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GET1_YEAS7
ID   GET1_YEAS7              Reviewed;         235 AA.
AC   A6ZUX3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 49.
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}; ORFNames=SCY_2206;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000102; EDN61581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZUX3; -.
DR   SMR; A6ZUX3; -.
DR   TopDownProteomics; A6ZUX3; -.
DR   EnsemblFungi; EDN61581; EDN61581; SCY_2206.
DR   HOGENOM; CLU_089418_2_1_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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:0071816; P:tail-anchored membrane protein insertion into ER membrane; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..235
FT                   /note="Golgi to ER traffic protein 1"
FT                   /id="PRO_0000388616"
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..104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        126..181
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        182..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        199..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   COILED          68..104
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
SQ   SEQUENCE   235 AA;  27092 MW;  C43DC5928D97DB7D CRC64;
     MHWAAAVAIF FIVVTKFLQY TNKYHEKWIS KFAPGNELSK KYLAKVKERH ELKEFNNSIS
     AQDNYAKWTK NNRKLDSLDK EINNLKDEIQ SENKAFQAHL HKLRLLALTV PFFVFKIMYG
     KTPVYKLSSS TSTLFPTFVS GVWSQGWLYV LLHPLRTISQ KWHIMEGKFG ASKFDDMALQ
     SVSLGIWVWA LMNVINGVEF IVKQLFLTPK MEAPASVETQ EEKALDAVDD AIILD
 
 
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