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P39524

- ATC3_YEAST

UniProt

P39524 - ATC3_YEAST

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Protein

Probable phospholipid-transporting ATPase DRS2

Gene

DRS2

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

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Seems to be involved in ribosome assembly.Curated

Catalytic activityi

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei560 – 56014-aspartylphosphate intermediateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cation-transporting ATPase activity Source: InterPro
  3. magnesium ion binding Source: InterPro
  4. phospholipid-translocating ATPase activity Source: SGD

GO - Biological processi

  1. endocytic recycling Source: SGD
  2. endocytosis Source: SGD
  3. intracellular protein transport Source: SGD
  4. phospholipid translocation Source: SGD
  5. post-Golgi vesicle-mediated transport Source: SGD
  6. ribosomal small subunit assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28837-MONOMER.
ReactomeiREACT_96459. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.8.2. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable phospholipid-transporting ATPase DRS2 (EC:3.6.3.1)
Gene namesi
Name:DRS2
Ordered Locus Names:YAL026C
ORF Names:FUN38
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome I

Organism-specific databases

CYGDiYAL026c.
SGDiS000000024. DRS2.

Subcellular locationi

Golgi apparatustrans-Golgi network membrane 2 Publications; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 221221CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei222 – 24221HelicalSequence AnalysisAdd
BLAST
Topological domaini243 – 2464LumenalSequence Analysis
Transmembranei247 – 26721HelicalSequence AnalysisAdd
BLAST
Topological domaini268 – 449182CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei450 – 47021HelicalSequence AnalysisAdd
BLAST
Topological domaini471 – 49020LumenalSequence AnalysisAdd
BLAST
Transmembranei491 – 51121HelicalSequence AnalysisAdd
BLAST
Topological domaini512 – 1012501CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1013 – 103321HelicalSequence AnalysisAdd
BLAST
Topological domaini1034 – 104310LumenalSequence Analysis
Transmembranei1044 – 106421HelicalSequence AnalysisAdd
BLAST
Topological domaini1065 – 109430CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1095 – 111521HelicalSequence AnalysisAdd
BLAST
Topological domaini1116 – 113116LumenalSequence AnalysisAdd
BLAST
Transmembranei1132 – 115221HelicalSequence AnalysisAdd
BLAST
Topological domaini1153 – 11619CytoplasmicSequence Analysis
Transmembranei1162 – 118221HelicalSequence AnalysisAdd
BLAST
Topological domaini1183 – 120220LumenalSequence AnalysisAdd
BLAST
Transmembranei1203 – 122321HelicalSequence AnalysisAdd
BLAST
Topological domaini1224 – 1355132CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. trans-Golgi network Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13551355Probable phospholipid-transporting ATPase DRS2PRO_0000046233Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39524.
PaxDbiP39524.

Expressioni

Gene expression databases

GenevestigatoriP39524.

Interactioni

Subunit structurei

Interacts with CDC50.1 Publication

Protein-protein interaction databases

BioGridi31740. 190 interactions.
DIPiDIP-2216N.
IntActiP39524. 10 interactions.
MINTiMINT-520976.
STRINGi4932.YAL026C.

Structurei

3D structure databases

ProteinModelPortaliP39524.
SMRiP39524. Positions 216-1019.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00770000120474.
HOGENOMiHOG000202528.
InParanoidiP39524.
KOiK14802.
OMAiIPRIYES.
OrthoDBiEOG7FR7QR.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. 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]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39524-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNDDRETPPK RKPGEDDTLF DIDFLDDTTS HSGSRSKVTN SHANANYIPP
60 70 80 90 100
SHVLPEETID LDADDDNIEN DVHENLFMSN NHDDQTSWNA NRFDSDAYQP
110 120 130 140 150
QSLRAVKPPG LFARFGNGLK NAFTFKRKKG PESFEMNHYN AVTNNELDDN
160 170 180 190 200
YLDSRNKFNI KILFNRYILR KNVGDAEGNG EPRVIHINDS LANSSFGYSD
210 220 230 240 250
NHISTTKYNF ATFLPKFLFQ EFSKYANLFF LCTSAIQQVP HVSPTNRYTT
260 270 280 290 300
IGTLLVVLIV SAMKECIEDI KRANSDKELN NSTAEIFSEA HDDFVEKRWI
310 320 330 340 350
DIRVGDIIRV KSEEPIPADT IILSSSEPEG LCYIETANLD GETNLKIKQS
360 370 380 390 400
RVETAKFIDV KTLKNMNGKV VSEQPNSSLY TYEGTMTLND RQIPLSPDQM
410 420 430 440 450
ILRGATLRNT AWIFGLVIFT GHETKLLRNA TATPIKRTAV EKIINRQIIA
460 470 480 490 500
LFTVLIVLIL ISSIGNVIMS TADAKHLSYL YLEGTNKAGL FFKDFLTFWI
510 520 530 540 550
LFSNLVPISL FVTVELIKYY QAFMIGSDLD LYYEKTDTPT VVRTSSLVEE
560 570 580 590 600
LGQIEYIFSD KTGTLTRNIM EFKSCSIAGH CYIDKIPEDK TATVEDGIEV
610 620 630 640 650
GYRKFDDLKK KLNDPSDEDS PIINDFLTLL ATCHTVIPEF QSDGSIKYQA
660 670 680 690 700
ASPDEGALVQ GGADLGYKFI IRKPNSVTVL LEETGEEKEY QLLNICEFNS
710 720 730 740 750
TRKRMSAIFR FPDGSIKLFC KGADTVILER LDDEANQYVE ATMRHLEDYA
760 770 780 790 800
SEGLRTLCLA MRDISEGEYE EWNSIYNEAA TTLDNRAEKL DEAANLIEKN
810 820 830 840 850
LILIGATAIE DKLQDGVPET IHTLQEAGIK IWVLTGDRQE TAINIGMSCR
860 870 880 890 900
LLSEDMNLLI INEETRDDTE RNLLEKINAL NEHQLSTHDM NTLALVIDGK
910 920 930 940 950
SLGFALEPEL EDYLLTVAKL CKAVICCRVS PLQKALVVKM VKRKSSSLLL
960 970 980 990 1000
AIGDGANDVS MIQAAHVGVG ISGMEGMQAA RSADIAVGQF KFLKKLLLVH
1010 1020 1030 1040 1050
GSWSYQRISV AILYSFYKNT ALYMTQFWYV FANAFSGQSI MESWTMSFYN
1060 1070 1080 1090 1100
LFFTVWPPFV IGVFDQFVSS RLLERYPQLY KLGQKGQFFS VYIFWGWIIN
1110 1120 1130 1140 1150
GFFHSAIVFI GTILIYRYGF ALNMHGELAD HWSWGVTVYT TSVIIVLGKA
1160 1170 1180 1190 1200
ALVTNQWTKF TLIAIPGSLL FWLIFFPIYA SIFPHANISR EYYGVVKHTY
1210 1220 1230 1240 1250
GSGVFWLTLI VLPIFALVRD FLWKYYKRMY EPETYHVIQE MQKYNISDSR
1260 1270 1280 1290 1300
PHVQQFQNAI RKVRQVQRMK KQRGFAFSQA EEGGQEKIVR MYDTTQKRGK
1310 1320 1330 1340 1350
YGELQDASAN PFNDNNGLGS NDFESAEPFI ENPFADGNQN SNRFSSSRDD

ISFDI
Length:1,355
Mass (Da):153,765
Last modified:July 27, 2011 - v2
Checksum:i5745B92901F8E1AE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462AN → GY in AAA16891. (PubMed:8247005)Curated
Sequence conflicti45 – 462AN → GY in AAC05006. (PubMed:7731988)Curated
Sequence conflicti450 – 4501A → R in AAA16891. (PubMed:8247005)Curated
Sequence conflicti450 – 4501A → R in AAC05006. (PubMed:7731988)Curated
Sequence conflicti674 – 6741P → G in AAA16891. (PubMed:8247005)Curated
Sequence conflicti674 – 6741P → G in AAC05006. (PubMed:7731988)Curated
Sequence conflicti891 – 8922NT → KS in AAA16891. (PubMed:8247005)Curated
Sequence conflicti891 – 8922NT → KS in AAC05006. (PubMed:7731988)Curated
Sequence conflicti953 – 9542GD → AS in AAA16891. (PubMed:8247005)Curated
Sequence conflicti953 – 9542GD → AS in AAC05006. (PubMed:7731988)Curated
Sequence conflicti987 – 9871V → L in AAA16891. (PubMed:8247005)Curated
Sequence conflicti987 – 9871V → L in AAC05006. (PubMed:7731988)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01795 Unassigned RNA. Translation: AAA16891.1.
U12980 Genomic DNA. Translation: AAC05006.1.
BK006935 Genomic DNA. Translation: DAA06962.2.
PIRiS51995.
RefSeqiNP_009376.2. NM_001178171.2.

Genome annotation databases

EnsemblFungiiYAL026C; YAL026C; YAL026C.
GeneIDi851207.
KEGGisce:YAL026C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01795 Unassigned RNA. Translation: AAA16891.1 .
U12980 Genomic DNA. Translation: AAC05006.1 .
BK006935 Genomic DNA. Translation: DAA06962.2 .
PIRi S51995.
RefSeqi NP_009376.2. NM_001178171.2.

3D structure databases

ProteinModelPortali P39524.
SMRi P39524. Positions 216-1019.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31740. 190 interactions.
DIPi DIP-2216N.
IntActi P39524. 10 interactions.
MINTi MINT-520976.
STRINGi 4932.YAL026C.

Protein family/group databases

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

Proteomic databases

MaxQBi P39524.
PaxDbi P39524.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YAL026C ; YAL026C ; YAL026C .
GeneIDi 851207.
KEGGi sce:YAL026C.

Organism-specific databases

CYGDi YAL026c.
SGDi S000000024. DRS2.

Phylogenomic databases

eggNOGi COG0474.
GeneTreei ENSGT00770000120474.
HOGENOMi HOG000202528.
InParanoidi P39524.
KOi K14802.
OMAi IPRIYES.
OrthoDBi EOG7FR7QR.

Enzyme and pathway databases

BioCyci YEAST:G3O-28837-MONOMER.
Reactomei REACT_96459. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi 968076.
PROi P39524.

Gene expression databases

Genevestigatori P39524.

Family and domain databases

Gene3Di 2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProi 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 ]
PANTHERi PTHR24092. PTHR24092. 1 hit.
Pfami PF00122. E1-E2_ATPase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SUPFAMi SSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsi TIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. 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].

Entry informationi

Entry nameiATC3_YEAST
AccessioniPrimary (citable) accession number: P39524
Secondary accession number(s): D6VPJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 606 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3