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Q8K348 (ACV1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activin receptor type-1C

EC=2.7.11.30
Alternative name(s):
Activin receptor type IC
Short name=ACTR-IC
Activin receptor-like kinase 7
Short name=ALK-7
Gene names
Name:Acvr1c
Synonyms:Alk7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (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 structure

Binds the type 2 receptor protein ACVR2A By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

Expressed in interdigital regions in developing limb buds. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 GS domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence AK142396 differs from that shown. Reason: Frameshift at position 236.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic nuclear changes

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

lipid storage

Inferred from mutant phenotype PubMed 18480258. Source: MGI

negative regulation of chorionic trophoblast cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 18480258. Source: MGI

negative regulation of trophoblast cell migration

Inferred from electronic annotation. Source: Ensembl

nodal signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

response to dietary excess

Inferred from mutant phenotype PubMed 18480259. Source: MGI

response to glucose

Inferred from mutant phenotype PubMed 18480258. Source: MGI

response to insulin

Inferred from mutant phenotype PubMed 18480259. Source: MGI

   Cellular_componentactivin receptor complex

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

activin receptor activity, type I

Inferred from sequence or structural similarity. Source: UniProtKB

growth factor binding

Inferred from sequence or structural similarity. Source: UniProt

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta-activated receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 493468Activin receptor type-1C
PRO_0000042629

Regions

Topological domain27 – 11387Extracellular Potential
Transmembrane114 – 13421Helical; Potential
Topological domain135 – 493359Cytoplasmic Potential
Domain165 – 19430GS
Domain195 – 485291Protein kinase
Nucleotide binding201 – 2099ATP By similarity UniProtKB Q04771

Sites

Active site3231Proton acceptor By similarity UniProtKB Q04771
Binding site2221ATP By similarity UniProtKB Q04771

Sequences

Sequence LengthMass (Da)Tools
Q8K348 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: CB9BE5E368CA2D2F

FASTA49354,700
        10         20         30         40         50         60 
MTPARGSALS LALLLVALAA DLAAGLKCVC LLCDSSNFTC QTEGACWASV MLTNGKEQVI 

        70         80         90        100        110        120 
KSCVSLPELN AQVFCHSSNN VTKTECCFTD FCNNITLHLP TASPNAPRLG PTELTVVITV 

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

       190        200        210        220        230        240 
SGLPLLVQRT 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 PEMLDDTMNL SIFESFKRAD IYSVGLVYWE IARRCSVGGV VEEYQLPYYD 

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

       490 
TISQLCVKED CKA 

« Hide

References

« Hide 'large scale' references
[1]"ALK7, a receptor for nodal, is dispensable for embryogenesis and left-right patterning in the mouse."
Joernvall H., Reissmann E., Andersson O., Mehrkash M., Ibanez C.F.
Mol. Cell. Biol. 24:9383-9389(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal lung.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-363.
Strain: C57BL/6J.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK142396 mRNA. No translation available.
AL772179 Genomic DNA. Translation: CAM13260.1.
CH466519 Genomic DNA. Translation: EDL26940.1.
BC028780 mRNA. Translation: AAH28780.1.
RefSeqNP_001104500.1. NM_001111030.1.
UniGeneMm.77751.

3D structure databases

ProteinModelPortalQ8K348.
SMRQ8K348. Positions 25-97, 145-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid234631. 1 interaction.
IntActQ8K348. 1 interaction.
MINTMINT-2842395.
STRING10090.ENSMUSP00000028178.

PTM databases

PhosphoSiteQ8K348.

Proteomic databases

PRIDEQ8K348.

Protocols and materials databases

DNASU269275.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028178; ENSMUSP00000028178; ENSMUSG00000026834.
GeneID269275.
KEGGmmu:269275.
UCSCuc008jsp.2. mouse.

Organism-specific databases

CTD130399.
MGIMGI:2661081. Acvr1c.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110337.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidA2AJR4.
KOK13568.
OMAWACQGRQ.
OrthoDBEOG7Q8CN3.
TreeFamTF314724.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_188576. Developmental Biology.

Gene expression databases

BgeeQ8K348.
CleanExMM_ACVR1C.
GenevestigatorQ8K348.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
[Graphical view]
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTSM00467. GS. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio392768.
PROQ8K348.
SOURCESearch...

Entry information

Entry nameACV1C_MOUSE
AccessionPrimary (citable) accession number: Q8K348
Secondary accession number(s): A2AJR4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot