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GET1_PICST
ID   GET1_PICST              Reviewed;         229 AA.
AC   A3LMX9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 63.
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=PICST_29392;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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; CP000496; ABN64763.2; -; Genomic_DNA.
DR   RefSeq; XP_001382792.2; XM_001382755.1.
DR   AlphaFoldDB; A3LMX9; -.
DR   SMR; A3LMX9; -.
DR   STRING; 4924.XP_001382792.2; -.
DR   EnsemblFungi; ABN64763; ABN64763; PICST_29392.
DR   GeneID; 4836766; -.
DR   KEGG; pic:PICST_29392; -.
DR   eggNOG; KOG4253; Eukaryota.
DR   HOGENOM; CLU_089418_2_0_1; -.
DR   InParanoid; A3LMX9; -.
DR   OMA; WFGPLTW; -.
DR   OrthoDB; 1498067at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..229
FT                   /note="Golgi to ER traffic protein 1"
FT                   /id="PRO_0000388611"
FT   TOPO_DOM        1..14
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        35..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        144..167
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        168..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        185..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   REGION          210..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          60..117
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
SQ   SEQUENCE   229 AA;  25785 MW;  EB076AB5926A1FB2 CRC64;
     MGILAALDLH PYTLVVSSFT VLLIQQLVGF IGKSTIQEFA WLFYLRVGGK LGLSNSFVAH
     TKKQEELHKL NREKRSISAQ DEYAKWTKLN RQAEKLTAEV KSLSDDIAKD KSKINSLVGV
     VLLFLTTLPL WVFRLWFRKS VLFYLPTGVF PYYVERVLAI PFFASGSVGL TVWMFAVNNV
     ISSVLFLLTF PFKPSVPIPI RQTKVEEVVP ESAESKESSP EVIDIADAN
 
 
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