GET1_YEAST
ID GET1_YEAST Reviewed; 235 AA.
AC P53192; D6VUB7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
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};
DE AltName: Full=Mitochondrial distribution and morphology protein 39;
GN Name=GET1 {ECO:0000255|HAMAP-Rule:MF_03113}; Synonyms=MDM39;
GN OrderedLocusNames=YGL020C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
RA Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N., Neupert W.,
RA Westermann B.;
RT "Genetic basis of mitochondrial function and morphology in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:847-853(2002).
RN [4]
RP IDENTIFICATION IN GET COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11805837; DOI=10.1038/415180a;
RA Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.-L.,
RA Millar A., Taylor P., Bennett K., Boutilier K., Yang L., Wolting C.,
RA Donaldson I., Schandorff S., Shewnarane J., Vo M., Taggart J.,
RA Goudreault M., Muskat B., Alfarano C., Dewar D., Lin Z., Michalickova K.,
RA Willems A.R., Sassi H., Nielsen P.A., Rasmussen K.J., Andersen J.R.,
RA Johansen L.E., Hansen L.H., Jespersen H., Podtelejnikov A., Nielsen E.,
RA Crawford J., Poulsen V., Soerensen B.D., Matthiesen J., Hendrickson R.C.,
RA Gleeson F., Pawson T., Moran M.F., Durocher D., Mann M., Hogue C.W.V.,
RA Figeys D., Tyers M.;
RT "Systematic identification of protein complexes in Saccharomyces cerevisiae
RT by mass spectrometry.";
RL Nature 415:180-183(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, IDENTIFICATION IN GET COMPLEX, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GET3.
RX PubMed=16269340; DOI=10.1016/j.cell.2005.08.031;
RA Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A.,
RA Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S.,
RA Krogan N.J.;
RT "Exploration of the function and organization of the yeast early secretory
RT pathway through an epistatic miniarray profile.";
RL Cell 123:507-519(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15909163; DOI=10.1007/s00438-005-1153-6;
RA Ando A., Suzuki C.;
RT "Cooperative function of the CHD5-like protein Mdm39p with a P-type ATPase
RT Spf1p in the maintenance of ER homeostasis in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 273:497-506(2005).
RN [9]
RP INTERACTION WITH GET3.
RX PubMed=16816426; DOI=10.1534/genetics.106.058362;
RA Auld K.L., Hitchcock A.L., Doherty H.K., Frietze S., Huang L.S.,
RA Silver P.A.;
RT "The conserved ATPase Get3/Arr4 modulates the activity of membrane-
RT associated proteins in Saccharomyces cerevisiae.";
RL Genetics 174:215-227(2006).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [11]
RP FUNCTION.
RX PubMed=18724936; DOI=10.1016/j.cell.2008.06.025;
RA Schuldiner M., Metz J., Schmid V., Denic V., Rakwalska M., Schmitt H.D.,
RA Schwappach B., Weissman J.S.;
RT "The GET complex mediates insertion of tail-anchored proteins into the ER
RT membrane.";
RL Cell 134:634-645(2008).
RN [12]
RP FUNCTION.
RX PubMed=24392163; DOI=10.1371/journal.pone.0085033;
RA Vilardi F., Stephan M., Clancy A., Janshoff A., Schwappach B.;
RT "WRB and CAML are necessary and sufficient to mediate tail-anchored protein
RT targeting to the ER membrane.";
RL PLoS ONE 9:e85033-e85033(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-104, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND TOPOLOGY.
RX PubMed=21835666; DOI=10.1016/j.molcel.2011.07.020;
RA Wang F., Whynot A., Tung M., Denic V.;
RT "The mechanism of tail-anchored protein insertion into the ER membrane.";
RL Mol. Cell 43:738-750(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 19-103 IN COMPLEX WITH GET2 AND
RP GET3, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21719644; DOI=10.1126/science.1207125;
RA Stefer S., Reitz S., Wang F., Wild K., Pang Y.Y., Schwarz D., Bomke J.,
RA Hein C., Lohr F., Bernhard F., Denic V., Dotsch V., Sinning I.;
RT "Structural basis for tail-anchored membrane protein biogenesis by the
RT Get3-receptor complex.";
RL Science 333:758-762(2011).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (14 ANGSTROMS) OF THE GET COMPLEX.
RX PubMed=32910895; DOI=10.1016/j.molcel.2020.08.012;
RA McDowell M.A., Heimes M., Fiorentino F., Mehmood S., Farkas A.,
RA Coy-Vergara J., Wu D., Bolla J.R., Schmid V., Heinze R., Wild K.,
RA Flemming D., Pfeffer S., Schwappach B., Robinson C.V., Sinning I.;
RT "Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET
RT Insertase Complex.";
RL Mol. Cell 80:72-86(2020).
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. Involved in
CC mitochondrial distribution and morphology. {ECO:0000255|HAMAP-
CC Rule:MF_03113, ECO:0000269|PubMed:11907266,
CC ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:18724936,
CC ECO:0000269|PubMed:21719644, ECO:0000269|PubMed:21835666,
CC ECO:0000269|PubMed:24392163}.
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 (PubMed:32910895).
CC {ECO:0000255|HAMAP-Rule:MF_03113, ECO:0000269|PubMed:11805837,
CC ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:21719644,
CC ECO:0000269|PubMed:21835666, ECO:0000269|PubMed:32910895}.
CC -!- INTERACTION:
CC P53192; P40056: GET2; NbExp=3; IntAct=EBI-23722, EBI-22604;
CC P53192; Q12154: GET3; NbExp=12; IntAct=EBI-23722, EBI-2989;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein. Mitochondrion membrane {ECO:0000269|PubMed:16823961}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WRB/GET1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03113}.
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DR EMBL; Z72542; CAA96720.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08078.1; -; Genomic_DNA.
DR PIR; S64022; S64022.
DR RefSeq; NP_011495.1; NM_001180885.1.
DR PDB; 3B2E; X-ray; 3.00 A; E/F/G/H=21-104.
DR PDB; 3SJA; X-ray; 3.00 A; C/D/G/H/J=36-93.
DR PDB; 3SJB; X-ray; 3.30 A; C/D=19-103.
DR PDB; 3SJC; X-ray; 3.20 A; C/D/G/H=36-93.
DR PDB; 3VLC; X-ray; 4.50 A; E=21-104.
DR PDB; 3ZS8; X-ray; 3.00 A; C/D=21-104.
DR PDBsum; 3B2E; -.
DR PDBsum; 3SJA; -.
DR PDBsum; 3SJB; -.
DR PDBsum; 3SJC; -.
DR PDBsum; 3VLC; -.
DR PDBsum; 3ZS8; -.
DR AlphaFoldDB; P53192; -.
DR SMR; P53192; -.
DR BioGRID; 33226; 777.
DR ComplexPortal; CPX-956; GET complex.
DR DIP; DIP-6309N; -.
DR IntAct; P53192; 3.
DR MINT; P53192; -.
DR STRING; 4932.YGL020C; -.
DR TCDB; 3.A.21.1.1; the c-terminal tail-anchored membrane protein biogenesis/ insertion complex (tamp-b) family.
DR MaxQB; P53192; -.
DR PaxDb; P53192; -.
DR PRIDE; P53192; -.
DR EnsemblFungi; YGL020C_mRNA; YGL020C; YGL020C.
DR GeneID; 852864; -.
DR KEGG; sce:YGL020C; -.
DR SGD; S000002988; GET1.
DR VEuPathDB; FungiDB:YGL020C; -.
DR eggNOG; KOG4253; Eukaryota.
DR HOGENOM; CLU_089418_2_1_1; -.
DR InParanoid; P53192; -.
DR OMA; AQDNYAR; -.
DR BioCyc; YEAST:G3O-30540-MON; -.
DR PRO; PR:P53192; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53192; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0043529; C:GET complex; IDA:UniProtKB.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IGI:SGD.
DR GO; GO:0000423; P:mitophagy; IMP:SGD.
DR GO; GO:0045048; P:protein insertion into ER membrane; IDA:ComplexPortal.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:SGD.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Mitochondrion; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..235
FT /note="Golgi to ER traffic protein 1"
FT /id="PRO_0000414847"
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..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TOPO_DOM 126..181
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TRANSMEM 182..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT TOPO_DOM 199..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT COILED 68..104
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT HELIX 40..56
FT /evidence="ECO:0007829|PDB:3B2E"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:3B2E"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:3B2E"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:3B2E"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:3B2E"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:3B2E"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3B2E"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:3SJB"
SQ SEQUENCE 235 AA; 27092 MW; C43DC5928D97DB7D CRC64;
MHWAAAVAIF FIVVTKFLQY TNKYHEKWIS KFAPGNELSK KYLAKVKERH ELKEFNNSIS
AQDNYAKWTK NNRKLDSLDK EINNLKDEIQ SENKAFQAHL HKLRLLALTV PFFVFKIMYG
KTPVYKLSSS TSTLFPTFVS GVWSQGWLYV LLHPLRTISQ KWHIMEGKFG ASKFDDMALQ
SVSLGIWVWA LMNVINGVEF IVKQLFLTPK MEAPASVETQ EEKALDAVDD AIILD
