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TMCO1_DANRE
ID   TMCO1_DANRE             Reviewed;         188 AA.
AC   Q6DGW9; A8E529; B0S7X3; Q568F9;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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:0000312|ZFIN:ZDB-GENE-050417-344};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, Liver, and Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=27212239; DOI=10.1016/j.cell.2016.04.051;
RA   Wang Q.C., Zheng Q., Tan H., Zhang B., Li X., Yang Y., Yu J., Liu Y.,
RA   Chai H., Wang X., Sun Z., Wang J.Q., Zhu S., Wang F., Yang M., Guo C.,
RA   Wang H., Zheng Q., Li Y., Chen Q., Zhou A., Tang T.S.;
RT   "TMCO1 is an ER Ca(2+) load-activated Ca(2+) channel.";
RL   Cell 165:1454-1466(2016).
CC   -!- FUNCTION: Calcium-selective channel required to prevent calcium stores
CC       from overfilling, thereby playing a key role in calcium homeostasis
CC       (PubMed:27212239). In response to endoplasmic reticulum (ER)
CC       overloading, assembles into a homotetramer, forming a functional
CC       calcium-selective channel, regulating the calcium content in
CC       endoplasmic reticulum store (By similarity). Necessary for the
CC       biogenesis and transport of multi-pass membrane proteins into the ER
CC       membrane (By similarity). {ECO:0000250|UniProtKB:Q9UM00,
CC       ECO:0000305|PubMed:27212239}.
CC   -!- SUBUNIT: Homodimer and homotetramer. Component of the ribosome-
CC       associated ER translocon complex. {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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6DGW9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6DGW9-2; Sequence=VSP_058496;
CC   -!- SIMILARITY: Belongs to the TMCO1 family. {ECO:0000305}.
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DR   EMBL; BX927144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC076218; AAH76218.1; -; mRNA.
DR   EMBL; BC092873; AAH92873.1; -; mRNA.
DR   EMBL; BC152265; AAI52266.1; -; mRNA.
DR   EMBL; BC153441; AAI53442.1; -; mRNA.
DR   EMBL; BC164974; AAI64974.1; -; mRNA.
DR   RefSeq; NP_001002575.1; NM_001002575.1. [Q6DGW9-1]
DR   AlphaFoldDB; Q6DGW9; -.
DR   SMR; Q6DGW9; -.
DR   STRING; 7955.ENSDARP00000091049; -.
DR   PaxDb; Q6DGW9; -.
DR   Ensembl; ENSDART00000100276; ENSDARP00000091049; ENSDARG00000069099. [Q6DGW9-1]
DR   Ensembl; ENSDART00000127371; ENSDARP00000106023; ENSDARG00000069099. [Q6DGW9-2]
DR   Ensembl; ENSDART00000187923; ENSDARP00000147474; ENSDARG00000113013. [Q6DGW9-2]
DR   GeneID; 378980; -.
DR   KEGG; dre:378980; -.
DR   CTD; 54499; -.
DR   ZFIN; ZDB-GENE-050417-344; tmco1.
DR   eggNOG; KOG3312; Eukaryota.
DR   GeneTree; ENSGT00390000002659; -.
DR   HOGENOM; CLU_081121_0_0_1; -.
DR   InParanoid; Q6DGW9; -.
DR   OMA; WADTLLI; -.
DR   OrthoDB; 1506634at2759; -.
DR   PhylomeDB; Q6DGW9; -.
DR   TreeFam; TF315045; -.
DR   PRO; PR:Q6DGW9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000069099; Expressed in early embryo and 30 other tissues.
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; IDA:UniProtKB.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IDA: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   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Coiled coil; Endoplasmic reticulum; Golgi apparatus; Ion channel;
KW   Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..188
FT                   /note="Calcium load-activated calcium channel"
FT                   /id="PRO_0000437215"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..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..133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM00"
FT   INTRAMEM        134..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   VAR_SEQ         1..23
FT                   /note="MSTMFADTILIVFISICTALLAE -> MQDKYSSKAALQFVSLCFT (in
FT                   isoform 2)"
FT                   /id="VSP_058496"
FT   CONFLICT        34
FT                   /note="D -> G (in Ref. 2; AAI53442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="R -> G (in Ref. 2; AAI53442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q6DGW9-2:9
FT                   /note="A -> S (in Ref. 2; AAH92873/AAI64974)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   188 AA;  21310 MW;  055C7526D96BA6C7 CRC64;
     MSTMFADTIL IVFISICTAL LAEGITWVLV YRTDKYKRLK AEVEKQSKKL EKKKETITES
     AGRQQKKKIE RQEEKLKNNN RDLSMVRMKS MFAIGFCFTA LMGMFNSIFD GRVVAKLPFV
     PLSYIQGLSH RNLLGEDYTD CSFIFLYILC TMSIRQNIQK MLGLAPSRAA TKQAGGFLGP
     PPQAAKFS
 
 
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