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P38445

- AVR2B_RAT

UniProt

P38445 - AVR2B_RAT

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Protein

Activin receptor type-2B

Gene

Acvr2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei217 – 2171ATPPROSITE-ProRule annotation
Active sitei322 – 3221Proton acceptorPROSITE-ProRule annotation

Regions

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

GO - Molecular functioni

  1. activin binding Source: RGD
  2. ATP binding Source: UniProtKB-KW
  3. inhibin binding Source: RGD
  4. metal ion binding Source: UniProtKB-KW
  5. protein serine/threonine/tyrosine kinase activity Source: Ensembl
  6. receptor signaling protein serine/threonine kinase activity Source: InterPro
  7. transforming growth factor beta-activated receptor activity Source: InterPro
  8. transmembrane receptor protein serine/threonine kinase activity Source: RGD

GO - Biological processi

  1. activation of protein kinase activity Source: Ensembl
  2. anterior/posterior pattern specification Source: Ensembl
  3. artery development Source: Ensembl
  4. blood vessel remodeling Source: Ensembl
  5. BMP signaling pathway Source: Ensembl
  6. determination of left/right symmetry Source: Ensembl
  7. embryonic foregut morphogenesis Source: Ensembl
  8. gastrulation with mouth forming second Source: Ensembl
  9. heart development Source: Ensembl
  10. insulin secretion Source: Ensembl
  11. kidney development Source: Ensembl
  12. lung development Source: Ensembl
  13. lymphangiogenesis Source: Ensembl
  14. lymphatic endothelial cell differentiation Source: Ensembl
  15. mesoderm development Source: Ensembl
  16. odontogenesis of dentin-containing tooth Source: Ensembl
  17. organ growth Source: Ensembl
  18. palate development Source: Ensembl
  19. pancreas development Source: Ensembl
  20. positive regulation of activin receptor signaling pathway Source: Ensembl
  21. positive regulation of bone mineralization Source: Ensembl
  22. positive regulation of osteoblast differentiation Source: Ensembl
  23. post-embryonic development Source: Ensembl
  24. protein phosphorylation Source: RGD
  25. response to glucose Source: Ensembl
  26. retina vasculature development in camera-type eye Source: Ensembl
  27. sexual reproduction Source: RGD
  28. skeletal system morphogenesis Source: Ensembl
  29. venous blood vessel development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_194628. Signaling by Activin.
REACT_194664. Signaling by NODAL.
REACT_199248. Regulation of signaling by NODAL.
REACT_234964. Signaling by BMP.

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
ProteomesiUP000002494: Chromosome 8

Organism-specific databases

RGDi2028. Acvr2b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 137119ExtracellularSequence AnalysisAdd
BLAST
Transmembranei138 – 15821HelicalSequence AnalysisAdd
BLAST
Topological domaini159 – 513355CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
  4. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 513495Activin receptor type-2BPRO_0000024406Add
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

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.

Expressioni

Gene expression databases

GenevestigatoriP38445.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000049841.

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 336Combined sources
Turni34 – 407Combined sources
Beta strandi43 – 486Combined sources
Beta strandi57 – 659Combined sources
Beta strandi70 – 7910Combined sources
Helixi82 – 843Combined sources
Beta strandi89 – 924Combined sources
Beta strandi98 – 1047Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1154Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NYSX-ray3.05A/C19-119[»]
1NYUX-ray3.10A/C19-119[»]
ProteinModelPortaliP38445.
SMRiP38445. Positions 26-120, 190-485.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38445.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini190 – 481292Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000231495.
HOVERGENiHBG054502.
InParanoidiP38445.
KOiK13596.
OrthoDBiEOG7JHM5B.

Family and domain databases

InterProiIPR000472. Activin_rcpt.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641R → P in AAA40772. (PubMed:1312838)Curated
Sequence conflicti64 – 641R → P(PubMed:7916681)Curated
Sequence conflicti255 – 2551Missing(PubMed:7916681)Curated
Sequence conflicti255 – 2551Missing in AAH97358. (PubMed:15489334)Curated
Sequence conflicti488 – 4881S → G in AAA40772. (PubMed:1312838)Curated
Sequence conflicti488 – 4881S → G(PubMed:7916681)Curated
Sequence conflicti501 – 5011V → S in AAA40772. (PubMed:1312838)Curated
Sequence conflicti501 – 5011V → S(PubMed:7916681)Curated

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

EnsembliENSRNOT00000019777; ENSRNOP00000019777; ENSRNOG00000014477.
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 .
PIRi B49193.
JQ1484.
RefSeqi NP_113742.1. NM_031554.1.
UniGenei Rn.24240.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P38445.
SMRi P38445. Positions 26-120, 190-485.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000049841.

Proteomic databases

PaxDbi P38445.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000019777 ; ENSRNOP00000019777 ; ENSRNOG00000014477 .
GeneIDi 25366.
KEGGi rno:25366.
UCSCi RGD:2028. rat.

Organism-specific databases

CTDi 93.
RGDi 2028. Acvr2b.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118876.
HOGENOMi HOG000231495.
HOVERGENi HBG054502.
InParanoidi P38445.
KOi K13596.
OrthoDBi EOG7JHM5B.

Enzyme and pathway databases

Reactomei REACT_194628. Signaling by Activin.
REACT_194664. Signaling by NODAL.
REACT_199248. Regulation of signaling by NODAL.
REACT_234964. Signaling by BMP.

Miscellaneous databases

EvolutionaryTracei P38445.
NextBioi 606365.
PROi P38445.

Gene expression databases

Genevestigatori P38445.

Family and domain databases

InterProi IPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
[Graphical view ]
PANTHERi PTHR23255. PTHR23255. 1 hit.
Pfami PF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR00653. ACTIVIN2R.
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

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 26, 2014
This is version 133 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

External Data

Dasty 3