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GET1_CANGA
ID   GET1_CANGA              Reviewed;         223 AA.
AC   Q6FXV6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Golgi to ER traffic protein 1 {ECO:0000255|HAMAP-Rule:MF_03113};
DE   AltName: Full=Guided entry of tail-anchored proteins 1 {ECO:0000255|HAMAP-Rule:MF_03113};
GN   Name=GET1 {ECO:0000255|HAMAP-Rule:MF_03113};
GN   OrderedLocusNames=CAGL0A00253g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Required for the post-translational delivery of tail-anchored
CC       (TA) proteins to the endoplasmic reticulum. Together with GET2, acts as
CC       a membrane receptor for soluble GET3, which recognizes and selectively
CC       binds the transmembrane domain of TA proteins in the cytosol. The GET
CC       complex cooperates with the HDEL receptor ERD2 to mediate the ATP-
CC       dependent retrieval of resident ER proteins that contain a C-terminal
CC       H-D-E-L retention signal from the Golgi to the ER. {ECO:0000255|HAMAP-
CC       Rule:MF_03113}.
CC   -!- SUBUNIT: Component of the Golgi to ER traffic (GET) complex, which is
CC       composed of GET1, GET2 and GET3. Within the complex, GET1 and GET2 form
CC       a heterotetramer which is stabilized by phosphatidylinositol binding
CC       and which binds to the GET3 homodimer. {ECO:0000255|HAMAP-
CC       Rule:MF_03113}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03113}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03113}. Golgi apparatus membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03113}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03113}.
CC   -!- SIMILARITY: Belongs to the WRB/GET1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03113}.
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DR   EMBL; CR380947; CAG57674.1; -; Genomic_DNA.
DR   RefSeq; XP_444783.1; XM_444783.1.
DR   AlphaFoldDB; Q6FXV6; -.
DR   SMR; Q6FXV6; -.
DR   STRING; 5478.XP_444783.1; -.
DR   EnsemblFungi; CAG57674; CAG57674; CAGL0A00253g.
DR   GeneID; 2886439; -.
DR   KEGG; cgr:CAGL0A00253g; -.
DR   CGD; CAL0126877; CAGL0A00253g.
DR   VEuPathDB; FungiDB:CAGL0A00253g; -.
DR   eggNOG; KOG4253; Eukaryota.
DR   HOGENOM; CLU_089418_2_1_1; -.
DR   InParanoid; Q6FXV6; -.
DR   OMA; AQDNYAR; -.
DR   Proteomes; UP000002428; Chromosome A.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043529; C:GET complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0000423; P:mitophagy; IEA:EnsemblFungi.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IEA:InterPro.
DR   Gene3D; 1.10.287.660; -; 1.
DR   HAMAP; MF_03113; Get1; 1.
DR   InterPro; IPR028945; Get1.
DR   InterPro; IPR027538; Get1_fungi.
DR   InterPro; IPR029012; Helix_hairpin_bin_sf.
DR   Pfam; PF04420; CHD5; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..223
FT                   /note="Golgi to ER traffic protein 1"
FT                   /id="PRO_0000388585"
FT   TOPO_DOM        1
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        2..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        22..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        127..177
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        178..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        195..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   COILED          56..105
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
SQ   SEQUENCE   223 AA;  25489 MW;  550ED2E77A0979C7 CRC64;
     MSWVVAIAVV FVVVLKVLEY STSYHDLVLQ SLFFKNSPIS VKFETLVKER RSIQEENKSI
     SAQDNYAKWT KNNRKLDKLD KEITELGAQL KAHNEQIKGH LKKVKLLLLT VPFLCFKLWK
     GKHIVYNLPH HQMFPQLVAG VWSQGWLYLA ILPLQLAKSI VTGSSFAIET ASFPHMGVSL
     GIWLWALNSV ISNIEFMTMQ LWAKPVSKPS KKLEIVTDEI KVD
 
 
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