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Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB)

 AVR2B_MOUSE             Reviewed;         536 AA.
P27040; Q3KQI1;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
25-OCT-2017, entry version 172.
RecName: Full=Activin receptor type-2B;
EC=2.7.11.30;
AltName: Full=Activin receptor type IIB;
Short=ACTR-IIB;
Flags: Precursor;
Name=Acvr2b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ACTR-IIB1; ACTR-IIB2; ACTR-IIB3
AND ACTR-IIB4).
STRAIN=BALB/cJ;
PubMed=1310075; DOI=10.1016/0092-8674(92)90209-U;
Attisano L., Wrana J.L., Cheifetz S., Massague J.;
"Novel activin receptors: distinct genes and alternative mRNA splicing
generate a repertoire of serine/threonine kinase receptors.";
Cell 68:97-108(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ACTR-IIB2).
TISSUE=Jaw;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INTERACTION WITH DYNLT.
PubMed=27502274; DOI=10.1074/jbc.M116.736884;
Merino-Gracia J., Zamora-Carreras H., Bruix M., Rodriguez-Crespo I.;
"Molecular basis for the protein recognition specificity of the dynein
light chain DYNLT1/Tctex1: characterization of the interaction with
activin receptor IIB.";
J. Biol. Chem. 291:20962-20975(2016).
-!- 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Forms an activin receptor complex with activin type II
receptors such as ACVR1B. Interacts with VPS39. Interacts with
DYNLT1. {ECO:0000250, ECO:0000269|PubMed:27502274}.
-!- INTERACTION:
P36896:ACVR1B (xeno); NbExp=4; IntAct=EBI-8571194, EBI-1384128;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=ActR-IIB1 and ActR-IIB2 have similar but higher
affinities for activin A than ActR-II, ActR-IIB3 and ActR-IIB4.;
Name=ActR-IIB1;
IsoId=P27040-1; Sequence=Displayed;
Name=ActR-IIB2;
IsoId=P27040-2; Sequence=VSP_004952;
Name=ActR-IIB3;
IsoId=P27040-3; Sequence=VSP_004951;
Name=ActR-IIB4;
IsoId=P27040-4; Sequence=VSP_004951, VSP_004952;
-!- PTM: Phosphorylated. Constitutive phosphorylation is in part
catalyzed by its own kinase activity (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M84120; AAA37172.1; -; mRNA.
EMBL; BC106189; AAI06190.1; -; mRNA.
CCDS; CCDS23615.1; -. [P27040-1]
PIR; A40829; A40829.
PIR; B40829; B40829.
PIR; C40829; C40829.
PIR; D40829; D40829.
RefSeq; NP_001300686.1; NM_001313757.1. [P27040-2]
RefSeq; NP_031423.1; NM_007397.3. [P27040-1]
RefSeq; XP_006511989.1; XM_006511926.3. [P27040-4]
UniGene; Mm.390239; -.
UniGene; Mm.8940; -.
PDB; 1S4Y; X-ray; 2.30 A; A/C=23-120.
PDB; 2H64; X-ray; 1.92 A; C=19-117.
PDBsum; 1S4Y; -.
PDBsum; 2H64; -.
ProteinModelPortal; P27040; -.
SMR; P27040; -.
BioGrid; 197956; 1.
DIP; DIP-5799N; -.
IntAct; P27040; 5.
MINT; MINT-2842249; -.
STRING; 10090.ENSMUSP00000126108; -.
PhosphoSitePlus; P27040; -.
MaxQB; P27040; -.
PaxDb; P27040; -.
PRIDE; P27040; -.
Ensembl; ENSMUST00000035093; ENSMUSP00000035093; ENSMUSG00000061393. [P27040-3]
Ensembl; ENSMUST00000165044; ENSMUSP00000126108; ENSMUSG00000061393. [P27040-1]
Ensembl; ENSMUST00000215746; ENSMUSP00000150566; ENSMUSG00000061393. [P27040-2]
GeneID; 11481; -.
KEGG; mmu:11481; -.
UCSC; uc009sax.1; mouse. [P27040-1]
UCSC; uc009say.1; mouse. [P27040-2]
CTD; 93; -.
MGI; MGI:87912; Acvr2b.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000231495; -.
HOVERGEN; HBG054502; -.
InParanoid; P27040; -.
KO; K13596; -.
OMA; PAIKDHW; -.
OrthoDB; EOG091G03YO; -.
PhylomeDB; P27040; -.
TreeFam; TF352876; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-1181150; Signaling by NODAL.
Reactome; R-MMU-1502540; Signaling by Activin.
Reactome; R-MMU-201451; Signaling by BMP.
EvolutionaryTrace; P27040; -.
PRO; PR:P27040; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000061393; -.
CleanEx; MM_ACVR2B; -.
Genevisible; P27040; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0048185; F:activin binding; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IMP:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:MGI.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:InterPro.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
GO; GO:0032147; P:activation of protein kinase activity; IDA:MGI.
GO; GO:0032924; P:activin receptor signaling pathway; ISO:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0060840; P:artery development; IMP:BHF-UCL.
GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
GO; GO:0001702; P:gastrulation with mouth forming second; IGI:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0030073; P:insulin secretion; IGI:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0030324; P:lung development; IGI:MGI.
GO; GO:0001946; P:lymphangiogenesis; IMP:BHF-UCL.
GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:BHF-UCL.
GO; GO:0007498; P:mesoderm development; IGI:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0035265; P:organ growth; IGI:MGI.
GO; GO:0060021; P:palate development; IMP:MGI.
GO; GO:0031016; P:pancreas development; IGI:MGI.
GO; GO:0007389; P:pattern specification process; IGI:MGI.
GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; ISO:MGI.
GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0009966; P:regulation of signal transduction; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0009749; P:response to glucose; IGI:MGI.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:BHF-UCL.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0001501; P:skeletal system development; IMP:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0060841; P:venous blood vessel development; IMP:BHF-UCL.
InterPro; IPR000472; Activin_recp.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR00653; ACTIVIN2R.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Kinase; Magnesium;
Manganese; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 536 Activin receptor type-2B.
/FTId=PRO_0000024405.
TOPO_DOM 19 137 Extracellular. {ECO:0000255}.
TRANSMEM 138 158 Helical. {ECO:0000255}.
TOPO_DOM 159 536 Cytoplasmic. {ECO:0000255}.
DOMAIN 214 504 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 220 228 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 515 536 Interaction with DYNLT1.
{ECO:0000269|PubMed:27502274}.
ACT_SITE 345 345 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 241 241 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 29 59 {ECO:0000250|UniProtKB:P38445}.
DISULFID 49 77 {ECO:0000250|UniProtKB:P38445}.
DISULFID 84 103 {ECO:0000250|UniProtKB:P38445}.
DISULFID 90 102 {ECO:0000250|UniProtKB:P38445}.
DISULFID 104 109 {ECO:0000250|UniProtKB:P38445}.
VAR_SEQ 124 131 Missing (in isoform ActR-IIB3 and isoform
ActR-IIB4). {ECO:0000303|PubMed:1310075}.
/FTId=VSP_004951.
VAR_SEQ 175 198 Missing (in isoform ActR-IIB2 and isoform
ActR-IIB4). {ECO:0000303|PubMed:1310075,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_004952.
STRAND 28 33 {ECO:0000244|PDB:2H64}.
TURN 34 40 {ECO:0000244|PDB:2H64}.
STRAND 43 48 {ECO:0000244|PDB:2H64}.
STRAND 57 66 {ECO:0000244|PDB:2H64}.
STRAND 69 79 {ECO:0000244|PDB:2H64}.
HELIX 82 84 {ECO:0000244|PDB:2H64}.
STRAND 88 92 {ECO:0000244|PDB:2H64}.
STRAND 93 96 {ECO:0000244|PDB:1S4Y}.
STRAND 98 106 {ECO:0000244|PDB:2H64}.
TURN 107 110 {ECO:0000244|PDB:2H64}.
STRAND 111 115 {ECO:0000244|PDB:2H64}.
SEQUENCE 536 AA; 60542 MW; BF1C8CAC974BF5E2 CRC64;
MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY
ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEPG
GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEVRQCQR
WAGRRDGCAD SFKPLPFQDP GPPPPSPLVG LKPLQLLEIK ARGRFGCVWK AQLMNDFVAV
KIFPLQDKQS WQSEREIFST PGMKHENLLQ FIAAEKRGSN LEVELWLITA FHDKGSLTDY
LKGNIITWNE LCHVAETMSR GLSYLHEDVP WCRGEGHKPS IAHRDFKSKN VLLKSDLTAV
LADFGLAVRF EPGKPPGDTH GQVGTRRYMA PEVLEGAINF QRDAFLRIDM YAMGLVLWEL
VSRCKAADGP VDEYMLPFEE EIGQHPSLEE LQEVVVHKKM RPTIKDHWLK HPGLAQLCVT
IEECWDHDAE ARLSAGCVEE RVSLIRRSVN GTTSDCLVSL VTSVTNVDLL PKESSI


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