ACV1C_RAT
ID ACV1C_RAT Reviewed; 493 AA.
AC P70539; P70603;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
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:AAC52803.1}; Synonyms=Alk7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC52803.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF THR-194 AND LYS-222.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAC52803.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAC52803.1};
RX PubMed=8875430; DOI=10.1006/mcne.1996.0034;
RA Tsuchida K., Sawchenko P.E., Nishikawa S., Vale W.W.;
RT "Molecular cloning of a novel type I receptor serine/threonine kinase for
RT the TGF beta superfamily from rat brain.";
RL Mol. Cell. Neurosci. 7:467-478(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC52919.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:8940033};
RX PubMed=8940033; DOI=10.1074/jbc.271.48.30603;
RA Ryden M., Imamura T., Joernvall H., Belluardo N., Neveu I., Trupp M.,
RA Okadome T., ten Dijke P., Ibanez C.F.;
RT "A novel type I receptor serine-threonine kinase predominantly expressed in
RT the adult central nervous system.";
RL J. Biol. Chem. 271:30603-30609(1996).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 139-159, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH ACVR2A; ACTIVIN AB AND B.
RX PubMed=15196700; DOI=10.1016/j.mce.2004.03.009;
RA Tsuchida K., Nakatani M., Yamakawa N., Hashimoto O., Hasegawa Y.,
RA Sugino H.;
RT "Activin isoforms signal through type I receptor serine/threonine kinase
RT ALK7.";
RL Mol. Cell. Endocrinol. 220:59-65(2004).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-194.
RX PubMed=9920806; DOI=10.1006/bbrc.1998.0118;
RA Watanabe R., Yamada Y., Ihara Y., Someya Y., Kubota A., Kagimoto S.,
RA Kuroe A., Iwakura T., Shen Z.-P., Inada A., Adachi T., Ban N., Miyawaki K.,
RA Sunaga Y., Tsuda K., Seino Y.;
RT "The MH1 domains of smad2 and smad3 are involved in the regulation of the
RT ALK7 signals.";
RL Biochem. Biophys. Res. Commun. 254:707-712(1999).
RN [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11084022; DOI=10.1074/jbc.m005200200;
RA Joernvall H., Blokzijl A., ten Dijke P., Ibanez C.F.;
RT "The orphan receptor serine/threonine kinase ALK7 signals arrest of
RT proliferation and morphological differentiation in a neuronal cell line.";
RL J. Biol. Chem. 276:5140-5146(2001).
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 {ECO:0000269|PubMed:11084022, ECO:0000269|PubMed:15196700,
CC ECO:0000269|PubMed:8875430, ECO:0000269|PubMed:9920806}.
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.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15196700}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:15196700}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, lung, liver, testis,
CC ovary, adrenal gland, heart, prostate, gastrointestinal tract, and
CC spleen. Distributed throughout both adult and embryonic central nervous
CC system and pancreatic islet cells. {ECO:0000269|PubMed:11084022,
CC ECO:0000269|PubMed:15196700, ECO:0000269|PubMed:8875430,
CC ECO:0000269|PubMed:8940033, ECO:0000269|PubMed:9920806}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; U35025; AAC52803.1; -; mRNA.
DR EMBL; U69702; AAC52919.1; -; mRNA.
DR RefSeq; NP_620790.1; NM_139090.1.
DR AlphaFoldDB; P70539; -.
DR SMR; P70539; -.
DR STRING; 10116.ENSRNOP00000056047; -.
DR PhosphoSitePlus; P70539; -.
DR PaxDb; P70539; -.
DR GeneID; 245921; -.
DR KEGG; rno:245921; -.
DR UCSC; RGD:621789; rat.
DR CTD; 130399; -.
DR RGD; 621789; Acvr1c.
DR eggNOG; KOG2052; Eukaryota.
DR InParanoid; P70539; -.
DR OrthoDB; 776697at2759; -.
DR PhylomeDB; P70539; -.
DR Reactome; R-RNO-1502540; Signaling by Activin.
DR PRO; PR:P70539; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0048179; C:activin receptor complex; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; IDA:MGI.
DR GO; GO:0016361; F:activin receptor activity, type I; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:HGNC-UCL.
DR GO; GO:0070700; F:BMP receptor binding; IDA:RGD.
DR GO; GO:0019838; F:growth factor binding; ISS:CAFA.
DR GO; GO:0046872; F:metal ion binding; IC:UniProtKB.
DR GO; GO:0038100; F:nodal binding; ISO:RGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC-UCL.
DR GO; GO:0046332; F:SMAD binding; IDA:HGNC-UCL.
DR GO; GO:0032924; P:activin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030262; P:apoptotic nuclear changes; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0019915; P:lipid storage; ISO:RGD.
DR GO; GO:0030901; P:midbrain development; IEP:RGD.
DR GO; GO:1901383; P:negative regulation of chorionic trophoblast cell proliferation; ISO:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:RGD.
DR GO; GO:1901164; P:negative regulation of trophoblast cell migration; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0038092; P:nodal signaling pathway; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:HGNC-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; ISO:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; IDA:RGD.
DR GO; GO:0001834; P:trophectodermal cell proliferation; ISO:RGD.
DR Gene3D; 2.10.60.10; -; 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; PTHR23255; 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; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 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 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Direct protein sequencing; Kinase; Magnesium;
KW Manganese; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..493
FT /note="Activin receptor type-1C"
FT /id="PRO_0000042630"
FT TOPO_DOM 26..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"
FT MUTAGEN 194
FT /note="T->D: Constitutively activates downstream
FT transcription factor function."
FT /evidence="ECO:0000269|PubMed:8875430,
FT ECO:0000269|PubMed:9920806"
FT MUTAGEN 222
FT /note="K->R: Fails to activate downstream transcription
FT factor function."
FT /evidence="ECO:0000269|PubMed:8875430"
FT CONFLICT 5
FT /note="R -> S (in Ref. 2; AAC52919)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="S -> I (in Ref. 2; AAC52919)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="Q -> L (in Ref. 2; AAC52919)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="P -> L (in Ref. 2; AAC52919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54842 MW; FB2BB3C2A026BCC3 CRC64;
MTPARRSALS LALLLVALAS DLAAGLKCVC LLCDSSNFTC QTEGACWASV MLTNGKEQVS
KSCVSLPELN AQVFCHSSNN VTKTECCFTD FCNNITQHLP TASPDAPRLG PTELTVVITV
PVCLLSIAAM LTIWACQDRQ CTYRKTKRHN VEEPLAEYSL VNAGKTLKDL IYDATASGSG
SGPPLLVQRT IARTIVLQEI VGKGRFGEVW HGRWCGEDVA VKIFSSRDER SWFREAEIYQ
TVMLRHENIL GFIAADNKDN GTWTQLWLVS EYHEQGSLYD YLNRNIVTVA GMVKLALSIA
SGLAHLHMEI VGTQGKPAIA HRDIKSKNIL VKKCDTCAIA DLGLAVKHDS IMNTIDIPQN
PKVGTKRYMA PEMLDDTMNV NIFESFKRAD IYSVGLVYWE IARRCSVGGL VEEYQLPYYD
MVPSDPSIEE MRKVVCDQKL RPNLPNQWQS CEALRVMGRI MRECWYANGA ARLTALRVKK
TISQLCVKED CKA
