EKS-RAN-00291

Eukaryotic Protein Kinase & Protein Phosphatase Database

Tag

Content

EKPD ID

EKS-RAN-00291

Classification

Group/Family	Score	E-Value	Start	End	Domain Length
TKL/STKR	455.7	7.7E-137	207	494	288

Status

Reviewed

Ensembl Protein

ENSRNOP00000009345

UniProt Accession

P80202;

Protein Name

Activin receptor type-1B

Protein Synonyms/Alias

Activin receptor type IB; ACTR-IB; Activin receptor-like kinase 4; ALK-4; Serine/threonine-protein kinase receptor R2; SKR2;

Gene Name

Acvr1b

Gene Synonyms/Alias

Acvr1b; Acvrlk4, Alk4;

Ensembl Information

Ensembl Gene ID	Ensembl Protein ID	Ensembl Transcript ID
ENSRNOG00000006934	ENSRNOP00000009345	ENSRNOT00000009345

Organism

Rattus norvegicus

Functional Description

Transmembrane serine/threonine kinase activin type-1receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a 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, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas 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 such as ACVR1B. 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. ACVR1B also phosphorylates TDP2 (By similarity).

Protein Length

505

Protein Sequence
(FASTA)

MAESAGASSF FPLVVLLLAG SGGSGPRGIQ ALLCACTSCL QTNYTCETDG ACMVSIFNLD 60

GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYIDF CNKIDLRVPS GHLKEPEHPS 120

MWGPVELVGI IAGPVFLLFL IIIIVFLVIN YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ 180

DLVYDLSTSG SGSGLPLFVQ RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE 240

ERSWFREAEI YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT 300

IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA IADLGLAVRH 360

DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC ADIYALGLVY WEIARRCNSG 420

GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNVPNWW QSYEALRVMG KMMRECWYAN 480

GAARLTALRI KKTLSQLSVQ EDVKI 505

Nucleotide Sequence
(FASTA)

ATGGCGGAGT CGGCCGGAGC CTCCTCCTTC TTCCCCCTTG TTGTCCTCCT GCTCGCCGGC 60

AGTGGCGGGT CCGGGCCCCG GGGGATCCAG GCTCTGCTGT GTGCATGCAC CAGCTGCCTA 120

CAGACCAACT ACACCTGCGA AACAGATGGG GCCTGCATGG TCTCCATCTT TAACCTGGAT 180

GGCATGGAGC ACCACGTACG CACCTGCATC CCCAAGGTGG AGCTTGTGCC TGCTGGGAAG 240

CCCTTCTACT GCCTGAGTTC AGAGGACCTG CGCAACACGC ACTGCTGCTA TATTGACTTC 300

TGCAACAAGA TTGACCTGAG GGTGCCCAGT GGACACCTCA AGGAGCCTGA GCACCCCTCC 360

ATGTGGGGCC CTGTGGAGCT GGTCGGCATC ATTGCCGGTC CTGTCTTCCT CCTCTTCCTC 420

ATCATCATCA TCGTCTTCCT GGTCATCAAC TATCATCAGC GTGTCTACCA CAACCGCCAA 480

AGACTGGACA TGGAGGACCC CTCATGTGAG ATGTGTCTCT CCAAAGACAA GACGCTCCAG 540

GATCTCGTCT ACGATCTCTC CACTTCAGGA TCGGGCTCAG GGTTACCCCT TTTTGTCCAG 600

CGCACAGTGG CCCGAACCAT TGTTTTACAA GAGATTATCG GCAAGGGCCG GTTTGGGGAA 660

GTATGGCGTG GCCGCTGGAG GGGTGGTGAT GTGGCTGTGA AAATCTTCTC TTCCCGTGAA 720

GAGCGGTCGT GGTTCCGGGA GGCAGAGATC TACCAGACTG TCATGCTGCG CCATGAAAAC 780

ATCCTTGGGT TTATTGCTGC TGACAATAAA GACAATGGCA CCTGGACCCA GCTGTGGCTT 840

GTCTCTGACT ATCACGAGCA CGGCTCACTG TTCGATTATC TGAACCGCTA CACAGTGACC 900

ATTGAGGGGA TGATTAAACT GGCCCTGTCT GCAGCCAGTG GTTTGGCACA CCTGCATATG 960

GAGATTGTGG GCACTCAGGG GAAGCCTGGA ATTGCTCATC GAGACTTGAA GTCAAAGAAC 1020

ATTCTGGTGA AGAAGAATGG CATGTGTGCC ATTGCAGACC TGGGCCTAGC TGTCCGTCAC 1080

GATGCTGTCA CTGACACCAT AGACATTGCT CCAAATCAGA GGGTGGGAAC CAAACGATAC 1140

ATGGCTCCTG AAGTACTTGA CGAGACCATC AACATGAAGC ACTTTGACTC CTTCAAGTGT 1200

GCCGATATCT ACGCCCTCGG GCTTGTCTAT TGGGAGATTG CTCGGAGGTG CAATTCTGGA 1260

GGAGTCCATG AAGAGTATCA ACTGCCATAT TATGATTTAG TGCCCTCTGA CCCTTCCATT 1320

GAGGAAATGC GAAAGGTCGT CTGTGACCAG AAGCTACGGC CCAATGTCCC CAACTGGTGG 1380

CAGAGTTATG AGGCCTTGCG AGTGATGGGG AAGATGATGC GGGAGTGCTG GTACGCCAAT 1440

GGTGCTGCCC GCCTGACAGC GCTGCGCATC AAGAAGACTT TGTCCCAGCT AAGCGTGCAG 1500

GAAGACGTGA AGATTTAA 1518

Domain Profile

S: 1     lklleligkGrygeVwkaklrgeevAvKifstedeaswkrEkeiyqtvllrhenilqfia  60

         + l+e+igkGr+geVw++++rg +vAvKifs+++e+sw+rE+eiyqtv+lrhenil+fia

Q: 207   IVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIA  266

         5789********************************************************

S: 61    adkkeedsltelllvteyhekgsLsdyLkretldveellrlalslasGlahLHeeivgtk  120

         ad+k+++++t+l+lv++yhe+gsL+dyL+r+t+++e +++lals+asGlahLH+eivgt+

Q: 267   ADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQ  326

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

S: 121   gkkKpaiaHRDlkskNilvkkdltcciaDlGLalkleeekeeldlaansqvGtkRYmaPE  180

         g  Kp iaHRDlkskNilvkk+++c+iaDlGLa+++++ ++++d+a n++vGtkRYmaPE

Q: 327   G--KPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPE  384

         *..*********************************************************

S: 181   vleealnlkdfeafkraDvYslgLvlWEvasRceevdeeveeyklpfeevvgsdPsleem  240

         vl+e++n+k+f++fk+aD+Y+lgLv+WE+a+Rc++ ++++eey+lp+++ v+sdPs+eem

Q: 385   VLDETINMKHFDSFKCADIYALGLVYWEIARRCNS-GGVHEEYQLPYYDLVPSDPSIEEM  443

         ***********************************.************************

S: 241   kevvvekklrPkipeawkkkealkelsklleecWdadpeaRltalrvkkrl  291

         ++vv+++klrP++p+ w++ eal+++ k+++ecW+a+++aRltalr+kk+l

Q: 444   RKVVCDQKLRPNVPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTL  494

         *************************************************97

Domain Sequence
(FASTA)

IVLQEIIGKG RFGEVWRGRW RGGDVAVKIF SSREERSWFR EAEIYQTVML RHENILGFIA 60

ADNKDNGTWT QLWLVSDYHE HGSLFDYLNR YTVTIEGMIK LALSAASGLA HLHMEIVGTQ 120

GKPGIAHRDL KSKNILVKKN GMCAIADLGL AVRHDAVTDT IDIAPNQRVG TKRYMAPEVL 180

DETINMKHFD SFKCADIYAL GLVYWEIARR CNSGGVHEEY QLPYYDLVPS DPSIEEMRKV 240

VCDQKLRPNV PNWWQSYEAL RVMGKMMREC WYANGAARLT ALRIKKTL 288

Keyword

ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane; Transmembrane helix; Ubl conjugation.

Sequence Source

Ensembl

Orthology

Ortholog group

Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Danio rerio"; ?>Equus caballus"; ?>Felis catus"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Microcebus murinus"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>

Gene Ontology

GO:0009986	; C:cell surface
GO:0005887	; C:integral to plasma membrane
GO:0016361	; F:activin receptor activity, type I
GO:0005524	; F:ATP binding
GO:0046872	; F:metal ion binding
GO:0004702	; F:receptor signaling protein serine/threonine kinase activity
GO:0046332	; F:SMAD binding
GO:0005024	; F:transforming growth factor beta-activated receptor activity
GO:0007417	; P:central nervous system development
GO:0046545	; P:development of primary female sexual characteristics
GO:0000082	; P:G1/S transition of mitotic cell cycle
GO:0001942	; P:hair follicle development
GO:0001701	; P:in utero embryonic development
GO:0006917	; P:induction of apoptosis
GO:0030308	; P:negative regulation of cell growth
GO:0038092	; P:nodal signaling pathway
GO:0018107	; P:peptidyl-threonine phosphorylation
GO:0032927	; P:positive regulation of activin receptor signaling pathway
GO:0045648	; P:positive regulation of erythrocyte differentiation
GO:0010862	; P:positive regulation of pathway-restricted SMAD protein phosphorylation
GO:0045944	; P:positive regulation of transcription from RNA polymerase II promoter
GO:0046777	; P:protein autophosphorylation

KEGG

rno:29381

;

InterPros

IPR000472	; Activin_rcpt.
IPR011009	; Kinase-like_dom.
IPR000719	; Prot_kinase_cat_dom.
IPR017441	; Protein_kinase_ATP_BS.
IPR008271	; Ser/Thr_kinase_AS.
IPR003605	; TGF_beta_rcpt_GS.

Pfam

PF01064	; Activin_recp; 1.
PF00069	; Pkinase; 1.
PF08515	; TGF_beta_GS; 1.

SMARTs

SM00467

; GS; 1.

Prosites

PS51256	; GS; 1.
PS00107	; PROTEIN_KINASE_ATP; 1.
PS50011	; PROTEIN_KINASE_DOM; 1.
PS00108	; PROTEIN_KINASE_ST; 1.

Prints

Created Date

20-Feb-2013