ID ACV1C_MOUSE Reviewed; 493 AA.
AC Q8K348; A2AJR4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Activin receptor type-1C;
DE EC=2.7.11.30;
DE AltName: Full=Activin receptor type IC;
DE Short=ACTR-IC;
DE AltName: Full=Activin receptor-like kinase 7;
DE Short=ALK-7;
DE Flags: Precursor;
GN Name=Acvr1c {ECO:0000312|EMBL:AAH28780.1};
GN Synonyms=Alk7 {ECO:0000250|UniProtKB:Q04771};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15485907; DOI=10.1128/mcb.24.21.9383-9389.2004;
RA Joernvall H., Reissmann E., Andersson O., Mehrkash M., Ibanez C.F.;
RT "ALK7, a receptor for nodal, is dispensable for embryogenesis and left-
RT right patterning in the mouse.";
RL Mol. Cell. Biol. 24:9383-9389(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH28780.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-363.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH28780.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH28780.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Serine/threonine protein kinase which forms a receptor
CC complex on ligand binding. The receptor complex consisting of 2 type II
CC and 2 type I transmembrane serine/threonine kinases. Type II receptors
CC phosphorylate and activate type I receptors which autophosphorylate,
CC then bind and activate SMAD transcriptional regulators, SMAD2 and
CC SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in
CC cell differentiation, growth arrest and apoptosis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC -!- SUBUNIT: Binds the type 2 receptor protein ACVR2A. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in interdigital regions in developing
CC limb buds. {ECO:0000269|PubMed:15485907}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK142396; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK142396; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL772179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL26940.1; -; Genomic_DNA.
DR EMBL; BC028780; AAH28780.1; -; mRNA.
DR CCDS; CCDS50586.1; -.
DR RefSeq; NP_001104500.1; NM_001111030.1.
DR AlphaFoldDB; Q8K348; -.
DR SMR; Q8K348; -.
DR BioGRID; 234631; 1.
DR IntAct; Q8K348; 1.
DR MINT; Q8K348; -.
DR STRING; 10090.ENSMUSP00000028178; -.
DR iPTMnet; Q8K348; -.
DR PhosphoSitePlus; Q8K348; -.
DR jPOST; Q8K348; -.
DR MaxQB; Q8K348; -.
DR PaxDb; 10090-ENSMUSP00000028178; -.
DR ProteomicsDB; 281932; -.
DR Antibodypedia; 2075; 477 antibodies from 35 providers.
DR DNASU; 269275; -.
DR Ensembl; ENSMUST00000028178.14; ENSMUSP00000028178.8; ENSMUSG00000026834.14.
DR GeneID; 269275; -.
DR KEGG; mmu:269275; -.
DR UCSC; uc008jsp.2; mouse.
DR AGR; MGI:2661081; -.
DR CTD; 130399; -.
DR MGI; MGI:2661081; Acvr1c.
DR VEuPathDB; HostDB:ENSMUSG00000026834; -.
DR eggNOG; KOG2052; Eukaryota.
DR GeneTree; ENSGT00940000158842; -.
DR InParanoid; Q8K348; -.
DR OMA; DVMNTNI; -.
DR OrthoDB; 3900892at2759; -.
DR PhylomeDB; Q8K348; -.
DR TreeFam; TF314724; -.
DR Reactome; R-MMU-1502540; Signaling by Activin.
DR BioGRID-ORCS; 269275; 2 hits in 79 CRISPR screens.
DR PRO; PR:Q8K348; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K348; Protein.
DR Bgee; ENSMUSG00000026834; Expressed in brown adipose tissue and 116 other cell types or tissues.
DR ExpressionAtlas; Q8K348; baseline and differential.
DR Genevisible; Q8K348; MM.
DR GO; GO:0048179; C:activin receptor complex; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; ISO:MGI.
DR GO; GO:0017002; F:activin receptor activity; ISO:MGI.
DR GO; GO:0016361; F:activin receptor activity, type I; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0070700; F:BMP receptor binding; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; ISS:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038100; F:nodal binding; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISO:MGI.
DR GO; GO:0030262; P:apoptotic nuclear changes; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0019915; P:lipid storage; IMP:MGI.
DR GO; GO:1901383; P:negative regulation of chorionic trophoblast cell proliferation; ISO:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
DR GO; GO:1901164; P:negative regulation of trophoblast cell migration; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0038092; P:nodal signaling pathway; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR GO; GO:0009749; P:response to glucose; IMP:MGI.
DR GO; GO:0032868; P:response to insulin; IMP:MGI.
DR GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; ISO:MGI.
DR GO; GO:0001834; P:trophectodermal cell proliferation; ISO:MGI.
DR CDD; cd14143; STKc_TGFbR1_ACVR1b_ACVR1c; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR003605; GS_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255:SF58; ACTIVIN RECEPTOR TYPE-1C; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 1.
DR PROSITE; PS51256; GS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; ATP-binding; Kinase; Magnesium; Manganese; Membrane;
KW Metal-binding; Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..493
FT /note="Activin receptor type-1C"
FT /id="PRO_0000042629"
FT TOPO_DOM 27..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 165..194
FT /note="GS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT DOMAIN 195..485
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q04771,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 201..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q04771,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q04771,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ 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
//
