm. Expressed in the dorsal root ganglia (DRG).3 Publications

Inductioni

By activin.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000030643.

Structurei

3D structure databases

ProteinModelPortaliQ90670.
SMRiQ90670. Positions 24-117, 190-484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini190 – 478289Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi128 – 1336Poly-Pro
Compositional biasi176 – 1838Poly-Pro

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000231495.
HOVERGENiHBG054502.
InParanoidiQ90670.
KOiK13596.
PhylomeDBiQ90670.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000472. TFB_recept_I/II_C.
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.

Q90670-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASWLTLAV LCATLGAGPG HGEAETRECI YYNANWELEK TNQSGVERCE
60 70 80 90 100
GEKDKRLHCY ASWRNNSGSI ELVKKGCWLD DFNCYDRQEC VATEENPQVF
110 120 130 140 150
FCCCEGNYCN EKFTHLPEVT GPEVIYEPPP PTPSLLNILV YSLLPIAVLS
160 170 180 190 200
VAILLAFWMY RHRKPPYGHV DINEDPGPPP PSPLVGLKPL QLLEIKARGR
210 220 230 240 250
FGCVWKAQLM NDYVAVKIFP IQDKQSWQSE REIFNTPGMK HENLLQFIAA
260 270 280 290 300
EKRGTNLETE LWLITAFHDK GSLTDYLKGN IISWNELCHV AETMARGLSY
310 320 330 340 350
LHEDVPWCKG EGHKPAIAHR DFKSKNVLLK NDLTAVLADF GLAVRFEPGK
360 370 380 390 400
PPGDTHGQVG TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC
410 420 430 440 450
RAVDGPVDEY MLPFEEEIGQ HPSLEDLQEV VVHKKMRPVF KDHWLKHPGL
460 470 480 490 500
AQLCVTIEEC WDHDAEARLS AGCVEERIAQ IRKSVNGTTS DCLVSIVTSV
510
TNVDLPPKES SI
Length:512
Mass (Da):57,776
Last modified:November 1, 1996 - v1
Checksum:i6051F0CBE94AE060
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31223 mRNA. Translation: AAA87842.1.
RefSeqiNP_989648.1. NM_204317.1.
UniGeneiGga.764.

Genome annotation databases

GeneIDi374213.
KEGGigga:374213.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31223 mRNA. Translation: AAA87842.1.
RefSeqiNP_989648.1. NM_204317.1.
UniGeneiGga.764.

3D structure databases

ProteinModelPortaliQ90670.
SMRiQ90670. Positions 24-117, 190-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000030643.

Proteomic databases

PaxDbiQ90670.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi374213.
KEGGigga:374213.

Organism-specific databases

CTDi93.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000231495.
HOVERGENiHBG054502.
InParanoidiQ90670.
KOiK13596.
PhylomeDBiQ90670.

Miscellaneous databases

NextBioi20813717.
PROiQ90670.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000472. TFB_recept_I/II_C.
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...

Publicationsi

  1. "Activin and its receptors during gastrulation and the later phases of mesoderm development in the chick embryo."
    Stern C.D., Yu R.T., Kakizuka A., Kintner C.R., Mathews L.S., Vale W.W., Evans R.M., Umesono K.
    Dev. Biol. 172:192-205(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, FUNCTION, INDUCTION.
  2. "Activin type II receptors in embryonic dorsal root ganglion neurons of the chicken."
    Kos K., Fine L., Coulombe J.N.
    J. Neurobiol. 47:93-108(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  3. "The activin signaling pathway promotes differentiation of dI3 interneurons in the spinal neural tube."
    Timmer J., Chesnutt C., Niswander L.
    Dev. Biol. 285:1-10(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  4. "Variation in pituitary expression of mRNAs encoding the putative inhibin co-receptor (betaglycan) and type-I and type-II activin receptors during the chicken ovulatory cycle."
    Lovell T.M., Knight P.G., Gladwell R.T.
    J. Endocrinol. 186:447-455(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Differential expression of mRNAs encoding the putative inhibin co-receptor (betaglycan) and activin type-I and type-II receptors in preovulatory and prehierarchical follicles of the laying hen ovary."
    Lovell T.M., Knight P.G., Gladwell R.T.
    J. Endocrinol. 188:241-249(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiAVR2B_CHICK
AccessioniPrimary (citable) accession number: Q90670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.