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UniProtKB/Swiss-Prot entry Q8K348


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

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Entry information
Entry name ACV1C_MOUSE
Primary accession number Q8K348
Secondary accession numbers None
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on October 25, 2005 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 56)
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
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
DOI=10.1128/MCB.24.21.9383-9389.2004; PubMed=15485907 [NCBI, ExPASy, EBI, Israel, Japan]
Joernvall H., Reissmann E., Andersson O., Mehrkash M., Ibanez C.F.;
"ALK7, a receptor for nodal, is dispensable for embryogenesis and left-right patterning in the mouse.";
Mol. Cell. Biol. 24:9383-9389(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal lung;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-363.
STRAIN=C57BL/6J;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
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
AK142396; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AL772179; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC028780; AAH28780.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Mm.123481
3D structure databases
HSSP P36897; 1IAS. [HSSP ENTRY / PDB]
SMR Q8K348; 161-489.
ModBase Q8K348.
Organism-specific databases
MGI MGI:2661081; Acvr1c.
Gene expression databases
ArrayExpress Q8K348; -.
CleanEx MM_ACVR1C; -.
GermOnline ENSMUSG00000026834; Mus musculus.
Ontologies
GO
GO:0048179; Cellular component: activin receptor complex (inferred from sequence or structural similarity from UniProtKB).
GO:0016361; Molecular function: activin receptor activity, type I (inferred from sequence or structural similarity from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030154; Biological process: cell differentiation (inferred from sequence or structural similarity from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0042981; Biological process: regulation of apoptosis (inferred from sequence or structural similarity 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).
ProtoNet Q8K348.
Genome annotation databases
Ensembl ENSMUSG00000026834; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM Q8K348; -.
HOVERGEN Q8K348; -.
Other
SOURCE Acvr1c; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoptosis; ATP-binding; 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_0000042629
TOPO_DOM   27   113  87     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). 
Sequence information
Length: 493 AA [This is the length of the unprocessed precursor] Molecular weight: 54684 Da [This is the MW of the unprocessed precursor] CRC64: A79C82C328C6647F [This is a checksum on the sequence]
        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 
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 PEMLDDTMNL SIFESFKRAD IYSVGLVYWE IARRCSVGGV VEEYQLPYYD 

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

       490 
TISQLCVKED CKA 

Q8K348 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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