GET2_CANAW
ID GET2_CANAW Reviewed; 298 AA.
AC P0CB64; Q5APC6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 42.
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=CAWG_00456;
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 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; CH672346; EEQ42252.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CB64; -.
DR SMR; P0CB64; -.
DR STRING; 5476.P0CB64; -.
DR EnsemblFungi; EEQ42252; EEQ42252; CAWG_00456.
DR VEuPathDB; FungiDB:CAWG_00456; -.
DR HOGENOM; CLU_066477_0_0_1; -.
DR OMA; ALQYWDV; -.
DR Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
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..298
FT /note="Golgi to ER traffic protein 2"
FT /id="PRO_0000388625"
FT TOPO_DOM 1..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 186..211
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 232..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 297..298
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT REGION 40..92
FT /note="Disordered"
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 298 AA; 33632 MW; 247A5AF2D45C5DDC CRC64;
MSEPVVDTAE LSAEEKKRLL RERRQAKMSK GKATARLNDI LSQGSSVKTS GVKSVLDQEK
EATPSHDEDP EIQDITEITT PPPRTPPIGE DAPQDIDKIF QSMLQQQGQG ADTAGDPFAQ
IMKMFNQVEG GDSPPSESAT STQDPAELKY RQELLEYNTY NQKLWKFRFL LVRVSVTLFN
FFYHYINLSN FHASNYAYVR DLSSEKYPVR DFFTWFATTE VVLVAAYYSI FHSLGLFHAA
NQNSFVLKAM SMGSMVLPQL EHYKPLVARF LGYYELLGIV LGDLSLVIVL FGLLSFAN
