|AVR2B_HUMAN » Activin receptor type-2B » Activin receptor type IIB;ACTR-IIB;|
|Hydrophobic Thickness||36.0 ± 1.2 Å|
|Tilt Angle||9 ± 4°|
|Links||UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB|
|TM Segments||136-160 (133-164)|
Developmental Biology (Reactome)
Signal Transduction (Reactome)
TGF-beta signaling pathway (KEGG)
|PDB||2qlu (190-487), 2h62 (D=19-116), 4fao (E/F...=19-134)|
ACVR1, Complex: ACVR1:AVR2B
|UniProt annotation for AVR2B_HUMAN » Activin receptor type-2B|
|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. CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor- protein] phosphate. SUBUNIT: Forms an activin receptor complex with activin type II receptors such as ACVR1B. Interacts with VPS39. DISEASE: Heterotaxy, visceral, 4, autosomal (HTX4) OMIM: A form of visceral heterotaxy, a complex disorder due to disruption of the normal left-right asymmetry of the thoracoabdominal organs. Visceral heterotaxy or situs ambiguus results in randomization of the placement of visceral organs, including the heart, lungs, liver, spleen, and stomach. The organs are oriented randomly with respect to the left-right axis and with respect to one another. It can been associated with variety of congenital defects including cardiac malformations. HTX4 clinical features include dextrocardia, right aortic arch and a right-sided spleen, anomalies of the inferior and the superior vena cava, atrial ventricular canal defect with dextro-transposed great arteries, pulmonary stenosis, polysplenia and midline liver. mutations affecting the gene represented in this entry.|
|UniProt features for AVR2B_HUMAN » Activin receptor type-2B|
SIGNAL 1 18 Potential. |
CHAIN 19 512 Activin receptor type-2B.
DOMAIN 190 480 Protein kinase.
ACT_SITE 321 321 Proton acceptor (By similarity).
DISULFID 29 59
DISULFID 49 77
DISULFID 84 103
DISULFID 90 102
DISULFID 104 109
|Amino Acid Sequence for AVR2B_HUMAN » Activin receptor type-2B|
|MTAPWVALAL LWGSLCAGSG 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 EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ HPSLEELQEV VVHKKMRPTI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI|