TMCO1_PONAB
ID TMCO1_PONAB Reviewed; 188 AA.
AC Q5R9B0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Calcium load-activated calcium channel {ECO:0000250|UniProtKB:Q9UM00};
DE Short=CLAC channel {ECO:0000250|UniProtKB:Q9UM00};
DE AltName: Full=Transmembrane and coiled-coil domain-containing protein 1 {ECO:0000250|UniProtKB:Q9UM00};
GN Name=TMCO1 {ECO:0000250|UniProtKB:Q9UM00};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859479; CAH91650.1; -; mRNA.
DR RefSeq; NP_001125969.1; NM_001132497.1.
DR AlphaFoldDB; Q5R9B0; -.
DR SMR; Q5R9B0; -.
DR STRING; 9601.ENSPPYP00000000661; -.
DR GeneID; 100172905; -.
DR KEGG; pon:100172905; -.
DR CTD; 54499; -.
DR eggNOG; KOG3312; Eukaryota.
DR InParanoid; Q5R9B0; -.
DR OrthoDB; 1506634at2759; -.
DR Proteomes; UP000001595; Unplaced.
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: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_0000244078"
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"
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
