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Golgi to ER traffic protein 1 (Guided entry of tail-anchored proteins 1) (Mitochondrial distribution and morphology protein 39)

 GET1_YEAST              Reviewed;         235 AA.
P53192; D6VUB7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 137.
RecName: Full=Golgi to ER traffic protein 1 {ECO:0000255|HAMAP-Rule:MF_03113};
AltName: Full=Guided entry of tail-anchored proteins 1 {ECO:0000255|HAMAP-Rule:MF_03113};
AltName: Full=Mitochondrial distribution and morphology protein 39;
Name=GET1 {ECO:0000255|HAMAP-Rule:MF_03113}; Synonyms=MDM39;
OrderedLocusNames=YGL020C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N.,
Neupert W., Westermann B.;
"Genetic basis of mitochondrial function and morphology in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 13:847-853(2002).
[4]
IDENTIFICATION IN GET COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11805837; DOI=10.1038/415180a;
Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.-L.,
Millar A., Taylor P., Bennett K., Boutilier K., Yang L., Wolting C.,
Donaldson I., Schandorff S., Shewnarane J., Vo M., Taggart J.,
Goudreault M., Muskat B., Alfarano C., Dewar D., Lin Z.,
Michalickova K., Willems A.R., Sassi H., Nielsen P.A., Rasmussen K.J.,
Andersen J.R., Johansen L.E., Hansen L.H., Jespersen H.,
Podtelejnikov A., Nielsen E., Crawford J., Poulsen V., Soerensen B.D.,
Matthiesen J., Hendrickson R.C., Gleeson F., Pawson T., Moran M.F.,
Durocher D., Mann M., Hogue C.W.V., Figeys D., Tyers M.;
"Systematic identification of protein complexes in Saccharomyces
cerevisiae by mass spectrometry.";
Nature 415:180-183(2002).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
FUNCTION, IDENTIFICATION IN GET COMPLEX, SUBCELLULAR LOCATION, AND
INTERACTION WITH GET3.
PubMed=16269340; DOI=10.1016/j.cell.2005.08.031;
Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A.,
Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F.,
Weissman J.S., Krogan N.J.;
"Exploration of the function and organization of the yeast early
secretory pathway through an epistatic miniarray profile.";
Cell 123:507-519(2005).
[8]
SUBCELLULAR LOCATION.
PubMed=15909163; DOI=10.1007/s00438-005-1153-6;
Ando A., Suzuki C.;
"Cooperative function of the CHD5-like protein Mdm39p with a P-type
ATPase Spf1p in the maintenance of ER homeostasis in Saccharomyces
cerevisiae.";
Mol. Genet. Genomics 273:497-506(2005).
[9]
INTERACTION WITH GET3.
PubMed=16816426; DOI=10.1534/genetics.106.058362;
Auld K.L., Hitchcock A.L., Doherty H.K., Frietze S., Huang L.S.,
Silver P.A.;
"The conserved ATPase Get3/Arr4 modulates the activity of membrane-
associated proteins in Saccharomyces cerevisiae.";
Genetics 174:215-227(2006).
[10]
FUNCTION.
PubMed=18724936; DOI=10.1016/j.cell.2008.06.025;
Schuldiner M., Metz J., Schmid V., Denic V., Rakwalska M.,
Schmitt H.D., Schwappach B., Weissman J.S.;
"The GET complex mediates insertion of tail-anchored proteins into the
ER membrane.";
Cell 134:634-645(2008).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-104, FUNCTION, SUBCELLULAR
LOCATION, SUBUNIT, AND TOPOLOGY.
PubMed=21835666; DOI=10.1016/j.molcel.2011.07.020;
Wang F., Whynot A., Tung M., Denic V.;
"The mechanism of tail-anchored protein insertion into the ER
membrane.";
Mol. Cell 43:738-750(2011).
[12]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 19-103 IN COMPLEX WITH GET2
AND GET3, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=21719644; DOI=10.1126/science.1207125;
Stefer S., Reitz S., Wang F., Wild K., Pang Y.Y., Schwarz D.,
Bomke J., Hein C., Lohr F., Bernhard F., Denic V., Dotsch V.,
Sinning I.;
"Structural basis for tail-anchored membrane protein biogenesis by the
Get3-receptor complex.";
Science 333:758-762(2011).
-!- FUNCTION: Required for the post-translational delivery of tail-
anchored (TA) proteins to the endoplasmic reticulum. Together with
GET2, acts as a membrane receptor for soluble GET3, which
recognizes and selectively binds the transmembrane domain of TA
proteins in the cytosol. The GET complex cooperates with the HDEL
receptor ERD2 to mediate the ATP-dependent retrieval of resident
ER proteins that contain a C-terminal H-D-E-L retention signal
from the Golgi to the ER. Involved in mitochondrial distribution
and morphology. {ECO:0000255|HAMAP-Rule:MF_03113,
ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:16269340,
ECO:0000269|PubMed:18724936, ECO:0000269|PubMed:21719644,
ECO:0000269|PubMed:21835666}.
-!- SUBUNIT: Component of the Golgi to ER traffic (GET) complex, which
is composed of GET1, GET2 and GET3. {ECO:0000255|HAMAP-
Rule:MF_03113, ECO:0000269|PubMed:11805837,
ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:21719644,
ECO:0000269|PubMed:21835666}.
-!- INTERACTION:
P40056:GET2; NbExp=3; IntAct=EBI-23722, EBI-22604;
Q12154:GET3; NbExp=12; IntAct=EBI-23722, EBI-2989;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein. Golgi apparatus membrane; Multi-pass membrane
protein.
-!- MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the WRB/GET1 family. {ECO:0000255|HAMAP-
Rule:MF_03113}.
-----------------------------------------------------------------------
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EMBL; Z72542; CAA96720.1; -; Genomic_DNA.
EMBL; BK006941; DAA08078.1; -; Genomic_DNA.
PIR; S64022; S64022.
RefSeq; NP_011495.1; NM_001180885.1.
PDB; 3B2E; X-ray; 3.00 A; E/F/G/H=21-104.
PDB; 3SJA; X-ray; 3.00 A; C/D/G/H/J=36-93.
PDB; 3SJB; X-ray; 3.30 A; C/D=19-103.
PDB; 3SJC; X-ray; 3.20 A; C/D/G/H=36-93.
PDB; 3VLC; X-ray; 4.50 A; E=21-104.
PDB; 3ZS8; X-ray; 3.00 A; C/D=21-104.
PDBsum; 3B2E; -.
PDBsum; 3SJA; -.
PDBsum; 3SJB; -.
PDBsum; 3SJC; -.
PDBsum; 3VLC; -.
PDBsum; 3ZS8; -.
ProteinModelPortal; P53192; -.
SMR; P53192; -.
BioGrid; 33226; 757.
DIP; DIP-6309N; -.
IntAct; P53192; 3.
MINT; MINT-694680; -.
STRING; 4932.YGL020C; -.
TCDB; 3.A.21.1.1; the c-terminal tail-anchored membrane protein biogenesis/ insertion complex (tamp-b) family.
MaxQB; P53192; -.
PRIDE; P53192; -.
EnsemblFungi; YGL020C; YGL020C; YGL020C.
GeneID; 852864; -.
KEGG; sce:YGL020C; -.
EuPathDB; FungiDB:YGL020C; -.
SGD; S000002988; GET1.
HOGENOM; HOG000000946; -.
InParanoid; P53192; -.
OMA; KWTKNNR; -.
OrthoDB; EOG092C5MDK; -.
BioCyc; YEAST:G3O-30540-MONOMER; -.
PRO; PR:P53192; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043529; C:GET complex; IPI:SGD.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; ISM:SGD.
GO; GO:0043495; F:protein membrane anchor; IGI:SGD.
GO; GO:0045048; P:protein insertion into ER membrane; IGI:SGD.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IDA:SGD.
GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IEA:InterPro.
HAMAP; MF_03113; Get1; 1.
InterPro; IPR027538; Get1_fungi.
InterPro; IPR028945; WRB/Get1.
Pfam; PF04420; CHD5; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Endoplasmic reticulum;
ER-Golgi transport; Golgi apparatus; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 235 Golgi to ER traffic protein 1.
/FTId=PRO_0000414847.
TOPO_DOM 1 1 Lumenal. {ECO:0000255|HAMAP-
Rule:MF_03113}.
TRANSMEM 2 21 Helical. {ECO:0000255|HAMAP-
Rule:MF_03113}.
TOPO_DOM 22 104 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03113}.
TRANSMEM 105 125 Helical. {ECO:0000255|HAMAP-
Rule:MF_03113}.
TOPO_DOM 126 181 Lumenal. {ECO:0000255|HAMAP-
Rule:MF_03113}.
TRANSMEM 182 198 Helical. {ECO:0000255|HAMAP-
Rule:MF_03113}.
TOPO_DOM 199 235 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03113}.
COILED 68 104 {ECO:0000255|HAMAP-Rule:MF_03113}.
HELIX 40 56 {ECO:0000244|PDB:3B2E}.
TURN 61 64 {ECO:0000244|PDB:3B2E}.
HELIX 65 78 {ECO:0000244|PDB:3B2E}.
TURN 79 82 {ECO:0000244|PDB:3B2E}.
HELIX 85 88 {ECO:0000244|PDB:3B2E}.
TURN 89 93 {ECO:0000244|PDB:3B2E}.
TURN 96 98 {ECO:0000244|PDB:3B2E}.
HELIX 100 103 {ECO:0000244|PDB:3SJB}.
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


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