P40056 (GET2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Golgi to ER traffic protein 2

Alternative name(s):
Guided entry of tail-anchored proteins 2
Hydroxyurea resistance protein 2
Required for meiotic nuclear division protein 7

Gene names

Name:	GET2
Synonyms:	HUR2, RMD7
Ordered Locus Names:	YER083C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET1, 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 DNA replication and DNA damage response and also in cell wall function. Ref.3 Ref.5 Ref.8 Ref.9 Ref.13 Ref.15 Ref.16
Subunit structure	Component of the Golgi to ER traffic (GET) complex, which is composed of GET1, GET2 and GET3. Ref.4 Ref.9 Ref.15 Ref.16
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein Ref.7 Ref.9 Ref.15 Ref.16.
Sequence similarities	Belongs to the GET2 family.
Sequence caution	The sequence AAB64638.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	ER-Golgi transport Transport
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein insertion into ER membrane Inferred from genetic interaction Ref.13. Source: SGD retrograde vesicle-mediated transport, Golgi to ER Inferred from direct assay Ref.9. Source: SGD
Cellular_component	GET complex Inferred from genetic interaction Ref.9. Source: SGD Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from sequence model PubMed 12192589Ref.9. Source: SGD
Molecular_function	protein anchor Inferred from genetic interaction Ref.13. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 285

285

Golgi to ER traffic protein 2 HAMAP-Rule MF_03114

PRO_0000097362

Regions

Topological domain

1 – 148

148

Cytoplasmic Potential

Transmembrane

149 – 169

21

Helical; Potential

Topological domain

170 – 196

27

Lumenal Potential

Transmembrane

197 – 216

20

Helical; Potential

Topological domain

217 – 263

47

Cytoplasmic Potential

Transmembrane

264 – 284

21

Helical; Potential

Topological domain

285

1

Lumenal Potential

Amino acid modifications

Modified residue

45

1

Phosphoserine Ref.11

Modified residue

56

1

Phosphothreonine Ref.12 Ref.14

Glycosylation

173

1

N-linked (GlcNAc...) Potential

Glycosylation

196

1

N-linked (GlcNAc...) Potential

Secondary structure

1

.

.

.

.

.

285

Helix Strand Turn

Details...

Helix

6 – 21

16

Turn

22 – 24

3

Helix

25 – 33

9

Sequences

	Sequence		Length	Mass (Da)
	P40056 [UniParc]. Last modified May 16, 2006. Version 2. Checksum: 1667E7C879CFB6EA	FASTA	285	31,493
	10 20 30 40 50 60 MSELTEAEKR RLLRERRQKK FSNGGASSRL NKITGQASSH LNAESPLDAP SAAKTTPPAS 70 80 90 100 110 120 VHSATPDIKE DSNVAPQLDL LKQLAAMQGQ GTGKSTPQDS STPDLLSLLS SMNTGMPSAE 130 140 150 160 170 180 GTPSFGQAAP AAPINQAALD YHDYLLNRLK AWTILVKWVF FLLPYLYLIT RPNSSVWPAY 190 200 210 220 230 240 AFTQSAWFAP LRNPSNFTRI FATFEFLSIS IYYQLLKNVE HKSKIKNLQD TNKLVKLVSL 250 260 270 280 VPEGVIPVAN LKGKLITLLQ YWDLLSMLIT DISFVLIVLG LLTYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Functional discovery via a compendium of expression profiles." Hughes T.R., Marton M.J., Jones A.R., Roberts C.J., Stoughton R., Armour C.D., Bennett H.A., Coffey E., Dai H., He Y.D., Kidd M.J., King A.M., Meyer M.R., Slade D., Lum P.Y., Stepaniants S.B., Shoemaker D.D., Gachotte D. , Chakraburtty K., Simon J., Bard M., Friend S.H. Cell 102:109-126(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry." 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. Nature 415:180-183(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN GET COMPLEX, MASS SPECTROMETRY.
[5]	"Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae." Enyenihi A.H., Saunders W.S. Genetics 163:47-54(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Novel functions of the phosphatidylinositol metabolic pathway discovered by a chemical genomics screen with wortmannin." Zewail A., Xie M.W., Xing Y., Lin L., Zhang P.F., Zou W., Saxe J.P., Huang J. Proc. Natl. Acad. Sci. U.S.A. 100:3345-3350(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[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.
[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 GET3.
[11]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, MASS SPECTROMETRY. Strain: ADR376.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-56, MASS SPECTROMETRY.
[13]	"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.
[14]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-56, MASS SPECTROMETRY.
[15]	"The mechanism of tail-anchored protein insertion into the ER membrane." Wang F., Whynot A., Tung M., Denic V. Mol. Cell 43:738-750(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-38 IN COMPLEX WITH GET3, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.
[16]	"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 (4.6 ANGSTROMS) OF 2-35 IN COMPLEX WITH GET3, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U18839 Genomic DNA. Translation: AAB64638.1. Different initiation.
BK006939 Genomic DNA. Translation: DAA07744.1.

PIR

S50586.

RefSeq

NP_011006.2. NM_001178974.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SJD	X-ray	4.60	D/E	2-35	[»]
3ZS9	X-ray	2.10	C/D	1-38	[»]

ProteinModelPortal

P40056.

SMR

P40056. Positions 4-38.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4508N.

IntAct

P40056. 9 interactions.

MINT

MINT-501836.

STRING

4932.YER083C.

Proteomic databases

PaxDb

P40056.

PeptideAtlas

P40056.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YER083C; YER083C; YER083C.

GeneID

856817.

KEGG

sce:YER083C.

Organism-specific databases

CYGD

YER083c.

SGD

S000000885. GET2.

Phylogenomic databases

eggNOG

NOG38846.

HOGENOM

HOG000066100.

OMA

SISIYYQ.

OrthoDB

EOG451J19.

Gene expression databases

Genevestigator

P40056.

GermOnline

YER083C. Saccharomyces cerevisiae.

Family and domain databases

HAMAP

MF_03114. Get2.

InterPro

IPR014802. GET_GET2.
[Graphical view]

Pfam

PF08690. GET2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P40056.

NextBio

983091.

Entry information

Entry name

GET2_YEAST

Accession

Primary (citable) accession number: P40056
Secondary accession number(s): D3DLZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 16, 2006
Last modified:	April 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program