GET2_CLAL4
ID GET2_CLAL4 Reviewed; 292 AA.
AC C4YCC3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 47.
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=CLUG_05762;
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720;
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; CH408083; EEQ41634.1; -; Genomic_DNA.
DR RefSeq; XP_002614276.1; XM_002614230.1.
DR AlphaFoldDB; C4YCC3; -.
DR SMR; C4YCC3; -.
DR STRING; 306902.C4YCC3; -.
DR EnsemblFungi; EEQ41634; EEQ41634; CLUG_05762.
DR GeneID; 8494732; -.
DR KEGG; clu:CLUG_05762; -.
DR VEuPathDB; FungiDB:CLUG_05762; -.
DR HOGENOM; CLU_066477_0_0_1; -.
DR InParanoid; C4YCC3; -.
DR OMA; ALQYWDV; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..292
FT /note="Golgi to ER traffic protein 2"
FT /id="PRO_0000388630"
FT TOPO_DOM 1..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 180..205
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 206..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 226..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 290..292
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 292 AA; 32394 MW; C5ED91ADB9D2B176 CRC64;
MSELSAEEKR KLLRERRQAK MAQGKATDRL NNILSQGSSV KSSNVTSVLD KPEKATTTVM
DLPSRETQSP TPLHDDPEVP DITSLLKEKE NEAPDMEAML QQILGGSGAH TGPGNDGGAN
FLQEMMKAMA EDPSGGSTAE ESSYQSQLSQ YHAYEQKQWK ARFLVVRWII HTLNFVYHYI
ASGYKLSASP YAFVRAQAVD SHVRTFFTAF LTVEVAVISA YFLVMSQPKF KDFSRENLVS
RILSMASAVV PAVGRYQPLV TRALVYWNGA SIFVGDLMLM VFYFGITSVL GN
