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Activin receptor type-1B (EC 2.7.11.30) (Activin receptor type IB) (ACTR-IB) (Activin receptor-like kinase 4) (ALK-4) (Serine/threonine-protein kinase receptor R2) (SKR2)

 ACV1B_RAT               Reviewed;         505 AA.
P80202;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
07-JUN-2017, entry version 159.
RecName: Full=Activin receptor type-1B;
EC=2.7.11.30;
AltName: Full=Activin receptor type IB;
Short=ACTR-IB;
AltName: Full=Activin receptor-like kinase 4;
Short=ALK-4;
AltName: Full=Serine/threonine-protein kinase receptor R2;
Short=SKR2;
Flags: Precursor;
Name=Acvr1b; Synonyms=Acvrlk4, Alk4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Urogenital ridge;
PubMed=8395914; DOI=10.1002/aja.1001960207;
He W.-W., Gustafson M.L., Hirobe S., Donahoe P.K.;
"Developmental expression of four novel serine/threonine kinase
receptors homologous to the activin/transforming growth factor-beta
type II receptor family.";
Dev. Dyn. 196:133-142(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pituitary;
PubMed=7813622; DOI=10.1006/excr.1995.1026;
Takumi T., Moustakas A., Lin H.Y., Lodish H.F.;
"Molecular characterization of a type I serine-threonine kinase
receptor for TGF-beta and activin in the rat pituitary tumor cell line
GH3.";
Exp. Cell Res. 216:208-214(1995).
-!- FUNCTION: Transmembrane serine/threonine kinase activin type-1
receptor forming an activin receptor complex with activin receptor
type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the
cell surface to the cytoplasm and is thus regulating a 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, type-2 receptors (ACVR2A and/or ACVR2B) act as a
primary activin receptors whereas 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 such as ACVR1B.
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. ACVR1B also phosphorylates TDP2
(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};
-!- ENZYME REGULATION: Activin receptor type-2 (ACVR2A or ACVR2B)
activates the type-1 receptor through phosphorylation of its
regulatory GS domain. {ECO:0000250}.
-!- SUBUNIT: Forms an activin receptor complex with activin receptor
type-2 (ACVR2A or ACVR2B). Interacts with TDP2 (By similarity).
Interacts with AIP1, FKBP1A, IGSF1, TDGF1, SMAD2, SMAD3 and SMAD7
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Urogenital ridge, testis, ovary, brain and
lungs.
-!- DOMAIN: The GS domain is a 30-amino-acid sequence adjacent to the
N-terminal boundary of the kinase domain and highly conserved in
all other known type-1 receptors but not in type-2 receptors. The
GS domain is the site of activation through phosphorylation by the
II receptors (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated. Phosphorylated by activin receptor type-2
(ACVR2A or ACVR2B) in response to activin-binding at serine and
threonine residues in the GS domain. Phosphorylation of ACVR1B by
activin receptor type-2 regulates association with SMAD7 (By
similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Level of ubiquitination is regulated by the
SMAD7-SMURF1 complex (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. {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; S76466; AAB33045.1; -; mRNA.
RefSeq; NP_954700.1; NM_199230.1.
UniGene; Rn.214018; -.
ProteinModelPortal; P80202; -.
BioGrid; 248033; 1.
STRING; 10116.ENSRNOP00000009345; -.
iPTMnet; P80202; -.
PhosphoSitePlus; P80202; -.
PaxDb; P80202; -.
Ensembl; ENSRNOT00000009345; ENSRNOP00000009345; ENSRNOG00000006934.
GeneID; 29381; -.
KEGG; rno:29381; -.
UCSC; RGD:735207; rat.
CTD; 91; -.
RGD; 735207; Acvr1b.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000230587; -.
HOVERGEN; HBG054502; -.
InParanoid; P80202; -.
KO; K13567; -.
OMA; GPVFLLC; -.
OrthoDB; EOG091G0BIU; -.
PhylomeDB; P80202; -.
BRENDA; 2.7.10.2; 5301.
Reactome; R-RNO-1502540; Signaling by Activin.
PRO; PR:P80202; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000006934; -.
GO; GO:0048179; C:activin receptor complex; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0048185; F:activin binding; IEA:Ensembl.
GO; GO:0016361; F:activin receptor activity, type I; IMP:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
GO; GO:0034711; F:inhibin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IMP:RGD.
GO; GO:0046332; F:SMAD binding; IMP:RGD.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; TAS:RGD.
GO; GO:0007417; P:central nervous system development; IEP:RGD.
GO; GO:0046545; P:development of primary female sexual characteristics; IEP:RGD.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0038092; P:nodal signaling pathway; IEA:Ensembl.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:1901165; P:positive regulation of trophoblast cell migration; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IMP:RGD.
InterPro; IPR000472; Activin_recp.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08515; TGF_beta_GS; 1.
SMART; SM00467; GS; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51256; GS; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Kinase;
Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 505 Activin receptor type-1B.
/FTId=PRO_0000024419.
TOPO_DOM 24 126 Extracellular. {ECO:0000255}.
TRANSMEM 127 149 Helical. {ECO:0000255}.
TOPO_DOM 150 505 Cytoplasmic. {ECO:0000255}.
DOMAIN 177 206 GS. {ECO:0000255|PROSITE-
ProRule:PRU00585}.
DOMAIN 207 497 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 213 221 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 335 335 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 234 234 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 380 380 Phosphotyrosine.
{ECO:0000250|UniProtKB:P36896}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 505 AA; 56805 MW; 377F4A5C867B3860 CRC64;
MAESAGASSF FPLVVLLLAG SGGSGPRGIQ ALLCACTSCL QTNYTCETDG ACMVSIFNLD
GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYIDF CNKIDLRVPS GHLKEPEHPS
MWGPVELVGI IAGPVFLLFL IIIIVFLVIN YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ
DLVYDLSTSG SGSGLPLFVQ RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE
ERSWFREAEI YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT
IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA IADLGLAVRH
DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC ADIYALGLVY WEIARRCNSG
GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNVPNWW QSYEALRVMG KMMRECWYAN
GAARLTALRI KKTLSQLSVQ EDVKI


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