Probable phospholipid-transporting ATPase DRS2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P39524 (ATC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable phospholipid-transporting ATPase DRS2
EC=3.6.3.1

Gene names

Name:	DRS2
Ordered Locus Names:	YAL026C
ORF Names:	FUN38

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1355 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids Potential. Seems to be involved in ribosome assembly.
Catalytic activity	ATP + H₂O + phospholipid(side 1) = ADP + phosphate + phospholipid(side 2).
Subunit structure	Interacts with CDC50. Ref.7
Subcellular location	Golgi apparatus › trans-Golgi network membrane; Multi-pass membrane protein Ref.4 Ref.5.
Miscellaneous	Present with 606 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from genetic interaction PubMed 12631737 PubMed 16195350. Source: SGD intracellular protein transport Inferred from genetic interaction PubMed 12221123. Source: SGD phospholipid translocation Inferred from mutant phenotype PubMed 15249668 PubMed 16452632. Source: SGD post-Golgi vesicle-mediated transport Inferred from mutant phenotype PubMed 10601336. Source: SGD ribosomal small subunit assembly Inferred from mutant phenotype Ref.1. Source: SGD
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD trans-Golgi network Inferred from direct assay PubMed 10601336 PubMed 12221123 Ref.7. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cation-transporting ATPase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro phospholipid-translocating ATPase activity Inferred from mutant phenotype PubMed 15249668 PubMed 16452632 PubMed 8633245. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1355

1355

Probable phospholipid-transporting ATPase DRS2

PRO_0000046233

Regions

Topological domain

1 – 221

221

Cytoplasmic Potential

Transmembrane

222 – 242

Helical; Potential

Topological domain

243 – 246

Lumenal Potential

Transmembrane

247 – 267

Helical; Potential

Topological domain

268 – 449

182

Cytoplasmic Potential

Transmembrane

450 – 470

Helical; Potential

Topological domain

471 – 490

Lumenal Potential

Transmembrane

491 – 511

Helical; Potential

Topological domain

512 – 1012

501

Cytoplasmic Potential

Transmembrane

1013 – 1033

Helical; Potential

Topological domain

1034 – 1043

Lumenal Potential

Transmembrane

1044 – 1064

Helical; Potential

Topological domain

1065 – 1094

Cytoplasmic Potential

Transmembrane

1095 – 1115

Helical; Potential

Topological domain

1116 – 1131

Lumenal Potential

Transmembrane

1132 – 1152

Helical; Potential

Topological domain

1153 – 1161

Cytoplasmic Potential

Transmembrane

1162 – 1182

Helical; Potential

Topological domain

1183 – 1202

Lumenal Potential

Transmembrane

1203 – 1223

Helical; Potential

Topological domain

1224 – 1355

132

Cytoplasmic Potential

Sites

Active site

560

4-aspartylphosphate intermediate By similarity

Amino acid modifications

Modified residue

102

Phosphoserine Ref.10

Modified residue

1347

Phosphoserine Ref.10

Modified residue

1352

Phosphoserine Ref.8

Experimental info

Sequence conflict

45 – 46

AN → GY in AAA16891. Ref.1

Sequence conflict

45 – 46

AN → GY in AAC05006. Ref.2

Sequence conflict

450

A → R in AAA16891. Ref.1

Sequence conflict

450

A → R in AAC05006. Ref.2

Sequence conflict

674

P → G in AAA16891. Ref.1

Sequence conflict

674

P → G in AAC05006. Ref.2

Sequence conflict

891 – 892

NT → KS in AAA16891. Ref.1

Sequence conflict

891 – 892

NT → KS in AAC05006. Ref.2

Sequence conflict

953 – 954

GD → AS in AAA16891. Ref.1

Sequence conflict

953 – 954

GD → AS in AAC05006. Ref.2

Sequence conflict

987

V → L in AAA16891. Ref.1

Sequence conflict

987

V → L in AAC05006. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P39524 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 5745B92901F8E1AE
Show »

FASTA

1,355

153,765

        10         20         30         40         50         60 
MNDDRETPPK RKPGEDDTLF DIDFLDDTTS HSGSRSKVTN SHANANYIPP SHVLPEETID 

        70         80         90        100        110        120 
LDADDDNIEN DVHENLFMSN NHDDQTSWNA NRFDSDAYQP QSLRAVKPPG LFARFGNGLK 

       130        140        150        160        170        180 
NAFTFKRKKG PESFEMNHYN AVTNNELDDN YLDSRNKFNI KILFNRYILR KNVGDAEGNG 

       190        200        210        220        230        240 
EPRVIHINDS LANSSFGYSD NHISTTKYNF ATFLPKFLFQ EFSKYANLFF LCTSAIQQVP 

       250        260        270        280        290        300 
HVSPTNRYTT IGTLLVVLIV SAMKECIEDI KRANSDKELN NSTAEIFSEA HDDFVEKRWI 

       310        320        330        340        350        360 
DIRVGDIIRV KSEEPIPADT IILSSSEPEG LCYIETANLD GETNLKIKQS RVETAKFIDV 

       370        380        390        400        410        420 
KTLKNMNGKV VSEQPNSSLY TYEGTMTLND RQIPLSPDQM ILRGATLRNT AWIFGLVIFT 

       430        440        450        460        470        480 
GHETKLLRNA TATPIKRTAV EKIINRQIIA LFTVLIVLIL ISSIGNVIMS TADAKHLSYL 

       490        500        510        520        530        540 
YLEGTNKAGL FFKDFLTFWI LFSNLVPISL FVTVELIKYY QAFMIGSDLD LYYEKTDTPT 

       550        560        570        580        590        600 
VVRTSSLVEE LGQIEYIFSD KTGTLTRNIM EFKSCSIAGH CYIDKIPEDK TATVEDGIEV 

       610        620        630        640        650        660 
GYRKFDDLKK KLNDPSDEDS PIINDFLTLL ATCHTVIPEF QSDGSIKYQA ASPDEGALVQ 

       670        680        690        700        710        720 
GGADLGYKFI IRKPNSVTVL LEETGEEKEY QLLNICEFNS TRKRMSAIFR FPDGSIKLFC 

       730        740        750        760        770        780 
KGADTVILER LDDEANQYVE ATMRHLEDYA SEGLRTLCLA MRDISEGEYE EWNSIYNEAA 

       790        800        810        820        830        840 
TTLDNRAEKL DEAANLIEKN LILIGATAIE DKLQDGVPET IHTLQEAGIK IWVLTGDRQE 

       850        860        870        880        890        900 
TAINIGMSCR LLSEDMNLLI INEETRDDTE RNLLEKINAL NEHQLSTHDM NTLALVIDGK 

       910        920        930        940        950        960 
SLGFALEPEL EDYLLTVAKL CKAVICCRVS PLQKALVVKM VKRKSSSLLL AIGDGANDVS 

       970        980        990       1000       1010       1020 
MIQAAHVGVG ISGMEGMQAA RSADIAVGQF KFLKKLLLVH GSWSYQRISV AILYSFYKNT 

      1030       1040       1050       1060       1070       1080 
ALYMTQFWYV FANAFSGQSI MESWTMSFYN LFFTVWPPFV IGVFDQFVSS RLLERYPQLY 

      1090       1100       1110       1120       1130       1140 
KLGQKGQFFS VYIFWGWIIN GFFHSAIVFI GTILIYRYGF ALNMHGELAD HWSWGVTVYT 

      1150       1160       1170       1180       1190       1200 
TSVIIVLGKA ALVTNQWTKF TLIAIPGSLL FWLIFFPIYA SIFPHANISR EYYGVVKHTY 

      1210       1220       1230       1240       1250       1260 
GSGVFWLTLI VLPIFALVRD FLWKYYKRMY EPETYHVIQE MQKYNISDSR PHVQQFQNAI 

      1270       1280       1290       1300       1310       1320 
RKVRQVQRMK KQRGFAFSQA EEGGQEKIVR MYDTTQKRGK YGELQDASAN PFNDNNGLGS 

      1330       1340       1350 
NDFESAEPFI ENPFADGNQN SNRFSSSRDD ISFDI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae." Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr. Mol. Cell. Biol. 13:7901-7912(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 45-46; 450; 674; 891-892; 953-954 AND 987. Strain: ATCC 204508 / S288c.
[4]	"Drs2p-dependent formation of exocytic clathrin-coated vesicles in vivo." Gall W.E., Geething N.C., Hua Z., Ingram M.F., Liu K., Chen S.I., Graham T.R. Curr. Biol. 12:1623-1627(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
[5]	"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].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae." Saito K., Fujimura-Kamada K., Furuta N., Kato U., Umeda M., Tanaka K. Mol. Biol. Cell 15:3418-3432(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDC50.
[8]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1352, MASS SPECTROMETRY. Strain: YAL6B.
[9]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
[10]	"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 SER-102 AND SER-1347, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L01795 Unassigned RNA. Translation: AAA16891.1. U12980 Genomic DNA. Translation: AAC05006.1. BK006935 Genomic DNA. Translation: DAA06962.2.
PIR	S51995.
RefSeq	NP_009376.2. NM_001178171.2.
3D structure databases
ProteinModelPortal	P39524.
SMR	P39524. Positions 216-1019.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2216N.
IntAct	P39524. 10 interactions.
MINT	MINT-520976.
STRING	4932.YAL026C.
Protein family/group databases
TCDB	3.A.3.8.11. P-type ATPase (P-ATPase) superfamily. 3.A.3.8.2. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PaxDb	P39524.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YAL026C; YAL026C; YAL026C.
GeneID	851207.
KEGG	sce:YAL026C.
Organism-specific databases
CYGD	YAL026c.
SGD	S000000024. DRS2.
Phylogenomic databases
eggNOG	COG0474.
GeneTree	ENSGT00690000102080.
HOGENOM	HOG000202528.
KO	K14802.
OMA	NIXATRE.
OrthoDB	EOG4STWCQ.
Gene expression databases
Genevestigator	P39524.
GermOnline	YAL026C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.70.150.10. 2 hits. 3.40.1110.10. 1 hit. 3.40.50.1000. 2 hits.
InterPro	IPR023299. ATPase_P-typ_cyto_domN. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transp. IPR008250. ATPase_P-typ_transduc_dom_A. IPR001757. Cation_transp_P_typ_ATPase. IPR023214. HAD-like_dom. [Graphical view]
PANTHER	PTHR24092. PTHR24092. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 1 hit.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968076.

Entry information

Entry name

ATC3_YEAST

Accession

Primary (citable) accession number: P39524
Secondary accession number(s): D6VPJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents