ID   GET2_CANDC              Reviewed;         301 AA.
AC   B9W8Z2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Golgi to ER traffic protein 2 {ECO:0000255|HAMAP-Rule:MF_03114};
GN   Name=GET2 {ECO:0000255|HAMAP-Rule:MF_03114}; ORFNames=CD36_09180;
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 GET1, 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_03114}.
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_03114}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03114}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03114}. Golgi apparatus membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03114}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03114}.
CC   -!- SIMILARITY: Belongs to the GET2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03114}.
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DR   EMBL; FM992688; CAX45217.1; -; Genomic_DNA.
DR   RefSeq; XP_002417562.1; XM_002417517.1.
DR   AlphaFoldDB; B9W8Z2; -.
DR   SMR; B9W8Z2; -.
DR   STRING; 42374.XP_002417562.1; -.
DR   EnsemblFungi; CAX45217; CAX45217; CD36_09180.
DR   GeneID; 8045109; -.
DR   KEGG; cdu:CD36_09180; -.
DR   CGD; CAL0000161574; Cd36_09180.
DR   VEuPathDB; FungiDB:CD36_09180; -.
DR   eggNOG; ENOG502QW0H; Eukaryota.
DR   HOGENOM; CLU_066477_0_0_1; -.
DR   OrthoDB; 1416320at2759; -.
DR   Proteomes; UP000002605; Chromosome 1.
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:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_03114; Get2; 1.
DR   InterPro; IPR014802; GET2.
DR   InterPro; IPR028143; Get2/sif1.
DR   PANTHER; PTHR28263; PTHR28263; 1.
DR   Pfam; PF08690; GET2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..301
FT                   /note="Golgi to ER traffic protein 2"
FT                   /id="PRO_0000388627"
FT   TOPO_DOM        1..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TOPO_DOM        189..214
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TRANSMEM        215..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TOPO_DOM        235..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   TOPO_DOM        300..301
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT   REGION          42..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  34034 MW;  EABA438FB7AA898B CRC64;
     MSEPVVDTAE LSAEEKKRLL RERRQAKMSK GKATARLNNI LSQGSSVKTS GVKSVLDQEK
     EATSSHDDDP EIQDITEITT PPPRTPPIGE DAPQDIDKIF QTMLQQQQQR GQGANTADDP
     FAQIMKMFNQ TEGPDSLINE GSASTQDPTE IKYHQELLEY NTYNQKLWKF RFLLVRVLVT
     LFNFFYHYTS ISDFHASNYA YVRDLSSEEY PVRDFFTWFA TSEVVLVAAY YSVFHSLGLF
     HAANQNSIIL KVMSMGSMIL PQLESYKPLV ARFLGYYELL GIVLGGLSLV IVLFGLLSFA
     N