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P39524 (ATC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable phospholipid-transporting ATPase DRS2

EC=3.6.3.1
Gene names
Name:DRS2
Ordered Locus Names:YAL026C
ORF Names:FUN38
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1355 AA.
Sequence statusComplete.
Protein existenceEvidence 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 apparatustrans-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]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13551355Probable phospholipid-transporting ATPase DRS2
PRO_0000046233

Regions

Topological domain1 – 221221Cytoplasmic Potential
Transmembrane222 – 24221Helical; Potential
Topological domain243 – 2464Lumenal Potential
Transmembrane247 – 26721Helical; Potential
Topological domain268 – 449182Cytoplasmic Potential
Transmembrane450 – 47021Helical; Potential
Topological domain471 – 49020Lumenal Potential
Transmembrane491 – 51121Helical; Potential
Topological domain512 – 1012501Cytoplasmic Potential
Transmembrane1013 – 103321Helical; Potential
Topological domain1034 – 104310Lumenal Potential
Transmembrane1044 – 106421Helical; Potential
Topological domain1065 – 109430Cytoplasmic Potential
Transmembrane1095 – 111521Helical; Potential
Topological domain1116 – 113116Lumenal Potential
Transmembrane1132 – 115221Helical; Potential
Topological domain1153 – 11619Cytoplasmic Potential
Transmembrane1162 – 118221Helical; Potential
Topological domain1183 – 120220Lumenal Potential
Transmembrane1203 – 122321Helical; Potential
Topological domain1224 – 1355132Cytoplasmic Potential

Sites

Active site56014-aspartylphosphate intermediate By similarity

Amino acid modifications

Modified residue1021Phosphoserine Ref.10 Ref.11

Experimental info

Sequence conflict45 – 462AN → GY in AAA16891. Ref.1
Sequence conflict45 – 462AN → GY in AAC05006. Ref.2
Sequence conflict4501A → R in AAA16891. Ref.1
Sequence conflict4501A → R in AAC05006. Ref.2
Sequence conflict6741P → G in AAA16891. Ref.1
Sequence conflict6741P → G in AAC05006. Ref.2
Sequence conflict891 – 8922NT → KS in AAA16891. Ref.1
Sequence conflict891 – 8922NT → KS in AAC05006. Ref.2
Sequence conflict953 – 9542GD → AS in AAA16891. Ref.1
Sequence conflict953 – 9542GD → AS in AAC05006. Ref.2
Sequence conflict9871V → L in AAA16891. Ref.1
Sequence conflict9871V → L in AAC05006. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P39524 [UniParc].

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

FASTA1,355153,765
        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' 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 204508 / S288c.
[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]"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.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS51995.
RefSeqNP_009376.2. NM_001178171.2.

3D structure databases

ProteinModelPortalP39524.
SMRP39524. Positions 216-1019.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31740. 189 interactions.
DIPDIP-2216N.
IntActP39524. 10 interactions.
MINTMINT-520976.
STRING4932.YAL026C.

Protein family/group databases

TCDB3.A.3.8.11. the p-type atpase (p-atpase) superfamily.
3.A.3.8.2. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbP39524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL026C; YAL026C; YAL026C.
GeneID851207.
KEGGsce:YAL026C.

Organism-specific databases

CYGDYAL026c.
SGDS000000024. DRS2.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00740000115297.
HOGENOMHOG000202528.
KOK14802.
OMAPCSQQNM.
OrthoDBEOG7FR7QR.

Enzyme and pathway databases

BioCycYEAST:G3O-28837-MONOMER.

Gene expression databases

GenevestigatorP39524.

Family and domain databases

Gene3D2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR023299. 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]
PANTHERPTHR24092. PTHR24092. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968076.
PROP39524.

Entry information

Entry nameATC3_YEAST
AccessionPrimary (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: March 19, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

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

Yeast

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

SIMILARITY comments

Index of protein domains and families