ID   AVR2B_PIG               Reviewed;         512 AA.
AC   Q66T47;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 114.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Song J.H., Wise T.H., Ford J.J.;
RT   "Complete sequence of activin receptor IIB cDNA in boars.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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; AY705387; AAU07920.1; -; mRNA.
DR   RefSeq; NP_001005350.1; NM_001005350.2.
DR   AlphaFoldDB; Q66T47; -.
DR   SMR; Q66T47; -.
DR   STRING; 9823.ENSSSCP00000067564; -.
DR   GlyCosmos; Q66T47; 2 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000028777; -.
DR   GeneID; 448845; -.
DR   KEGG; ssc:448845; -.
DR   CTD; 93; -.
DR   eggNOG; KOG3653; Eukaryota.
DR   InParanoid; Q66T47; -.
DR   OrthoDB; 3900892at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; 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: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: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:1901389; P:negative regulation of transforming growth factor beta activation; IMP:AgBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14140; STKc_ACVR2b; 1.
DR   Gene3D; 2.10.60.10; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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:SF70; ACTIVIN RECEPTOR TYPE-2B; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 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_0000234419"
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;  57693 MW;  59A5A00239A92EAC CRC64;
     MTAPWAALAL LWGSLCVGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY
     ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG
     GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP
     PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK
     HENLLQFIAA EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY
     LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG
     TRRYMAPEVL EGAINFQRNA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ
     HPSLEELQEV VVHKKMRPAI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL
     IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI
//