GET1_VANPO
ID GET1_VANPO Reviewed; 225 AA.
AC A7TKW8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 60.
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}; ORFNames=Kpol_1025p44;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480410; EDO17123.1; -; Genomic_DNA.
DR RefSeq; XP_001644981.1; XM_001644931.1.
DR AlphaFoldDB; A7TKW8; -.
DR STRING; 436907.A7TKW8; -.
DR EnsemblFungi; EDO17123; EDO17123; Kpol_1025p44.
DR GeneID; 5545318; -.
DR KEGG; vpo:Kpol_1025p44; -.
DR eggNOG; KOG4253; Eukaryota.
DR HOGENOM; CLU_089418_2_1_1; -.
DR InParanoid; A7TKW8; -.
DR OMA; AQDNYAR; -.
DR OrthoDB; 1498067at2759; -.
DR PhylomeDB; A7TKW8; -.
DR Proteomes; UP000000267; 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: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..225
FT /note="Golgi to ER traffic protein 1"
FT /id="PRO_0000388621"
FT TOPO_DOM 1
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TRANSMEM 2..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TOPO_DOM 22..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TOPO_DOM 129..172
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TRANSMEM 173..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TOPO_DOM 190..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT COILED 37..104
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
SQ SEQUENCE 225 AA; 25930 MW; ED60D18E4304512F CRC64;
MNWVIIAALF FVIINKLLQY TSRYQEAWIN KFSISSDISS LSKEYSKLSA ERLKIKEENQ
SISAQDNYAR WTKNNRKLTK LEGELEKLRS NLKIAKDSQS KLFNRLKLLT LTLPFMILKL
WKGKFIVYDI PTKDTFPVIV NGVLSQGLLY IPLLPINFLR GIDPNKHILV PGVSLGIWLM
ALTKTIDTVE FIVKQLVFQP VVSKQVKEKT KEKVVELKTT EAELD
