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P39986 (ATC6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. 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:
Manganese-transporting ATPase 1

EC=3.6.3.-
Gene names
Name:SPF1
Ordered Locus Names:YEL031W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis. Ref.8

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.8.

Disruption phenotype

Specific reduction in the luminal concentration of manganese ions, and increase of cytosolic Mn2+-dependent processes. Interruption of sphingolipids biosynthesis, reduced exit of GPI-anchored proteins from the ER, reduced protein mannosylation. Overexpression leads to an increase of luminal manganese. Ref.8

Miscellaneous

Present with 1870 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily. [View classification]

Ontologies

Keywords
   Biological processTransport
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 12058017. Source: SGD

cellular manganese ion homeostasis

Inferred from mutant phenotype Ref.8. Source: SGD

ion transmembrane transport

Inferred from direct assay PubMed 12058017PubMed 22745129. Source: GOC

sterol homeostasis

Inferred from mutant phenotype PubMed 22918956. Source: SGD

transmembrane transport

Inferred from mutant phenotype PubMed 12058017. Source: SGD

   Cellular_componentcis-Golgi network

Inferred from direct assay PubMed 11791712. Source: SGD

endoplasmic reticulum membrane

Inferred from direct assay PubMed 12058017PubMed 22745129. Source: SGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism

Inferred from direct assay PubMed 12058017PubMed 22745129. Source: SGD

cation-transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12151215Manganese-transporting ATPase 1
PRO_0000046349

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4322Helical; Potential
Topological domain44 – 496Extracellular Potential
Transmembrane50 – 7223Helical; Potential
Topological domain73 – 191119Cytoplasmic Potential
Transmembrane192 – 21423Helical; Potential
Topological domain215 – 2173Extracellular Potential
Transmembrane218 – 23619Helical; Potential
Topological domain237 – 399163Cytoplasmic Potential
Transmembrane400 – 41920Helical; Potential
Topological domain420 – 43213Extracellular Potential
Transmembrane433 – 45422Helical; Potential
Topological domain455 – 993539Cytoplasmic Potential
Transmembrane994 – 101320Helical; Potential
Topological domain1014 – 10207Extracellular Potential
Transmembrane1021 – 103717Helical; Potential
Topological domain1038 – 105518Cytoplasmic Potential
Transmembrane1056 – 107924Helical; Potential
Topological domain1080 – 109920Extracellular Potential
Transmembrane1100 – 112223Helical; Potential
Topological domain1123 – 113311Cytoplasmic Potential
Transmembrane1134 – 115320Helical; Potential
Topological domain1154 – 117017Extracellular Potential
Transmembrane1171 – 119323Helical; Potential
Topological domain1194 – 121522Cytoplasmic Potential

Sites

Active site48714-aspartylphosphate intermediate By similarity
Metal binding8161Magnesium By similarity
Metal binding8201Magnesium By similarity

Amino acid modifications

Modified residue3241Phosphoserine Ref.6
Modified residue9361Phosphoserine Ref.6

Experimental info

Mutagenesis4871D → N: Loss of ATPase activity and transport function. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P39986 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 7A9960D34B91B5AE

FASTA1,215135,269
        10         20         30         40         50         60 
MTKKSFVSSP IVRDSTLLVP KSLIAKPYVL PFFPLYATFA QLYFQQYDRY IKGPEWTFVY 

        70         80         90        100        110        120 
LGTLVSLNIL VMLMPAWNVK IKAKFNYSTT KNVNEATHIL IYTTPNNGSD GIVEIQRVTE 

       130        140        150        160        170        180 
AGSLQTFFQF QKKRFLWHEN EQVFSSPKFL VDESPKIGDF QKCKGHSGDL THLKRLYGEN 

       190        200        210        220        230        240 
SFDIPIPTFM ELFKEHAVAP LFVFQVFCVA LWLLDEFWYY SLFNLFMIIS MEAAAVFQRL 

       250        260        270        280        290        300 
TALKEFRTMG IKPYTINVFR NKKWVALQTN ELLPMDLVSI TRTAEESAIP CDLILLDGSA 

       310        320        330        340        350        360 
IVNEAMLSGE STPLLKESIK LRPSEDNLQL DGVDKIAVLH GGTKALQVTP PEHKSDIPPP 

       370        380        390        400        410        420 
PDGGALAIVT KTGFETSQGS LVRVMIYSAE RVSVDNKEAL MFILFLLIFA VIASWYVWVE 

       430        440        450        460        470        480 
GTKMGRIQSK LILDCILIIT SVVPPELPME LTMAVNSSLA ALAKFYVYCT EPFRIPFAGR 

       490        500        510        520        530        540 
IDVCCFDKTG TLTGEDLVFE GLAGISADSE NIRHLYSAAE APESTILVIG AAHALVKLED 

       550        560        570        580        590        600 
GDIVGDPMEK ATLKAVGWAV ERKNSNYREG TGKLDIIRRF QFSSALKRSA SIASHNDALF 

       610        620        630        640        650        660 
AAVKGAPETI RERLSDIPKN YDEIYKSFTR SGSRVLALAS KSLPKMSQSK IDDLNRDDVE 

       670        680        690        700        710        720 
SELTFNGFLI FHCPLKDDAI ETIKMLNESS HRSIMITGDN PLTAVHVAKE VGIVFGETLI 

       730        740        750        760        770        780 
LDRAGKSDDN QLLFRDVEET VSIPFDPSKD TFDHSKLFDR YDIAVTGYAL NALEGHSQLR 

       790        800        810        820        830        840 
DLLRHTWVYA RVSPSQKEFL LNTLKDMGYQ TLMCGDGTND VGALKQAHVG IALLNGTEEG 

       850        860        870        880        890        900 
LKKLGEQRRL EGMKMMYIKQ TEFMARWNQP QPPVPEPIAH LFPPGPKNPH YLKALESKGT 

       910        920        930        940        950        960 
VITPEIRKAV EEANSKPVEV IKPNGLSEKK PADLASLLLN SAGDAQGDEA PALKLGDASC 

       970        980        990       1000       1010       1020 
AAPFTSKLAN VSAVTNIIRQ GRCALVNTIQ MYKILALNCL ISAYSLSIIY MAGVKFGDGQ 

      1030       1040       1050       1060       1070       1080 
ATVSGLLLSV CFLSISRGKP LEKLSKQRPQ SGIFNVYIMG SILSQFAVHI ATLVYITTEI 

      1090       1100       1110       1120       1130       1140 
YKLEPREPQV DLEKEFAPSL LNTGIFIIQL VQQVSTFAVN YQGEPFRENI RSNKGMYYGL 

      1150       1160       1170       1180       1190       1200 
LGVTGLALAS ATEFLPELNE AMKFVPMTDD FKIKLTLTLL LDFFGSWGVE HFFKFFFMDD 

      1210 
KPSDISVQQV KIASK 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"P-type ATPase spf1 mutants show a novel resistance mechanism for the killer toxin SMKT."
Suzuki C., Shimma Y.
Mol. Microbiol. 32:813-823(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"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].
[5]"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.
[6]"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-324 AND SER-936, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"The yeast p5 type ATPase, spf1, regulates manganese transport into the endoplasmic reticulum."
Cohen Y., Megyeri M., Chen O.C., Condomitti G., Riezman I., Loizides-Mangold U., Abdul-Sada A., Rimon N., Riezman H., Platt F.M., Futerman A.H., Schuldiner M.
PLoS ONE 8:E85519-E85519(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-487.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18530 Genomic DNA. Translation: AAB64508.1.
BK006939 Genomic DNA. Translation: DAA07622.1.
PIRS50428.
RefSeqNP_010883.3. NM_001178846.3.

3D structure databases

ProteinModelPortalP39986.
SMRP39986. Positions 225-865, 939-999.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36698. 321 interactions.
DIPDIP-6637N.
IntActP39986. 3 interactions.
MINTMINT-633403.
STRING4932.YEL031W.

Protein family/group databases

TCDB3.A.3.10.3. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBP39986.
PaxDbP39986.
PeptideAtlasP39986.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL031W; YEL031W; YEL031W.
GeneID856681.
KEGGsce:YEL031W.

Organism-specific databases

CYGDYEL031w.
SGDS000000757. SPF1.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00550000075064.
HOGENOMHOG000199432.
KOK14950.
OMAIISCPLK.
OrthoDBEOG74R1ZZ.

Enzyme and pathway databases

BioCycYEAST:G3O-30153-MONOMER.

Gene expression databases

GenevestigatorP39986.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR006544. ATPase_P-typ_Cation_typ_V.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PANTHERPTHR24093:SF82. PTHR24093:SF82. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982710.
PROP39986.

Entry information

Entry nameATC6_YEAST
AccessionPrimary (citable) accession number: P39986
Secondary accession number(s): D3DLL8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

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

SIMILARITY comments

Index of protein domains and families