EKS-MUM-00314

Eukaryotic Protein Kinase & Protein Phosphatase Database

Tag

Content

EKPD ID

EKS-MUM-00314

Classification

Group/Family	Score	E-Value	Start	End	Domain Length
TKL/STKR	408.4	3.9E-122	206	493	288

Status

Reviewed

Ensembl Protein

ENSMUSP00000035093

UniProt Accession

P27040; Q3KQI1;

Protein Name

Activin receptor type-2B

Protein Synonyms/Alias

Activin receptor type IIB; ACTR-IIB;

Gene Name

Acvr2b

Gene Synonyms/Alias

Acvr2b;

Ensembl Information

Ensembl Gene ID	Ensembl Protein ID	Ensembl Transcript ID
ENSMUSG00000061393	ENSMUSP00000126108	ENSMUST00000165044
ENSMUSG00000061393	ENSMUSP00000035093	ENSMUST00000035093

Organism

Mus musculus

Functional Description

Transmembrane serine/threonine kinase activin type-2receptor 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).

Protein Length

528

Protein Sequence
(FASTA)

MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY 60

ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEPG 120

GPEAPTLLTV LAYSLLPIGG LSLIVLLAFW MYRHRKPPYG HVDIHEVRQC QRWAGRRDGC 180

ADSFKPLPFQ DPGPPPPSPL VGLKPLQLLE IKARGRFGCV WKAQLMNDFV AVKIFPLQDK 240

QSWQSEREIF STPGMKHENL LQFIAAEKRG SNLEVELWLI TAFHDKGSLT DYLKGNIITW 300

NELCHVAETM SRGLSYLHED VPWCRGEGHK PSIAHRDFKS KNVLLKSDLT AVLADFGLAV 360

RFEPGKPPGD THGQVGTRRY MAPEVLEGAI NFQRDAFLRI DMYAMGLVLW ELVSRCKAAD 420

GPVDEYMLPF EEEIGQHPSL EELQEVVVHK KMRPTIKDHW LKHPGLAQLC VTIEECWDHD 480

AEARLSAGCV EERVSLIRRS VNGTTSDCLV SLVTSVTNVD LLPKESSI 528

Nucleotide Sequence
(FASTA)

ATGACGGCGC CCTGGGCGGC CCTCGCCCTT CTCTGGGGAT CGCTGTGCGC CGGTTCCGGG 60

CGAGGGGAGG CTGAGACTCG GGAGTGCATC TACTACAACG CCAACTGGGA GCTGGAGCGC 120

ACCAACCAGA GCGGCCTGGA GCGCTGCGAG GGGGAACAGG ACAAGCGGCT GCACTGCTAC 180

GCCTCGTGGC GCAACAGCTC GGGCACCATC GAGCTGGTGA AGAAGGGCTG CTGGCTAGAT 240

GACTTCAATT GCTACGACAG GCAGGAGTGT GTGGCCACCG AGGAGAACCC CCAGGTGTAC 300

TTCTGCTGCT GCGAAGGCAA CTTCTGCAAC GAGCGCTTCA CCCACTTGCC GGAGCCTGGG 360

GGCCCAGAAG CCCCCACCCT GCTCACGGTG CTGGCCTACT CGCTGCTGCC CATTGGAGGC 420

CTCTCTCTCA TCGTCCTGCT GGCCTTCTGG ATGTATCGTC ATCGGAAGCC TCCCTACGGC 480

CATGTGGACA TCCATGAGGT GAGACAGTGC CAGCGTTGGG CAGGGAGAAG GGACGGCTGT 540

GCGGACTCCT TTAAGCCCTT GCCTTTCCAG GACCCGGGGC CTCCGCCCCC ATCCCCTCTG 600

GTGGGCCTGA AGCCACTACA GCTGCTGGAG ATCAAGGCTC GGGGCCGCTT TGGCTGCGTT 660

TGGAAAGCTC AGCTCATGAA CGACTTTGTG GCTGTGAAGA TCTTCCCACT TCAGGACAAG 720

CAGTCGTGGC AGAGTGAACG GGAAATCTTC AGCACACCCG GCATGAAGCA CGAAAACTTG 780

TTGCAGTTCA TTGCTGCCGA GAAACGAGGC TCCAACCTGG AGGTGGAGCT GTGGCTCATC 840

ACAGCCTTCC ACGACAAGGG CTCCCTCACG GATTACCTCA AGGGGAACAT CATCACGTGG 900

AACGAACTGT GCCACGTGGC GGAGACGATG TCACGAGGCC TCTCATACCT GCATGAGGAT 960

GTGCCGTGGT GTCGTGGTGA GGGCCACAAG CCTTCTATTG CCCACAGGGA CTTCAAAAGC 1020

AAGAATGTAC TGCTGAAGAG CGACCTCACC GCGGTGCTGG CTGACTTCGG CCTGGCTGTT 1080

CGGTTTGAGC CAGGGAAGCC TCCTGGGGAT ACCCATGGAC AGGTTGGCAC CAGACGGTAC 1140

ATGGCCCCTG AGGTGCTGGA AGGAGCCATC AACTTCCAGA GAGACGCCTT CCTGCGTATC 1200

GACATGTACG CCATGGGCCT GGTGCTGTGG GAGCTCGTCT CTCGGTGCAA GGCTGCAGAC 1260

GGGCCTGTCG ATGAGTACAT GCTGCCCTTC GAGGAGGAGA TTGGCCAGCA CCCTTCGCTG 1320

GAGGAGCTTC AGGAGGTGGT TGTCCACAAG AAGATGAGGC CCACGATTAA GGATCACTGG 1380

CTGAAACACC CGGGCCTGGC CCAGCTCTGC GTGACCATCG AGGAGTGCTG GGACCATGAT 1440

GCAGAGGCTC GCCTTTCTGC AGGCTGTGTA GAAGAGCGGG TATCCCTGAT CAGGAGGTCG 1500

GTCAACGGCA CTACCTCGGA CTGTCTCGTC TCTCTGGTGA CCTCCGTCAC CAATGTGGAC 1560

CTGCTCCCTA AAGAGTCCAG CATCTAA 1587

Domain Profile

S: 1     lklleligkGrygeVwkaklrgeevAvKifstedeaswkrEkeiyqtvllrhenilqfia  60

         l+lle+ ++Gr+g+Vwka+l+++ vAvKif+ +d++sw++E+ei++t+ ++hen+lqfia

Q: 206   LQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIA  265

         6899********************************************************

S: 61    adkkeedsltelllvteyhekgsLsdyLkretldveellrlalslasGlahLHeeivgtk  120

         a+k+ +++++el+l+t++h+kgsL+dyLk ++++++el+++a+++++Gl++LHe++++++

Q: 266   AEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCR  325

         ************************************************************

S: 121   g.kkKpaiaHRDlkskNilvkkdltcciaDlGLalkleeekeeldlaansqvGtkRYmaP  179

         g  +Kp+iaHRD+kskN+l+k+dlt+++aD+GLa+++e  k   d  ++ qvGt+RYmaP

Q: 326   GeGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGD--THGQVGTRRYMAP  383

         *99***************************************888..79***********

S: 180   EvleealnlkdfeafkraDvYslgLvlWEvasRceevdeeveeyklpfeevvgsdPslee  239

         Evle+a+n+++ +af r+D+Y++gLvlWE++sRc+++d+ v+ey+lpfee++g++Pslee

Q: 384   EVLEGAINFQR-DAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEE  442

         **********9.9***********************************************

S: 240   mkevvvekklrPkipeawkkkealkelsklleecWdadpeaRltalrvkkr  290

         ++evvv+kk+rP+i+++w k++ l++l+ ++eecWd+d+eaRl+a +v++r

Q: 443   LQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEER  493

         ************************************************998

Domain Sequence
(FASTA)

LQLLEIKARG RFGCVWKAQL MNDFVAVKIF PLQDKQSWQS EREIFSTPGM KHENLLQFIA 60

AEKRGSNLEV ELWLITAFHD KGSLTDYLKG NIITWNELCH VAETMSRGLS YLHEDVPWCR 120

GEGHKPSIAH RDFKSKNVLL KSDLTAVLAD FGLAVRFEPG KPPGDTHGQV GTRRYMAPEV 180

LEGAINFQRD AFLRIDMYAM GLVLWELVSR CKAADGPVDE YMLPFEEEIG QHPSLEELQE 240

VVVHKKMRPT IKDHWLKHPG LAQLCVTIEE CWDHDAEARL SAGCVEER 288

Keyword

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.

Sequence Source

Ensembl

Orthology

Ortholog group

Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Danio rerio"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Microcebus murinus"; ?>Monodelphis domestica"; ?>Mustela putorius furo"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tupaia belangeri"; ?>Tursiops truncatus"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>

Gene Ontology

GO:0009986	; C:cell surface
GO:0005737	; C:cytoplasm
GO:0016021	; C:integral to membrane
GO:0005886	; C:plasma membrane
GO:0048185	; F:activin binding
GO:0017002	; F:activin-activated receptor activity
GO:0005524	; F:ATP binding
GO:0019838	; F:growth factor binding
GO:0046872	; F:metal ion binding
GO:0004674	; F:protein serine/threonine kinase activity
GO:0004712	; F:protein serine/threonine/tyrosine kinase activity
GO:0004702	; F:receptor signaling protein serine/threonine kinase activity
GO:0005024	; F:transforming growth factor beta-activated receptor activity
GO:0032147	; P:activation of protein kinase activity
GO:0009952	; P:anterior/posterior pattern specification
GO:0060840	; P:artery development
GO:0001974	; P:blood vessel remodeling
GO:0030509	; P:BMP signaling pathway
GO:0007368	; P:determination of left/right symmetry
GO:0048617	; P:embryonic foregut morphogenesis
GO:0001702	; P:gastrulation with mouth forming second
GO:0007507	; P:heart development
GO:0030073	; P:insulin secretion
GO:0001822	; P:kidney development
GO:0030324	; P:lung development
GO:0001946	; P:lymphangiogenesis
GO:0060836	; P:lymphatic endothelial cell differentiation
GO:0007498	; P:mesoderm development
GO:0042475	; P:odontogenesis of dentin-containing tooth
GO:0035265	; P:organ growth
GO:0060021	; P:palate development
GO:0031016	; P:pancreas development
GO:0032927	; P:positive regulation of activin receptor signaling pathway
GO:0030501	; P:positive regulation of bone mineralization
GO:0045669	; P:positive regulation of osteoblast differentiation
GO:0009791	; P:post-embryonic development
GO:0009966	; P:regulation of signal transduction
GO:0009749	; P:response to glucose stimulus
GO:0061298	; P:retina vasculature development in camera-type eye
GO:0023014	; P:signal transduction by phosphorylation
GO:0048705	; P:skeletal system morphogenesis
GO:0060841	; P:venous blood vessel development

KEGG

mmu:11481

;

InterPros

IPR000333	; Activin_II/TGFBeta-II_recpt.
IPR015768	; Activin_II_recpt.
IPR000472	; Activin_rcpt.
IPR011009	; Kinase-like_dom.
IPR000719	; Prot_kinase_cat_dom.
IPR008271	; Ser/Thr_kinase_AS.

Pfam

PF01064	; Activin_recp; 1.
PF00069	; Pkinase; 1.

SMARTs

Prosites

PS00107	; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011	; PROTEIN_KINASE_DOM; 1.
PS00108	; PROTEIN_KINASE_ST; 1.

Prints

PR00653

; ACTIVIN2R.

Created Date

20-Feb-2013