GET2_ASHGO
ID GET2_ASHGO Reviewed; 289 AA.
AC Q75CF5;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Golgi to ER traffic protein 2 {ECO:0000255|HAMAP-Rule:MF_03114};
GN Name=GET2 {ECO:0000255|HAMAP-Rule:MF_03114}; OrderedLocusNames=ACL036W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016816; AAS51192.1; -; Genomic_DNA.
DR RefSeq; NP_983368.1; NM_208721.1.
DR AlphaFoldDB; Q75CF5; -.
DR SMR; Q75CF5; -.
DR STRING; 33169.AAS51192; -.
DR EnsemblFungi; AAS51192; AAS51192; AGOS_ACL036W.
DR GeneID; 4619493; -.
DR KEGG; ago:AGOS_ACL036W; -.
DR eggNOG; ENOG502QW0H; Eukaryota.
DR HOGENOM; CLU_066477_0_0_1; -.
DR InParanoid; Q75CF5; -.
DR OMA; ALQYWDV; -.
DR Proteomes; UP000000591; Chromosome III.
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:0043495; F:protein-membrane adaptor activity; IEA:EnsemblFungi.
DR GO; GO:0000423; P:mitophagy; IEA:EnsemblFungi.
DR GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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..289
FT /note="Golgi to ER traffic protein 2"
FT /id="PRO_0000388624"
FT TOPO_DOM 1..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 174..196
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 217..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT TOPO_DOM 285..289
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03114"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 31959 MW; 29E7843AAFB12DE7 CRC64;
MSEVSEAEKR RILREKRKQK FSKGAGSARL HKITTQQPGG ASGDSTVTSA EISDNEGSLQ
RGSNSGQSTR EIDDLLAAMD PPIEPAEPLE SAAPEVAFIQ QLMKMQQGSA TPPADEKAGG
LFSPLLERLA EQEAGGAPVV SGEVGVHQFQ VRQLKAYMLL LRWAILLPFI YYVMHPGTAH
WLHTSRFLHF VMEPRNFFMV FTTFEVASIS IYYQVLLTLE RTNKVNSLSY SSKLVTWAGL
VPDGMLPIDN LQGKVVVALH YWDILSMYLT DLSLCLVAAG LMKYYHAAP
