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Protein

ATPase GET3

Gene

GET3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1 and GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. 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 low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance.UniRule annotation5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei57 – 571
Binding sitei245 – 2451ATP
Binding sitei272 – 2721ATP
Metal bindingi285 – 2851Zinc; shared with dimeric partnerUniRule annotation1 Publication
Metal bindingi288 – 2881Zinc; shared with dimeric partnerUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338ATP
Nucleotide bindingi315 – 3228ATP

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-HAMAP
  • guanyl-nucleotide exchange factor activity Source: SGD
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • unfolded protein binding Source: SGD

GO - Biological processi

  • ATP-independent chaperone mediated protein folding Source: SGD
  • pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
  • positive regulation of GTPase activity Source: GOC
  • posttranslational protein targeting to membrane Source: SGD
  • protein insertion into ER membrane Source: SGD
  • response to arsenic-containing substance Source: UniProtKB-KW
  • response to heat Source: SGD
  • response to metal ion Source: SGD
  • retrograde vesicle-mediated transport, Golgi to ER Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arsenical resistance, ER-Golgi transport, Transport

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29503-MONOMER.
ReactomeiR-SCE-381038. XBP1(S) activates chaperone genes.

Protein family/group databases

TCDBi3.A.21.1.1. the c-terminal tail-anchored membrane protein biogenesis/ insertion complex (tamp-b) family.

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase GET3UniRule annotation (EC:3.6.-.-UniRule annotation)
Alternative name(s):
Arsenical pump-driving ATPaseUniRule annotation
Arsenite-stimulated ATPaseUniRule annotation
Golgi to ER traffic protein 3UniRule annotation
Guided entry of tail-anchored proteins 3UniRule annotation
Gene namesi
Name:GET3UniRule annotation
Synonyms:ARR4
Ordered Locus Names:YDL100C
ORF Names:D2371
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL100C.
SGDiS000002258. GET3.

Subcellular locationi

GO - Cellular componenti

  • GET complex Source: SGD
  • Golgi apparatus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301G → R: Abolishes ATPase activity, leading to secretion of resident ER proteins. 2 Publications
Mutagenesisi57 – 571D → N: Abolishes ATP hydrolysis. 1 Publication
Mutagenesisi285 – 2851C → S: Prevents dimerization; when associated with S-288. 1 Publication
Mutagenesisi288 – 2881C → S: Prevents dimerization; when associated with S-285. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354ATPase GET3PRO_0000152256Add
BLAST

Proteomic databases

MaxQBiQ12154.
PeptideAtlasiQ12154.

Interactioni

Subunit structurei

Homodimer. Component of the Golgi to ER traffic (GET) complex, which is composed of GET1, GET2 and GET3. Interacts with the chloride channel protein GEF1.UniRule annotation10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-2989,EBI-2989
GEF1P370206EBI-2989,EBI-7552
GET1P531923EBI-2989,EBI-23722
GET4Q121254EBI-2989,EBI-36940
MDY2Q122853EBI-2989,EBI-34904

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi31962. 259 interactions.
DIPiDIP-3908N.
IntActiQ12154. 48 interactions.
MINTiMINT-511570.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Helixi10 – 134Combined sources
Beta strandi20 – 267Combined sources
Beta strandi27 – 304Combined sources
Helixi31 – 4515Combined sources
Beta strandi47 – 493Combined sources
Beta strandi51 – 555Combined sources
Beta strandi57 – 593Combined sources
Helixi62 – 665Combined sources
Beta strandi81 – 877Combined sources
Helixi90 – 989Combined sources
Turni102 – 1043Combined sources
Beta strandi114 – 1163Combined sources
Helixi117 – 1204Combined sources
Helixi122 – 1243Combined sources
Helixi125 – 1306Combined sources
Helixi136 – 15318Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi161 – 1666Combined sources
Helixi170 – 1778Combined sources
Helixi179 – 18810Combined sources
Helixi191 – 1944Combined sources
Beta strandi195 – 1973Combined sources
Helixi200 – 2056Combined sources
Turni206 – 2083Combined sources
Helixi213 – 23018Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 24510Combined sources
Helixi246 – 26116Combined sources
Beta strandi268 – 2747Combined sources
Turni277 – 2815Combined sources
Helixi286 – 30520Combined sources
Turni306 – 3083Combined sources
Beta strandi309 – 3157Combined sources
Helixi323 – 33513Combined sources
Helixi340 – 3434Combined sources
Helixi344 – 3507Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WOJX-ray1.99A/B/C/D1-354[»]
3A36X-ray2.80A/B1-354[»]
3A37X-ray3.00A/B1-354[»]
3B2EX-ray3.00A/B/C/D1-354[»]
3H84X-ray2.30A/B1-354[»]
3IDQX-ray3.70A1-354[»]
3SJAX-ray3.00A/B/E/F/I1-354[»]
3SJBX-ray3.30A/B1-354[»]
3SJCX-ray3.20A/B/E/F1-354[»]
3SJDX-ray4.60A/B/C1-354[»]
3VLCX-ray4.50A1-354[»]
3ZS8X-ray3.00A/B1-354[»]
3ZS9X-ray2.10A/B1-354[»]
4PWXX-ray5.40A/B2-354[»]
4XTRX-ray2.05A/B1-354[»]
4XVUX-ray2.35A/B/G/H1-354[»]
4XWOX-ray2.75A/B/G/H/M/N/S/T1-354[»]
5BW8X-ray2.80A/B2-354[»]
5BWKX-ray6.00A/B/C/D/M/N/O/P2-354[»]
ProteinModelPortaliQ12154.
SMRiQ12154. Positions 4-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12154.

Family & Domainsi

Sequence similaritiesi

Belongs to the arsA ATPase family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000003817.
HOGENOMiHOG000197637.
InParanoidiQ12154.
KOiK01551.
OMAiYEIDTHN.
OrthoDBiEOG7XDBRV.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03112. Asna1_Get3.
InterProiIPR025723. Anion-transp_ATPase-like_dom.
IPR016300. ATPase_ArsA/GET3.
IPR027542. ATPase_ArsA/GET3_euk.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10803. PTHR10803. 1 hit.
PfamiPF02374. ArsA_ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00345. GET3_arsA_TRC40. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLTVEPNLH SLITSTTHKW IFVGGKGGVG KTTSSCSIAI QMALSQPNKQ
60 70 80 90 100
FLLISTDPAH NLSDAFGEKF GKDARKVTGM NNLSCMEIDP SAALKDMNDM
110 120 130 140 150
AVSRANNNGS DGQGDDLGSL LQGGALADLT GSIPGIDEAL SFMEVMKHIK
160 170 180 190 200
RQEQGEGETF DTVIFDTAPT GHTLRFLQLP NTLSKLLEKF GEITNKLGPM
210 220 230 240 250
LNSFMGAGNV DISGKLNELK ANVETIRQQF TDPDLTTFVC VCISEFLSLY
260 270 280 290 300
ETERLIQELI SYDMDVNSII VNQLLFAEND QEHNCKRCQA RWKMQKKYLD
310 320 330 340 350
QIDELYEDFH VVKMPLCAGE IRGLNNLTKF SQFLNKEYNP ITDGKVIYEL

EDKE
Length:354
Mass (Da):39,354
Last modified:November 1, 1996 - v1
Checksum:iF795C359B5A4A461
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431A → T in AAT93183 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95644 Genomic DNA. Translation: CAA64913.1.
Z74148 Genomic DNA. Translation: CAA98667.1.
AY693164 Genomic DNA. Translation: AAT93183.1.
BK006938 Genomic DNA. Translation: DAA11760.1.
PIRiS67642.
RefSeqiNP_010183.1. NM_001180159.1.

Genome annotation databases

EnsemblFungiiYDL100C; YDL100C; YDL100C.
GeneIDi851458.
KEGGisce:YDL100C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95644 Genomic DNA. Translation: CAA64913.1.
Z74148 Genomic DNA. Translation: CAA98667.1.
AY693164 Genomic DNA. Translation: AAT93183.1.
BK006938 Genomic DNA. Translation: DAA11760.1.
PIRiS67642.
RefSeqiNP_010183.1. NM_001180159.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WOJX-ray1.99A/B/C/D1-354[»]
3A36X-ray2.80A/B1-354[»]
3A37X-ray3.00A/B1-354[»]
3B2EX-ray3.00A/B/C/D1-354[»]
3H84X-ray2.30A/B1-354[»]
3IDQX-ray3.70A1-354[»]
3SJAX-ray3.00A/B/E/F/I1-354[»]
3SJBX-ray3.30A/B1-354[»]
3SJCX-ray3.20A/B/E/F1-354[»]
3SJDX-ray4.60A/B/C1-354[»]
3VLCX-ray4.50A1-354[»]
3ZS8X-ray3.00A/B1-354[»]
3ZS9X-ray2.10A/B1-354[»]
4PWXX-ray5.40A/B2-354[»]
4XTRX-ray2.05A/B1-354[»]
4XVUX-ray2.35A/B/G/H1-354[»]
4XWOX-ray2.75A/B/G/H/M/N/S/T1-354[»]
5BW8X-ray2.80A/B2-354[»]
5BWKX-ray6.00A/B/C/D/M/N/O/P2-354[»]
ProteinModelPortaliQ12154.
SMRiQ12154. Positions 4-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31962. 259 interactions.
DIPiDIP-3908N.
IntActiQ12154. 48 interactions.
MINTiMINT-511570.

Protein family/group databases

TCDBi3.A.21.1.1. the c-terminal tail-anchored membrane protein biogenesis/ insertion complex (tamp-b) family.

Proteomic databases

MaxQBiQ12154.
PeptideAtlasiQ12154.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL100C; YDL100C; YDL100C.
GeneIDi851458.
KEGGisce:YDL100C.

Organism-specific databases

EuPathDBiFungiDB:YDL100C.
SGDiS000002258. GET3.

Phylogenomic databases

GeneTreeiENSGT00390000003817.
HOGENOMiHOG000197637.
InParanoidiQ12154.
KOiK01551.
OMAiYEIDTHN.
OrthoDBiEOG7XDBRV.

Enzyme and pathway databases

BioCyciYEAST:G3O-29503-MONOMER.
ReactomeiR-SCE-381038. XBP1(S) activates chaperone genes.

Miscellaneous databases

EvolutionaryTraceiQ12154.
NextBioi968732.
PROiQ12154.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03112. Asna1_Get3.
InterProiIPR025723. Anion-transp_ATPase-like_dom.
IPR016300. ATPase_ArsA/GET3.
IPR027542. ATPase_ArsA/GET3_euk.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10803. PTHR10803. 1 hit.
PfamiPF02374. ArsA_ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00345. GET3_arsA_TRC40. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames."
    Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G., Jimenez A., Remacha M.A.
    Yeast 12:1377-1384(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: IDENTIFICATION IN GET COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance."
    Shen J., Hsu C.-M., Kang B.-K., Rosen B.P., Bhattacharjee H.
    BioMetals 16:369-378(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-30, SUBUNIT, SUBCELLULAR LOCATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile."
    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.
    Cell 123:507-519(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN GET COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH GET1.
  10. "The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae."
    Auld K.L., Hitchcock A.L., Doherty H.K., Frietze S., Huang L.S., Silver P.A.
    Genetics 174:215-227(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GET1 AND GET2, SUBCELLULAR LOCATION.
  11. "The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol."
    Metz J., Waechter A., Schmidt B., Bujnicki J.M., Schwappach B.
    J. Biol. Chem. 281:410-417(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GEF1, SUBUNIT.
  12. "The GET complex mediates insertion of tail-anchored proteins into the ER membrane."
    Schuldiner M., Metz J., Schmid V., Denic V., Rakwalska M., Schmitt H.D., Schwappach B., Weissman J.S.
    Cell 134:634-645(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "The structural basis of tail-anchored membrane protein recognition by Get3."
    Mateja A., Szlachcic A., Downing M.E., Dobosz M., Mariappan M., Hegde R.S., Keenan R.J.
    Nature 461:361-366(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH ADP AND ZINC, SUBUNIT, MUTAGENESIS OF ASP-57; CYS-285 AND CYS-288.
  14. "The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion."
    Hu J., Li J., Qian X., Denic V., Sha B.
    PLoS ONE 4:E8061-E8061(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  15. "Model for eukaryotic tail-anchored protein binding based on the structure of Get3."
    Suloway C.J.M., Chartron J.W., Zaslaver M., Clemons W.M. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 106:14849-14854(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS), SUBUNIT, MUTAGENESIS OF GLY-30.
  16. "Structural insight into the membrane insertion of tail-anchored proteins by Get3."
    Yamagata A., Mimura H., Sato Y., Yamashita M., Yoshikawa A., Fukai S.
    Genes Cells 15:29-41(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ADP.
  17. "The mechanism of membrane-associated steps in tail-anchored protein insertion."
    Mariappan M., Mateja A., Dobosz M., Bove E., Hegde R.S., Keenan R.J.
    Nature 477:61-66(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GET2, FUNCTION, SUBUNIT.
  18. "Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex."
    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.
    Science 333:758-762(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH GET1, FUNCTION, SUBUNIT.
  19. "Get1 stabilizes an open dimer conformation of get3 ATPase by binding two distinct interfaces."
    Kubota K., Yamagata A., Sato Y., Goto-Ito S., Fukai S.
    J. Mol. Biol. 422:366-375(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiGET3_YEAST
AccessioniPrimary (citable) accession number: Q12154
Secondary accession number(s): D6VRQ0, Q6B1B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 17300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.