YEAST:GET3

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	GET3 (ECO:0000255 with HAMAP-Rule:MF_03112) (synonyms: ARR4)
Protein Name(s)	ATPase GET3 (ECO:0000255 with HAMAP-Rule:MF_03112) Arsenical pump-driving ATPase (ECO:0000255 with HAMAP-Rule:MF_03112) Arsenite-stimulated ATPase (ECO:0000255 with HAMAP-Rule:MF_03112) Golgi to ER traffic protein 3 (ECO:0000255 with HAMAP-Rule:MF_03112) Guided entry of tail-anchored proteins 3 (ECO:0000255 with HAMAP-Rule:MF_03112)
External Links
UniProt	Q12154
EMBL	X95644 Z74148 AY693164 BK006938
PIR	S67642
RefSeq	NP_010183.1
PDB	2WOJ 3A36 3A37 3B2E 3H84 3IDQ 3SJA 3SJB 3SJC 3SJD 3VLC 3ZS8 3ZS9 4PWX
PDBsum	2WOJ 3A36 3A37 3B2E 3H84 3IDQ 3SJA 3SJB 3SJC 3SJD 3VLC 3ZS8 3ZS9 4PWX
ProteinModelPortal	Q12154
SMR	Q12154
BioGrid	31962
DIP	DIP-3908N
IntAct	Q12154
MINT	MINT-511570
STRING	4932.YDL100C
TCDB	3.A.21.1.1
MaxQB	Q12154
PaxDb	Q12154
PeptideAtlas	Q12154
EnsemblFungi	[example_ID YDL100C]
GeneID	851458
KEGG	sce:YDL100C
CYGD	YDL100c
SGD	S000002258
eggNOG	COG0003
GeneTree	ENSGT00390000003817
HOGENOM	HOG000197637
InParanoid	Q12154
KO	K01551
OMA	KYIMFGG
OrthoDB	EOG7XDBRV
BioCyc	YEAST:G3O-29503-MONOMER
EvolutionaryTrace	Q12154
NextBio	968732
PRO	PR:Q12154
Proteomes	UP000002311
Genevestigator	Q12154
GO	GO:0043529 GO:0005794 GO:0005524 GO:0016887 GO:0005085 GO:0042802 GO:0046872 GO:0051082 GO:0006200 GO:1990507 GO:0000750 GO:0043547 GO:0006620 GO:0045048 GO:0046685 GO:0009408 GO:0010038 GO:0006890
Gene3D	3.40.50.300
HAMAP	MF_03112
InterPro	IPR025723 IPR016300 IPR027542 IPR027417
PANTHER	PTHR10803
Pfam	PF02374
SUPFAM	SSF52540
TIGRFAMs	TIGR00345

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005524	ATP binding	PMID:22547793^[1]	ECO:0000315			F		Figures 1-6 provide the necessary information	complete CACAO 10595
	GO:1990507	ATP-independent chaperone mediated protein folding	PMID:23203805^[2]	ECO:0000314			P		Figure 7: Influence of Get3 on the aggregation behavior of citrate synthase (CS)."It is of note that addition of either 2 mM ATP or ADP reproducibly reduced the holdase activity of Get3, implying that Get3 acts most efficiently on these clients in the absence of nucleotides (Fig. 7D)"	complete CACAO 11722
part_of	GO:0005829	cytosol	PMID:26928762^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:14562095^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:25242142^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0034599)	Seeded From UniProt	complete
involved_in	GO:1990507	ATP-independent chaperone mediated protein folding	PMID:25242142^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:0034599)	Seeded From UniProt	complete
involved_in	GO:0045048	protein insertion into ER membrane	PMID:18724936^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043529	GET complex	PMID:16269340^[7]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002988	C		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:12680698^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010038	response to metal ion	PMID:12680698^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:12680698^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006890	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	PMID:16269340^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000136	P		Seeded From UniProt	complete
involved_in	GO:0006890	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	PMID:16269340^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006890	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	PMID:16269340^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006620	posttranslational protein targeting to endoplasmic reticulum membrane	PMID:20850366^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005085	guanyl-nucleotide exchange factor activity	PMID:18261907^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000750	pheromone-dependent signal transduction involved in conjugation with cellular fusion	PMID:18261907^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071816	tail-anchored membrane protein insertion into ER membrane	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000085952 UniProtKB:A8IXB8	P		Seeded From UniProt	complete
part_of	GO:0043529	GET complex	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000085952 SGD:S000002258	C		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002246741 SGD:S000002258 WB:WBGene00014025	F		Seeded From UniProt	complete
involved_in	GO:0006620	posttranslational protein targeting to endoplasmic reticulum membrane	PMID:21873635^[11]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000085952 SGD:S000002258	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25745174^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12154	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24727835^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12154	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22124326^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12154	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19706470^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12154	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19675567^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12154	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16260785^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12154	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016300 InterPro:IPR027542	F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016300 InterPro:IPR027542	F		Seeded From UniProt	complete
part_of	GO:0043529	GET complex	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000106709	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000106709	F		Seeded From UniProt	complete
involved_in	GO:0045048	protein insertion into ER membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000106709	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256 UniProtKB-SubCell:SL-0095	C		Seeded From UniProt	complete
involved_in	GO:0046685	response to arsenic-containing substance	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0059	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
involved_in	GO:0016192	vesicle-mediated transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0931	P		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333 UniProtKB-SubCell:SL-0132	C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Wereszczynski, J & McCammon, JA (2012) Nucleotide-dependent mechanism of Get3 as elucidated from free energy calculations. Proc. Natl. Acad. Sci. U.S.A. 109 7759-64 PubMed GONUTS page
↑ Powis, K et al. (2013) Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked. J. Cell. Sci. 126 473-83 PubMed GONUTS page
↑ Yofe, I et al. (2016) One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Nat. Methods 13 371-378 PubMed GONUTS page
↑ Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
↑ ^5.0 ^5.1 Voth, W et al. (2014) The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions. Mol. Cell 56 116-27 PubMed GONUTS page
↑ Schuldiner, M et al. (2008) The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell 134 634-45 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Schuldiner, M et al. (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123 507-19 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Shen, J et al. (2003) The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance. Biometals 16 369-78 PubMed GONUTS page
↑ Wang, F et al. (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 40 159-71 PubMed GONUTS page
↑ ^10.0 ^10.1 Lee, MJ & Dohlman, HG (2008) Coactivation of G protein signaling by cell-surface receptors and an intracellular exchange factor. Curr. Biol. 18 211-5 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Mateja, A et al. (2015) Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo. Science 347 1152-5 PubMed GONUTS page
↑ Gristick, HB et al. (2014) Crystal structure of ATP-bound Get3-Get4-Get5 complex reveals regulation of Get3 by Get4. Nat. Struct. Mol. Biol. 21 437-42 PubMed GONUTS page
↑ Suloway, CJ et al. (2012) Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue. EMBO J. 31 707-19 PubMed GONUTS page
↑ Suloway, CJ et al. (2009) Model for eukaryotic tail-anchored protein binding based on the structure of Get3. Proc. Natl. Acad. Sci. U.S.A. 106 14849-54 PubMed GONUTS page
↑ Mateja, A et al. (2009) The structural basis of tail-anchored membrane protein recognition by Get3. Nature 461 361-6 PubMed GONUTS page
↑ Metz, J et al. (2006) The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. J. Biol. Chem. 281 410-7 PubMed GONUTS page

[PMID:22547793-1] Wereszczynski, J & McCammon, JA (2012) Nucleotide-dependent mechanism of Get3 as elucidated from free energy calculations. Proc. Natl. Acad. Sci. U.S.A. 109 7759-64 PubMed GONUTS page

[PMID:23203805-2] Powis, K et al. (2013) Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked. J. Cell. Sci. 126 473-83 PubMed GONUTS page

[PMID:26928762-3] Yofe, I et al. (2016) One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Nat. Methods 13 371-378 PubMed GONUTS page

[PMID:14562095-4] Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page

[PMID:25242142-5] 5.0 ^5.1 Voth, W et al. (2014) The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions. Mol. Cell 56 116-27 PubMed GONUTS page

[PMID:18724936-6] Schuldiner, M et al. (2008) The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell 134 634-45 PubMed GONUTS page

[PMID:16269340-7] 7.0 ^7.1 ^7.2 ^7.3 Schuldiner, M et al. (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123 507-19 PubMed GONUTS page

[PMID:12680698-8] 8.0 ^8.1 ^8.2 Shen, J et al. (2003) The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance. Biometals 16 369-78 PubMed GONUTS page

[PMID:20850366-9] Wang, F et al. (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 40 159-71 PubMed GONUTS page

[PMID:18261907-10] 10.0 ^10.1 Lee, MJ & Dohlman, HG (2008) Coactivation of G protein signaling by cell-surface receptors and an intracellular exchange factor. Curr. Biol. 18 211-5 PubMed GONUTS page

[PMID:21873635-11] 11.0 ^11.1 ^11.2 ^11.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:25745174-12] Mateja, A et al. (2015) Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo. Science 347 1152-5 PubMed GONUTS page

[PMID:24727835-13] Gristick, HB et al. (2014) Crystal structure of ATP-bound Get3-Get4-Get5 complex reveals regulation of Get3 by Get4. Nat. Struct. Mol. Biol. 21 437-42 PubMed GONUTS page

[PMID:22124326-14] Suloway, CJ et al. (2012) Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue. EMBO J. 31 707-19 PubMed GONUTS page

[PMID:19706470-15] Suloway, CJ et al. (2009) Model for eukaryotic tail-anchored protein binding based on the structure of Get3. Proc. Natl. Acad. Sci. U.S.A. 106 14849-54 PubMed GONUTS page

[PMID:19675567-16] Mateja, A et al. (2009) The structural basis of tail-anchored membrane protein recognition by Get3. Nature 461 361-6 PubMed GONUTS page

[PMID:16260785-17] Metz, J et al. (2006) The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. J. Biol. Chem. 281 410-7 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

YEAST:GET3

Contents

Annotations

Notes

References

a

c

d

e

f

g

h

i

m

n

o

p

r

s

t

u

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools