GET1_ASHGO
ID GET1_ASHGO Reviewed; 205 AA.
AC Q754R6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Golgi to ER traffic protein 1 {ECO:0000255|HAMAP-Rule:MF_03113};
DE AltName: Full=Guided entry of tail-anchored proteins 1 {ECO:0000255|HAMAP-Rule:MF_03113};
GN Name=GET1 {ECO:0000255|HAMAP-Rule:MF_03113}; OrderedLocusNames=AFR006C;
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 GET2, 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_03113}.
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_03113}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03113}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03113}. Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_03113}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03113}.
CC -!- SIMILARITY: Belongs to the WRB/GET1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03113}.
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DR EMBL; AE016819; AAS53377.1; -; Genomic_DNA.
DR RefSeq; NP_985553.1; NM_210907.1.
DR AlphaFoldDB; Q754R6; -.
DR SMR; Q754R6; -.
DR STRING; 33169.AAS53377; -.
DR GeneID; 4621792; -.
DR KEGG; ago:AGOS_AFR006C; -.
DR eggNOG; KOG4253; Eukaryota.
DR InParanoid; Q754R6; -.
DR Proteomes; UP000000591; Chromosome VI.
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:0071816; P:tail-anchored membrane protein insertion into ER membrane; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.660; -; 1.
DR HAMAP; MF_03113; Get1; 1.
DR InterPro; IPR028945; Get1.
DR InterPro; IPR027538; Get1_fungi.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR Pfam; PF04420; CHD5; 1.
PE 3: Inferred from homology;
KW Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..205
FT /note="Golgi to ER traffic protein 1"
FT /id="PRO_0000388574"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TOPO_DOM 25..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TOPO_DOM 118..156
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TRANSMEM 157..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TOPO_DOM 174..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT COILED 32..96
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
SQ SEQUENCE 205 AA; 23342 MW; D1CF9E117B22ED6F CRC64;
MDYWILLVLA FLVADKSWHL TGLLATKLTS PERLQQLIRE RQELHQQQQS LSAQDHYAKW
TKNNRRLDVL DRDIARVRKN YLESVEATKA RLAKLKLLVV TVPFTALKFY KGKLPVYALP
KGMFPRFIEG TLEHGWLYMA LAPLNMKQFS EGASVAVSLG IWLFALLRVL GAIEFVLETL
REQNPQVATE TAKVHARTAQ AASAN
