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GET1_CANDC
ID   GET1_CANDC              Reviewed;         199 AA.
AC   B9WA88;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=CD36_15290;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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; FM992689; CAX43307.1; -; Genomic_DNA.
DR   RefSeq; XP_002418008.1; XM_002417963.1.
DR   AlphaFoldDB; B9WA88; -.
DR   SMR; B9WA88; -.
DR   STRING; 42374.XP_002418008.1; -.
DR   EnsemblFungi; CAX43307; CAX43307; CD36_15290.
DR   GeneID; 8045589; -.
DR   KEGG; cdu:CD36_15290; -.
DR   CGD; CAL0000167744; Cd36_15290.
DR   VEuPathDB; FungiDB:CD36_15290; -.
DR   eggNOG; KOG4253; Eukaryota.
DR   HOGENOM; CLU_089418_2_0_1; -.
DR   OrthoDB; 1498067at2759; -.
DR   Proteomes; UP000002605; 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; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..199
FT                   /note="Golgi to ER traffic protein 1"
FT                   /id="PRO_0000388584"
FT   TOPO_DOM        1..11
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        32..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        137..160
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        161..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        178..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   COILED          66..116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
SQ   SEQUENCE   199 AA;  22889 MW;  64BFD825E743B447 CRC64;
     MLLPDLHPYT ILLSIFIVLL LKQLVASIGK STIKEFVWLV YLKVSSNQSI KTYNSKQHEL
     HETNKEKRAI SAQDEYAKWT KLNRQADKLS AELQKLNQEI QQQKASIDKV SNALLLVLTT
     LPIWVARVLY RNTHLFYIRQ GIFPKYVEWV LALPFLPNGA VGLTIWMFAV NSVVSNFAFL
     VSFPFAKKVS KPVRDTKIE
 
 
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