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Activin receptor type-1C (EC 2.7.11.30) (Activin receptor type IC) (ACTR-IC) (Activin receptor-like kinase 7) (ALK-7)

 ACV1C_MOUSE             Reviewed;         493 AA.
Q8K348; A2AJR4;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
10-MAY-2017, entry version 135.
RecName: Full=Activin receptor type-1C;
EC=2.7.11.30;
AltName: Full=Activin receptor type IC;
Short=ACTR-IC;
AltName: Full=Activin receptor-like kinase 7;
Short=ALK-7;
Flags: Precursor;
Name=Acvr1c {ECO:0000312|EMBL:AAH28780.1};
Synonyms=Alk7 {ECO:0000250|UniProtKB:Q04771};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=15485907; DOI=10.1128/MCB.24.21.9383-9389.2004;
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;
PubMed=16141072; DOI=10.1126/science.1112014;
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;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:AAH28780.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-363.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH28780.1};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAH28780.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
-!- 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:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
-!- SUBUNIT: Binds the type 2 receptor protein ACVR2A. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in interdigital regions in
developing limb buds. {ECO:0000269|PubMed:15485907}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AK142396; Type=Frameshift; Positions=236; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK142396; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL772179; CAM13260.1; -; Genomic_DNA.
EMBL; CH466519; EDL26940.1; -; Genomic_DNA.
EMBL; BC028780; AAH28780.1; -; mRNA.
CCDS; CCDS50586.1; -.
RefSeq; NP_001104500.1; NM_001111030.1.
UniGene; Mm.77751; -.
ProteinModelPortal; Q8K348; -.
SMR; Q8K348; -.
BioGrid; 234631; 1.
IntAct; Q8K348; 1.
MINT; MINT-2842395; -.
STRING; 10090.ENSMUSP00000028178; -.
PhosphoSitePlus; Q8K348; -.
MaxQB; Q8K348; -.
PaxDb; Q8K348; -.
PRIDE; Q8K348; -.
DNASU; 269275; -.
Ensembl; ENSMUST00000028178; ENSMUSP00000028178; ENSMUSG00000026834.
GeneID; 269275; -.
KEGG; mmu:269275; -.
UCSC; uc008jsp.2; mouse.
CTD; 130399; -.
MGI; MGI:2661081; Acvr1c.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000230587; -.
HOVERGEN; HBG054502; -.
InParanoid; Q8K348; -.
KO; K13568; -.
OMA; APKLGPM; -.
OrthoDB; EOG091G0BIU; -.
TreeFam; TF314724; -.
Reactome; R-MMU-1181150; Signaling by NODAL.
Reactome; R-MMU-1502540; Signaling by Activin.
PRO; PR:Q8K348; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026834; -.
CleanEx; MM_ACVR1C; -.
ExpressionAtlas; Q8K348; baseline and differential.
Genevisible; Q8K348; MM.
GO; GO:0048179; C:activin receptor complex; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0048185; F:activin binding; ISO:MGI.
GO; GO:0016361; F:activin receptor activity, type I; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0038100; F:nodal binding; ISO:MGI.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:InterPro.
GO; GO:0030262; P:apoptotic nuclear changes; ISO:MGI.
GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
GO; GO:0019915; P:lipid storage; IMP:MGI.
GO; GO:1901383; P:negative regulation of chorionic trophoblast cell proliferation; ISO:MGI.
GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
GO; GO:1901164; P:negative regulation of trophoblast cell migration; ISO:MGI.
GO; GO:0038092; P:nodal signaling pathway; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0002021; P:response to dietary excess; IMP:MGI.
GO; GO:0009749; P:response to glucose; IMP:MGI.
GO; GO:0032868; P:response to insulin; IMP:MGI.
GO; GO:0001834; P:trophectodermal cell proliferation; ISO:MGI.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF08515; TGF_beta_GS; 1.
SMART; SM00467; GS; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51256; GS; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
Apoptosis; ATP-binding; Complete proteome; Kinase; Magnesium;
Manganese; Membrane; Metal-binding; Nucleotide-binding; Receptor;
Reference proteome; Serine/threonine-protein kinase; Signal;
Transferase; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 493 Activin receptor type-1C.
/FTId=PRO_0000042629.
TOPO_DOM 27 113 Extracellular. {ECO:0000255}.
TRANSMEM 114 134 Helical. {ECO:0000255}.
TOPO_DOM 135 493 Cytoplasmic. {ECO:0000255}.
DOMAIN 165 194 GS. {ECO:0000255|PROSITE-
ProRule:PRU00585}.
DOMAIN 195 485 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 201 209 ATP. {ECO:0000250|UniProtKB:Q04771,
ECO:0000255|PROSITE-ProRule:PRU00159}.
ACT_SITE 323 323 Proton acceptor.
{ECO:0000250|UniProtKB:Q04771,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 222 222 ATP. {ECO:0000250|UniProtKB:Q04771,
ECO:0000255|PROSITE-ProRule:PRU00159}.
SEQUENCE 493 AA; 54700 MW; CB9BE5E368CA2D2F CRC64;
MTPARGSALS LALLLVALAA DLAAGLKCVC LLCDSSNFTC QTEGACWASV MLTNGKEQVI
KSCVSLPELN AQVFCHSSNN VTKTECCFTD FCNNITLHLP TASPNAPRLG PTELTVVITV
PVCLLSIAAM LTIWACQDRQ CTYRKTKRHN VEEALAEYSL VNAGKTLKDL IYDATASGSG
SGLPLLVQRT IARTIVLQEI VGKGRFGEVW HGRWCGEDVA VKIFSSRDER SWFREAEIYQ
TVMLRHENIL GFIAADNKDN GTWTQLWLVS EYHEQGSLYD YLNRNIVTVA GMVKLALSIA
SGLAHLHMEI VGTQGKPAIA HRDIKSKNIL VKKCDTCAIA DLGLAVKHDS IMNTIDIPQN
PKVGTKRYMA PEMLDDTMNL SIFESFKRAD IYSVGLVYWE IARRCSVGGV VEEYQLPYYD
MVPSDPSIEE MRKVVCDQKL RPNLPNQWQS CEALRVMGRI MRECWYANGA ARLTALRVKK
TISQLCVKED CKA


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