ID A0A2U3YE90_LEPWE Unreviewed; 188 AA.
AC A0A2U3YE90;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Calcium load-activated calcium channel {ECO:0000256|ARBA:ARBA00014950, ECO:0000256|PIRNR:PIRNR023322};
DE Short=CLAC channel {ECO:0000256|PIRNR:PIRNR023322};
GN Name=TMCO1 {ECO:0000313|RefSeq:XP_006742055.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006742055.1};
RN [1] {ECO:0000313|RefSeq:XP_006742055.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006742055.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Calcium-selective channel required to prevent calcium stores
CC from overfilling. {ECO:0000256|PIRNR:PIRNR023322}.
CC -!- SUBUNIT: Homodimer and homotetramer. Homodimer under resting
CC conditions; forms homotetramers following and ER calcium overload.
CC {ECO:0000256|PIRNR:PIRNR023322}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TMCO1 family.
CC {ECO:0000256|ARBA:ARBA00006537, ECO:0000256|PIRNR:PIRNR023322}.
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DR RefSeq; XP_006742055.1; XM_006741992.2.
DR AlphaFoldDB; A0A2U3YE90; -.
DR SMR; A0A2U3YE90; -.
DR STRING; 9713.A0A2U3YE90; -.
DR GeneID; 102728759; -.
DR KEGG; lww:102728759; -.
DR CTD; 54499; -.
DR OrthoDB; 313692at2759; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IEA:UniProtKB-UniRule.
DR InterPro; IPR002809; EMC3/TMCO1.
DR InterPro; IPR008559; TMCO1.
DR PANTHER; PTHR20917:SF0; CALCIUM LOAD-ACTIVATED CALCIUM CHANNEL; 1.
DR PANTHER; PTHR20917; PNAS-RELATED; 1.
DR Pfam; PF01956; EMC3_TMCO1; 1.
DR PIRSF; PIRSF023322; DUF841_euk; 1.
DR SMART; SM01415; DUF106; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR023322};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|PIRNR:PIRNR023322};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR023322};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR023322};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR023322};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR023322}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..188
FT /note="Calcium load-activated calcium channel"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015601708"
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT COILED 33..89
FT /evidence="ECO:0000256|SAM:Coils"
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
//