ID   ACV1C_MOUSE             Reviewed;         493 AA.
AC   Q8K348;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Activin receptor type-1C;
DE            EC=2.7.11.30;
DE   AltName: Full=ACTR-IC;
DE   AltName: Full=Activin receptor-like kinase 7;
DE            Short=ALK-7;
DE   Flags: Precursor;
GN   Name=Acvr1c; Synonyms=Alk7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
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
RT   left-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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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;
RG   The mouse genome sequencing consortium;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-363.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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
RT   project: 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
CC       type II and 2 type I transmembrane serine/threonine kinases. Type
CC       II receptors phosphorylate and activate type I receptors which
CC       autophosphorylate, then bind and activate SMAD transcriptional
CC       regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B
CC       and NODAL. Plays a role in cell differentiation, growth arrest and
CC       apoptosis.
CC   -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC       protein] phosphate.
CC   -!- COFACTOR: Magnesium or manganese.
CC   -!- SUBUNIT: Binds the type 2 receptor protein ACVR2A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in interdigital regions in
CC       developing limb buds.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC   -!- SIMILARITY: Contains 1 GS domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AL772179; Type=Frameshift; Positions=236;
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DR   EMBL; AK142396; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL772179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC028780; AAH28780.1; -; mRNA.
DR   IPI; IPI00720121; -.
DR   UniGene; Mm.77751; -.
DR   HSSP; P36897; 1IAS.
DR   SMR; Q8K348; 161-489.
DR   PhosphoSite; Q8K348; -.
DR   Ensembl; ENSMUSG00000026834; Mus musculus.
DR   MGI; MGI:2661081; Acvr1c.
DR   HOGENOM; Q8K348; -.
DR   HOVERGEN; Q8K348; -.
DR   BRENDA; 2.7.11.30; 244.
DR   ArrayExpress; Q8K348; -.
DR   Bgee; Q8K348; -.
DR   CleanEx; MM_ACVR1C; -.
DR   GermOnline; ENSMUSG00000026834; Mus musculus.
DR   GO; GO:0048179; C:activin receptor complex; ISS:UniProtKB.
DR   GO; GO:0016361; F:activin receptor activity, type I; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR   GO; GO:0019915; P:lipid storage; IMP:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   GO; GO:0042981; P:regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR   GO; GO:0009749; P:response to glucose stimulus; IMP:MGI.
DR   GO; GO:0032868; P:response to insulin stimulus; IMP:MGI.
DR   InterPro; IPR000472; Activin_rcpt.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR003605; TGF_beta_rcpt_GS.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00467; GS; 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;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    493       Activin receptor type-1C.
FT                                /FTId=PRO_0000042629.
FT   TOPO_DOM     27    113       Extracellular (Potential).
FT   TRANSMEM    114    134       Potential.
FT   TOPO_DOM    135    493       Cytoplasmic (Potential).
FT   DOMAIN      165    194       GS.
FT   DOMAIN      195    485       Protein kinase.
FT   NP_BIND     201    209       ATP (By similarity).
FT   ACT_SITE    323    323       Proton acceptor (By similarity).
FT   BINDING     222    222       ATP (By similarity).
SQ   SEQUENCE   493 AA;  54684 MW;  A79C82C328C6647F CRC64;
     MTPARGSALS LALLLVALAA DLAAGLKCVC LLCDSSNFTC QTEGACWASV MLTNGKEQVI
     KSCVSLPELN AQVFCHSSNN VTKTECCFTD FCNNITLHLP TASPNAPRLG PTELTVVITV
     PVCLLSIAAM LTIWACQDRQ CTYRKTKRHN VEEALAEYSL VNAGKTLKDL IYDATASGSG
     SGPPLLVQRT 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
//