GET2_ZYGRC
ID GET2_ZYGRC Reviewed; 266 AA.
AC C5DTJ3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Golgi to ER traffic protein 2 {ECO:0000255|HAMAP-Rule:MF_03114};
GN Name=GET2 {ECO:0000255|HAMAP-Rule:MF_03114};
GN OrderedLocusNames=ZYRO0C09020g;
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(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; CU928175; CAR27104.1; -; Genomic_DNA.
DR RefSeq; XP_002496037.1; XM_002495992.1.
DR AlphaFoldDB; C5DTJ3; -.
DR SMR; C5DTJ3; -.
DR STRING; 559307.C5DTJ3; -.
DR EnsemblFungi; CAR27104; CAR27104; ZYRO0C09020g.
DR GeneID; 8203249; -.
DR KEGG; zro:ZYRO0C09020g; -.
DR HOGENOM; CLU_066477_0_0_1; -.
DR InParanoid; C5DTJ3; -.
DR Proteomes; UP000008536; Chromosome C.
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..266
FT /note="Golgi to ER traffic protein 2"
FT /id="PRO_0000388641"
FT TOPO_DOM 1..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 161..177
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 198..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 266
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 29743 MW; 9FC87ED0A73005F7 CRC64;
MSELSDAEKR RILKERRQKK FGSGGGTNRL NKITGQADSL MSTESTLDQR ERTPEAAINT
RQNEAGNNQS TTDNNPQVSL LKQLAEQDRQ EGSEAPPDLM SMLQSMTGGD AKNGTPPTLG
TPPAPVDQSM LDYHNYLVNR LKAWSIIIKW IVLLPYMYVV THDVPLSLPF GLMDSSNFFS
VLMGFEIVAT SIYYKRLQSI EKGTSVNTMM HGSMIAKLIS LIPDQAPQQK NLKSRLFTLL
QYWDVVSMLI TDICFVLVVL GIFTHI
