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UniProtKB/Swiss-Prot entry P70539


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACV1C_RAT
Primary accession number P70539
Secondary accession number P70603
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 62)
Name and origin of the protein
Protein name Activin receptor type-1C [Precursor]
Synonyms EC 2.7.11.30
ACTR-IC
Activin receptor-like kinase 7
ALK-7
Gene name
Name: Acvr1c
Synonyms: Alk7
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-194 AND LYS-222.
STRAIN=Sprague-Dawley;
TISSUE=Brain;
DOI=10.1006/mcne.1996.0034; PubMed=8875430 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuchida K., Sawchenko P.E., Nishikawa S., Vale W.W.;
"Molecular cloning of a novel type I receptor serine/threonine kinase for the TGF beta superfamily from rat brain.";
Mol. Cell. Neurosci. 7:467-478(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
DOI=10.1074/jbc.271.48.30603; PubMed=8940033 [NCBI, ExPASy, EBI, Israel, Japan]
Ryden M., Imamura T., Joernvall H., Belluardo N., Neveu I., Trupp M., Okadome T., ten Dijke P., Ibanez C.F.;
"A novel type I receptor serine-threonine kinase predominantly expressed in the adult central nervous system.";
J. Biol. Chem. 271:30603-30609(1996).
[3]
PROTEIN SEQUENCE OF 139-159, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH ACVR2A; ACTIVIN AB AND B.
DOI=10.1016/j.mce.2004.03.009; PubMed=15196700 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuchida K., Nakatani M., Yamakawa N., Hashimoto O., Hasegawa Y., Sugino H.;
"Activin isoforms signal through type I receptor serine/threonine kinase ALK7.";
Mol. Cell. Endocrinol. 220:59-65(2004).
[4]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-194.
DOI=10.1006/bbrc.1998.0118; PubMed=9920806 [NCBI, ExPASy, EBI, Israel, Japan]
Watanabe R., Yamada Y., Ihara Y., Someya Y., Kubota A., Kagimoto S., Kuroe A., Iwakura T., Shen Z.-P., Inada A., Adachi T., Ban N., Miyawaki K., Sunaga Y., Tsuda K., Seino Y.;
"The MH1 domains of smad2 and smad3 are involved in the regulation of the ALK7 signals.";
Biochem. Biophys. Res. Commun. 254:707-712(1999).
[5]
FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M005200200; PubMed=11084022 [NCBI, ExPASy, EBI, Israel, Japan]
Joernvall H., Blokzijl A., ten Dijke P., Ibanez C.F.;
"The orphan receptor serine/threonine kinase ALK7 signals arrest of proliferation and morphological differentiation in a neuronal cell line.";
J. Biol. Chem. 276:5140-5146(2001).
Comments
  • FUNCTION: Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis.
  • CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
  • COFACTOR: Magnesium or manganese.
  • SUBUNIT: Binds the type 2 receptor protein ACVR2A.
  • SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
  • TISSUE SPECIFICITY: Expressed in brain, kidney, lung, liver, testis, ovary, adrenal gland, heart, prostate, gastrointestinal tract, and spleen. Distributed throughout both adult and embryonic central nervous system and pancreatic islet cells.
  • SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
  • SIMILARITY: Contains 1 GS domain.
  • SIMILARITY: Contains 1 protein kinase domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U35025; AAC52803.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U69702; AAC52919.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_620790.1; -.
UniGene Rn.10580
3D structure databases
HSSP P36897; 1IAS. [HSSP ENTRY / PDB]
SMR P70539; 161-489.
ModBase P70539.
Organism-specific databases
RGD 621789; Acvr1c.
Gene expression databases
ArrayExpress P70539; -.
GermOnline ENSRNOG00000004828; Rattus norvegicus.
Ontologies
GO
GO:0048179; Cellular component: activin receptor complex (inferred from direct assay from UniProtKB).
GO:0016361; Molecular function: activin receptor activity, type I (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred by curator from UniProtKB).
GO:0046872; Molecular function: metal ion binding (inferred by curator from UniProtKB).
GO:0046332; Molecular function: SMAD binding (inferred from direct assay from HGNC).
GO:0030154; Biological process: cell differentiation (inferred from direct assay from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred by curator from UniProtKB).
GO:0042981; Biological process: regulation of apoptosis (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR003605; TGF_beta_rcpt_GS.
Graphical view of domain structure.
Pfam PF01064; Activin_recp; 1.
PF00069; Pkinase; 1.
PF08515; TGF_beta_GS; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00467; GS; 1.
SMART graphical view of domain structure.
PROSITE PS51256; GS; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P70539.
Genome annotation databases
Ensembl ENSRNOG00000004828; Rattus norvegicus. [Contig view]
GeneID 245921; -.
KEGG rno:245921; -.
Phylogenomic databases
HOVERGEN P70539; -.
Other
ProtoNet P70539.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoptosis; ATP-binding; Direct protein sequencing; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    25  25     Potential. 
CHAIN   26   493  468     Activin receptor type-1C. PRO_0000042630
TOPO_DOM   26   113  88     Extracellular (Potential). 
TRANSMEM   114   134  21     Potential. 
TOPO_DOM   135   493  359     Cytoplasmic (Potential). 
DOMAIN   165   194  30     GS. 
DOMAIN   195   485  291     Protein kinase. 
NP_BIND   201   209  9     ATP (By similarity). 
ACT_SITE   323   323        Proton acceptor (By similarity). 
BINDING   222   222        ATP (By similarity). 
MUTAGEN   194   194        T->D: Constitutively activates downstream transcription factor function. 
MUTAGEN   222   222        K->R: Fails to activate downstream transcription factor function. 
CONFLICT   5     5        R -> S (in Ref. 2; AAC52919). 
CONFLICT   60    60        S -> I (in Ref. 2; AAC52919). 
CONFLICT   97    97        Q -> L (in Ref. 2; AAC52919). 
CONFLICT   183   183        P -> L (in Ref. 2; AAC52919). 
Sequence information
Length: 493 AA [This is the length of the unprocessed precursor] Molecular weight: 54842 Da [This is the MW of the unprocessed precursor] CRC64: FB2BB3C2A026BCC3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTPARRSALS LALLLVALAS DLAAGLKCVC LLCDSSNFTC QTEGACWASV MLTNGKEQVS 

        70         80         90        100        110        120 
KSCVSLPELN AQVFCHSSNN VTKTECCFTD FCNNITQHLP TASPDAPRLG PTELTVVITV 

       130        140        150        160        170        180 
PVCLLSIAAM LTIWACQDRQ CTYRKTKRHN VEEPLAEYSL VNAGKTLKDL IYDATASGSG 

       190        200        210        220        230        240 
SGPPLLVQRT IARTIVLQEI VGKGRFGEVW HGRWCGEDVA VKIFSSRDER SWFREAEIYQ 

       250        260        270        280        290        300 
TVMLRHENIL GFIAADNKDN GTWTQLWLVS EYHEQGSLYD YLNRNIVTVA GMVKLALSIA 

       310        320        330        340        350        360 
SGLAHLHMEI VGTQGKPAIA HRDIKSKNIL VKKCDTCAIA DLGLAVKHDS IMNTIDIPQN 

       370        380        390        400        410        420 
PKVGTKRYMA PEMLDDTMNV NIFESFKRAD IYSVGLVYWE IARRCSVGGL VEEYQLPYYD 

       430        440        450        460        470        480 
MVPSDPSIEE MRKVVCDQKL RPNLPNQWQS CEALRVMGRI MRECWYANGA ARLTALRVKK 

       490 
TISQLCVKED CKA 

P70539 in FASTA format

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