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TMCO1_RAT
ID   TMCO1_RAT               Reviewed;         188 AA.
AC   Q5I0H4; Q71DI0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Calcium load-activated calcium channel {ECO:0000250|UniProtKB:Q9UM00};
DE            Short=CLAC channel {ECO:0000250|UniProtKB:Q9UM00};
DE   AltName: Full=Meg-2-like protein {ECO:0000303|Ref.2};
DE   AltName: Full=Transmembrane and coiled-coil domain-containing protein 1 {ECO:0000305};
GN   Name=Tmco1 {ECO:0000312|RGD:1359178};
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-186.
RC   STRAIN=Wistar;
RA   Miyata T., Inagi R., Nangaku M., Kurokawa K.;
RT   "Rat partial cDNA homologous to human mesangium-predominant gene, meg-2.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Calcium-selective channel required to prevent calcium stores
CC       from overfilling, thereby playing a key role in calcium homeostasis. In
CC       response to endoplasmic reticulum (ER) overloading, assembles into a
CC       homotetramer, forming a functional calcium-selective channel,
CC       regulating the calcium content in endoplasmic reticulum store.
CC       Component of a ribosome-associated ER translocon complex involved in
CC       multi-pass membrane protein transport into the ER membrane and
CC       biogenesis. Together with SEC61 and TMEM147, forms the lipid-filled
CC       cavity at the center of the translocon where TMEM147 may insert
CC       hydrophobic segments of mutli-pass membrane proteins from the lumen
CC       into de central membrane cavity in a process gated by SEC61, and TMCO1
CC       may insert hydrophobic segments of nascent chains from the cytosol into
CC       the cavity. {ECO:0000250|UniProtKB:Q9UM00}.
CC   -!- SUBUNIT: Homodimer and homotetramer. Homodimer under resting
CC       conditions; forms homotetramers following and ER calcium overload. The
CC       ribosome-associated ER translocon complex includes SEC61A1, SEC61B,
CC       SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence
CC       of ribosomes, only the complex forms with NCLN/Nicalin, NOMO and
CC       TMEM147 remains intact. {ECO:0000250|UniProtKB:Q9UM00}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9UM00}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9UM00}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9UM00}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9UM00}. Note=The first transmembrane region is
CC       required for localization to the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:Q9UM00}.
CC   -!- SIMILARITY: Belongs to the TMCO1 family. {ECO:0000305}.
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DR   EMBL; BC088319; AAH88319.1; -; mRNA.
DR   EMBL; AF531432; AAQ09812.1; -; mRNA.
DR   RefSeq; NP_001009631.1; NM_001009631.1.
DR   RefSeq; XP_017454197.1; XM_017598708.1.
DR   AlphaFoldDB; Q5I0H4; -.
DR   SMR; Q5I0H4; -.
DR   STRING; 10116.ENSRNOP00000005277; -.
DR   jPOST; Q5I0H4; -.
DR   PaxDb; Q5I0H4; -.
DR   PRIDE; Q5I0H4; -.
DR   GeneID; 289196; -.
DR   KEGG; rno:289196; -.
DR   UCSC; RGD:1359178; rat.
DR   CTD; 54499; -.
DR   RGD; 1359178; Tmco1.
DR   VEuPathDB; HostDB:ENSRNOG00000003928; -.
DR   eggNOG; KOG3312; Eukaryota.
DR   InParanoid; Q5I0H4; -.
DR   OMA; WADTLLI; -.
DR   OrthoDB; 1506634at2759; -.
DR   PhylomeDB; Q5I0H4; -.
DR   PRO; PR:Q5I0H4; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003928; Expressed in liver and 20 other tissues.
DR   Genevisible; Q5I0H4; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0006983; P:ER overload response; ISS:UniProtKB.
DR   InterPro; IPR002809; EMC3/TMCO1.
DR   InterPro; IPR008559; TMCO1.
DR   PANTHER; PTHR20917; PTHR20917; 1.
DR   Pfam; PF01956; EMC3_TMCO1; 1.
DR   PIRSF; PIRSF023322; DUF841_euk; 1.
DR   SMART; SM01415; DUF106; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Coiled coil;
KW   Endoplasmic reticulum; Golgi apparatus; Ion channel; Ion transport;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..188
FT                   /note="Calcium load-activated calcium channel"
FT                   /id="PRO_0000244079"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..90
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   INTRAMEM        138..154
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   TOPO_DOM        155..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   COILED          32..89
FT                   /evidence="ECO:0000255"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   CONFLICT        45
FT                   /note="K -> I (in Ref. 2; AAQ09812)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   188 AA;  21175 MW;  FB77BFC4F0629EB1 CRC64;
     MSTMFADTLL IVFISVCTAL LAEGITWVLV YRTDKYKRLK AEVEKQSKKL EKKKETITES
     AGRQQKKKIE RQEEKLKNNN RDLSMVRMKS MFAIGFCFTA LMGMFNSIFD GRVVAKLPFT
     PLSYIQGLSH RNLLGDDTTD CSFIFLYILC TMSIRQNIQK ILGLAPSRAA TKQAGGFLGP
     PPPSGKFS
 
 
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