AVR2B_BOVIN
ID AVR2B_BOVIN Reviewed; 512 AA.
AC Q95126;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Activin receptor type-2B;
DE EC=2.7.11.30;
DE AltName: Full=Activin receptor type IIB;
DE Short=ACTR-IIB;
DE Flags: Precursor;
GN Name=ACVR2B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpus luteum, and Pituitary;
RX PubMed=9165032; DOI=10.1210/endo.138.6.5173;
RA Ethier J.-F., Lussier J.G., Silversides D.W.;
RT "Bovine activin receptor type IIB messenger ribonucleic acid displays
RT alternative splicing involving a sequence homologous to Src-homology 3
RT domain binding sites.";
RL Endocrinology 138:2425-2434(1997).
CC -!- FUNCTION: Transmembrane serine/threonine kinase activin type-2 receptor
CC forming an activin receptor complex with activin type-1
CC serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces
CC the activin signal from the cell surface to the cytoplasm and is thus
CC regulating many physiological and pathological processes including
CC neuronal differentiation and neuronal survival, hair follicle
CC development and cycling, FSH production by the pituitary gland, wound
CC healing, extracellular matrix production, immunosuppression and
CC carcinogenesis. Activin is also thought to have a paracrine or
CC autocrine role in follicular development in the ovary. Within the
CC receptor complex, the type-2 receptors act as a primary activin
CC receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-
CC A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream
CC transducers of activin signals. Activin binds to type-2 receptor at the
CC plasma membrane and activates its serine-threonine kinase. The
CC activated receptor type-2 then phosphorylates and activates the type-1
CC receptor. Once activated, the type-1 receptor binds and phosphorylates
CC the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal
CC tail. Soon after their association with the activin receptor and
CC subsequent phosphorylation, SMAD2 and SMAD3 are released into the
CC cytoplasm where they interact with the common partner SMAD4. This SMAD
CC complex translocates into the nucleus where it mediates activin-induced
CC transcription. Inhibitory SMAD7, which is recruited to ACVR1B through
CC FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin
CC receptor complex, thereby blocking the activin signal. Activin signal
CC transduction is also antagonized by the binding to the receptor of
CC inhibin-B via the IGSF1 inhibin coreceptor (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Forms an activin receptor complex with activin type II
CC receptors such as ACVR1B. Interacts with VPS39. Interacts with DYNLT1.
CC {ECO:0000250, ECO:0000250|UniProtKB:P27040}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: Phosphorylated. Constitutive phosphorylation is in part catalyzed
CC by its own kinase activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; U57707; AAC02647.1; -; mRNA.
DR RefSeq; NP_776920.1; NM_174495.2.
DR AlphaFoldDB; Q95126; -.
DR SMR; Q95126; -.
DR STRING; 9913.ENSBTAP00000024095; -.
DR PaxDb; Q95126; -.
DR PRIDE; Q95126; -.
DR GeneID; 282131; -.
DR KEGG; bta:282131; -.
DR CTD; 93; -.
DR eggNOG; KOG3653; Eukaryota.
DR InParanoid; Q95126; -.
DR OrthoDB; 390511at2759; -.
DR BRENDA; 2.7.10.2; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0032924; P:activin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Kinase;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..512
FT /note="Activin receptor type-2B"
FT /id="PRO_0000024403"
FT TOPO_DOM 19..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 190..480
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 491..512
FT /note="Interaction with DYNLT1"
FT /evidence="ECO:0000250|UniProtKB:P27040"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 196..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..59
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 49..77
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 84..103
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 90..102
FT /evidence="ECO:0000250|UniProtKB:P38445"
FT DISULFID 104..109
FT /evidence="ECO:0000250|UniProtKB:P38445"
SQ SEQUENCE 512 AA; 57569 MW; D8E14D465B3EEF04 CRC64;
MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GERDKRLHCY
ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG
GPEVTYEPPP TAPTLLTVLA YSLLPVGGLS LIALLAFWMY RHRKPPYGHA DIHEDPGPPP
PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK
HENLLQFIAA EKRGSSLEAE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY
LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG
TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ
HPSLEELQEV VVHKKMRPAI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL
IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI
