GET1_CANAW
ID GET1_CANAW Reviewed; 199 AA.
AC C4YJ00;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 50.
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=CAWG_03812;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; CH672350; EEQ45484.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YJ00; -.
DR SMR; C4YJ00; -.
DR STRING; 5476.C4YJ00; -.
DR EnsemblFungi; EEQ45484; EEQ45484; CAWG_03812.
DR VEuPathDB; FungiDB:CAWG_03812; -.
DR HOGENOM; CLU_089418_2_0_1; -.
DR OMA; WFGPLTW; -.
DR Proteomes; UP000001429; Chromosome 2, Supercontig 1.5.
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_0000388582"
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 76..116
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
SQ SEQUENCE 199 AA; 22982 MW; 1D97B2BFE5CF461A CRC64;
MLLPDLHPYT ILLSIFLVLV VKQLVATIGK STIQEFVWLV YLKVSSNQSI KTYNSKQHEL
HETNRQKRAI SAQDEYAKWT KLNRQADKLS AELQKLNQEI QQQKSSIDKA SNALILVLTT
LPIWIARVFY RKTHLFYIRQ GIFPKYVEWV LALPFLPNGA VGLTIWMFAV NSVVSNFSFL
VSFPFAKRVS KPVRDTKVE
