EKS-RAN-00299

Eukaryotic Protein Kinase & Protein Phosphatase Database

Tag

Content

EKPD ID

EKS-RAN-00299

Classification

Group/Family	Score	E-Value	Start	End	Domain Length
TKL/STKR	408.5	1.8E-122	190	477	288

Status

Reviewed

Ensembl Protein

ENSRNOP00000019777

UniProt Accession

P38445; Q4V8J8;

Protein Name

Activin receptor type-2B

Protein Synonyms/Alias

Activin receptor type IIB; ACTR-IIB;

Gene Name

Acvr2b

Gene Synonyms/Alias

Acvr2b; Actriib;

Ensembl Information

Ensembl Gene ID	Ensembl Protein ID	Ensembl Transcript ID
ENSRNOG00000014477	ENSRNOP00000019777	ENSRNOT00000019777

Organism

Rattus norvegicus

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

512

Protein Sequence
(FASTA)

MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY 60

ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEPG 120

GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP 180

PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK 240

HENLLQFIAA EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY 300

LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG 360

TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ 420

HPSLEELQEV VVHKKMRPTI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL 480

IRRSVNSSTS DCLVSLVTSV TNVDLLPKES SI 512

Nucleotide Sequence
(FASTA)

ATGACGGCGC CCTGGGCGGC CCTCGCCCTT CTCTGGGGAT CGCTGTGCGC CGGTTCCGGG 60

CGAGGGGAAG CTGAGACTCG GGAGTGCATC TACTACAACG CCAACTGGGA GCTGGAGCGC 120

ACCAACCAGA GCGGCCTGGA GCGCTGCGAG GGGGAACAGG ACAAGCGGCT GCACTGCTAT 180

GCCTCGTGGC GCAACAGCTC GGGCACCATC GAGCTGGTGA AGAAGGGCTG CTGGCTAGAT 240

GACTTCAATT GCTACGACAG GCAGGAGTGT GTGGCCACTG AGGAGAACCC CCAGGTGTAT 300

TTCTGCTGCT GTGAAGGCAA TTTCTGCAAC GAGCGCTTCA CCCATTTGCC GGAGCCTGGG 360

GGCCCAGAAG TCACGTACGA GCCACCCCCG ACAGCCCCCA CCCTGCTCAC GGTGCTGGCC 420

TATTCGCTGC TGCCCATTGG AGGCCTCTCT CTCATCGTCC TGCTGGCCTT CTGGATGTAC 480

CGACATCGAA AGCCTCCCTA CGGCCACGTG GACATCCATG AGGACCCTGG GCCTCCTCCC 540

CCATCGCCTC TGGTGGGCCT GAAGCCGCTA CAGTTGCTGG AGATCAAGGC TCGAGGTCGC 600

TTTGGCTGCG TCTGGAAGGC TCAGCTCATG AACGACTTTG TGGCTGTGAA GATCTTCCCA 660

CTTCAGGACA AGCAGTCGTG GCAGAGTGAG CGGGAGATCT TCAGCACACC GGGCATGAAG 720

CACGAAAACC TCCTGCAGTT CATTGCTGCA GAGAAACGAG GCTCCAACCT GGAGGTGGAG 780

CTGTGGCTCA TCACAGCCTT CCACGACAAG GGCTCCCTCA CGGATTACCT CAAGGGGAAC 840

ATCATCACGT GGAACGAGCT GTGTCATGTG GCAGAGACGA TGTCACGAGG CCTCTCGTAC 900

CTGCATGAGG ATGTGCCGTG GTGTCGTGGC GAGGGCCACA AGCCTTCTAT TGCCCACAGG 960

GACTTCAAAA GCAAGAATGT TCTGCTGAAG AGCGACCTCA CCGCGGTGCT GGCTGACTTT 1020

GGCCTGGCTG TTCGGTTTGA GCCGGGGAAG CCTCCAGGGG ATACCCATGG GCAGGTTGGC 1080

ACCAGACGGT ACATGGCCCC CGAGGTGCTG GAGGGGGCCA TCAACTTCCA GAGAGACGCC 1140

TTCCTGCGTA TCGACATGTA CGCCATGGGC CTGGTGCTGT GGGAGCTCGT TTCTCGTTGC 1200

AAGGCCGCAG ATGGGCCTGT CGATGAGTAC ATGCTGCCTT TCGAGGAAGA GATTGGCCAA 1260

CACCCTTCAC TGGAGGAGCT TCAGGAGGTG GTTGTCCACA AGAAGATGAG GCCCACCATT 1320

AAGGATCACT GGCTGAAACA TCCGGGCCTG GCCCAGCTCT GCGTGACCAT CGAGGAGTGC 1380

TGGGACCATG ATGCAGAGGC TCGTCTGTCT GCAGGCTGTG TGGAAGAGCG GGTATCCCTG 1440

ATCAGGAGGT CGGTCAACAG CTCTACCTCG GACTGTCTCG TCTCTCTGGT GACCTCCGTC 1500

ACCAATGTGG ACCTGCTCCC TAAAGAGTCC AGCATCTAA 1539

Domain Profile

S: 1     lklleligkGrygeVwkaklrgeevAvKifstedeaswkrEkeiyqtvllrhenilqfia  60

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

Q: 190   LQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIA  249

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

S: 61    adkkeedsltelllvteyhekgsLsdyLkretldveellrlalslasGlahLHeeivgtk  120

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

Q: 250   AEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCR  309

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

S: 121   g.kkKpaiaHRDlkskNilvkkdltcciaDlGLalkleeekeeldlaansqvGtkRYmaP  179

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

Q: 310   GeGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGD--THGQVGTRRYMAP  367

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

S: 180   EvleealnlkdfeafkraDvYslgLvlWEvasRceevdeeveeyklpfeevvgsdPslee  239

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

Q: 368   EVLEGAINFQR-DAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEE  426

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

S: 240   mkevvvekklrPkipeawkkkealkelsklleecWdadpeaRltalrvkkr  290

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

Q: 427   LQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEER  477

         ************************************************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; 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"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Pteropus vampyrus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tupaia belangeri"; ?>Tursiops truncatus"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>

Gene Ontology

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:0034711	; F:inhibin binding
GO:0046872	; F:metal ion binding
GO:0004702	; F:receptor signaling protein serine/threonine kinase activity
GO:0005024	; F:transforming growth factor beta-activated receptor activity
GO:0004675	; F:transmembrane receptor protein serine/threonine kinase activity
GO:0019953	; P:sexual reproduction
GO:0023014	; P:signal transduction by phosphorylation

KEGG

rno:25366

;

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