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Protein

Manganese-transporting ATPase 1

Gene

SPF1

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

Functioni

Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei487 – 48714-aspartylphosphate intermediateBy similarity
Metal bindingi816 – 8161MagnesiumBy similarity
Metal bindingi820 – 8201MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

  • cation transport Source: InterPro
  • cellular calcium ion homeostasis Source: SGD
  • cellular manganese ion homeostasis Source: SGD
  • ion transmembrane transport Source: GOC
  • sterol homeostasis Source: SGD
  • transmembrane transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30153-MONOMER.

Protein family/group databases

TCDBi3.A.3.10.3. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Manganese-transporting ATPase 1 (EC:3.6.3.-)
Gene namesi
Name:SPF1
Ordered Locus Names:YEL031W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

CYGDiYEL031w.
EuPathDBiFungiDB:YEL031W.
SGDiS000000757. SPF1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei22 – 4322HelicalSequence AnalysisAdd
BLAST
Topological domaini44 – 496ExtracellularSequence Analysis
Transmembranei50 – 7223HelicalSequence AnalysisAdd
BLAST
Topological domaini73 – 191119CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei192 – 21423HelicalSequence AnalysisAdd
BLAST
Topological domaini215 – 2173ExtracellularSequence Analysis
Transmembranei218 – 23619HelicalSequence AnalysisAdd
BLAST
Topological domaini237 – 399163CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei400 – 41920HelicalSequence AnalysisAdd
BLAST
Topological domaini420 – 43213ExtracellularSequence AnalysisAdd
BLAST
Transmembranei433 – 45422HelicalSequence AnalysisAdd
BLAST
Topological domaini455 – 993539CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei994 – 101320HelicalSequence AnalysisAdd
BLAST
Topological domaini1014 – 10207ExtracellularSequence Analysis
Transmembranei1021 – 103717HelicalSequence AnalysisAdd
BLAST
Topological domaini1038 – 105518CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1056 – 107924HelicalSequence AnalysisAdd
BLAST
Topological domaini1080 – 109920ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1100 – 112223HelicalSequence AnalysisAdd
BLAST
Topological domaini1123 – 113311CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1134 – 115320HelicalSequence AnalysisAdd
BLAST
Topological domaini1154 – 117017ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1171 – 119323HelicalSequence AnalysisAdd
BLAST
Topological domaini1194 – 121522CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cis-Golgi network Source: SGD
  • endoplasmic reticulum membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi487 – 4871D → N: Loss of ATPase activity and transport function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12151215Manganese-transporting ATPase 1PRO_0000046349Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei324 – 3241Phosphoserine1 Publication
Modified residuei936 – 9361Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39986.
PaxDbiP39986.
PeptideAtlasiP39986.

Interactioni

Protein-protein interaction databases

BioGridi36698. 325 interactions.
DIPiDIP-6637N.
IntActiP39986. 3 interactions.
MINTiMINT-633403.
STRINGi4932.YEL031W.

Structurei

3D structure databases

ProteinModelPortaliP39986.
SMRiP39986. Positions 225-865.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00550000075064.
HOGENOMiHOG000199432.
InParanoidiP39986.
KOiK14950.
OMAiYLYSEAQ.
OrthoDBiEOG74R1ZZ.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF82. PTHR24093:SF82. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39986-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKSFVSSP IVRDSTLLVP KSLIAKPYVL PFFPLYATFA QLYFQQYDRY
60 70 80 90 100
IKGPEWTFVY LGTLVSLNIL VMLMPAWNVK IKAKFNYSTT KNVNEATHIL
110 120 130 140 150
IYTTPNNGSD GIVEIQRVTE AGSLQTFFQF QKKRFLWHEN EQVFSSPKFL
160 170 180 190 200
VDESPKIGDF QKCKGHSGDL THLKRLYGEN SFDIPIPTFM ELFKEHAVAP
210 220 230 240 250
LFVFQVFCVA LWLLDEFWYY SLFNLFMIIS MEAAAVFQRL TALKEFRTMG
260 270 280 290 300
IKPYTINVFR NKKWVALQTN ELLPMDLVSI TRTAEESAIP CDLILLDGSA
310 320 330 340 350
IVNEAMLSGE STPLLKESIK LRPSEDNLQL DGVDKIAVLH GGTKALQVTP
360 370 380 390 400
PEHKSDIPPP PDGGALAIVT KTGFETSQGS LVRVMIYSAE RVSVDNKEAL
410 420 430 440 450
MFILFLLIFA VIASWYVWVE GTKMGRIQSK LILDCILIIT SVVPPELPME
460 470 480 490 500
LTMAVNSSLA ALAKFYVYCT EPFRIPFAGR IDVCCFDKTG TLTGEDLVFE
510 520 530 540 550
GLAGISADSE NIRHLYSAAE APESTILVIG AAHALVKLED GDIVGDPMEK
560 570 580 590 600
ATLKAVGWAV ERKNSNYREG TGKLDIIRRF QFSSALKRSA SIASHNDALF
610 620 630 640 650
AAVKGAPETI RERLSDIPKN YDEIYKSFTR SGSRVLALAS KSLPKMSQSK
660 670 680 690 700
IDDLNRDDVE SELTFNGFLI FHCPLKDDAI ETIKMLNESS HRSIMITGDN
710 720 730 740 750
PLTAVHVAKE VGIVFGETLI LDRAGKSDDN QLLFRDVEET VSIPFDPSKD
760 770 780 790 800
TFDHSKLFDR YDIAVTGYAL NALEGHSQLR DLLRHTWVYA RVSPSQKEFL
810 820 830 840 850
LNTLKDMGYQ TLMCGDGTND VGALKQAHVG IALLNGTEEG LKKLGEQRRL
860 870 880 890 900
EGMKMMYIKQ TEFMARWNQP QPPVPEPIAH LFPPGPKNPH YLKALESKGT
910 920 930 940 950
VITPEIRKAV EEANSKPVEV IKPNGLSEKK PADLASLLLN SAGDAQGDEA
960 970 980 990 1000
PALKLGDASC AAPFTSKLAN VSAVTNIIRQ GRCALVNTIQ MYKILALNCL
1010 1020 1030 1040 1050
ISAYSLSIIY MAGVKFGDGQ ATVSGLLLSV CFLSISRGKP LEKLSKQRPQ
1060 1070 1080 1090 1100
SGIFNVYIMG SILSQFAVHI ATLVYITTEI YKLEPREPQV DLEKEFAPSL
1110 1120 1130 1140 1150
LNTGIFIIQL VQQVSTFAVN YQGEPFRENI RSNKGMYYGL LGVTGLALAS
1160 1170 1180 1190 1200
ATEFLPELNE AMKFVPMTDD FKIKLTLTLL LDFFGSWGVE HFFKFFFMDD
1210
KPSDISVQQV KIASK
Length:1,215
Mass (Da):135,269
Last modified:February 1, 1995 - v1
Checksum:i7A9960D34B91B5AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18530 Genomic DNA. Translation: AAB64508.1.
BK006939 Genomic DNA. Translation: DAA07622.1.
PIRiS50428.
RefSeqiNP_010883.3. NM_001178846.3.

Genome annotation databases

EnsemblFungiiYEL031W; YEL031W; YEL031W.
GeneIDi856681.
KEGGisce:YEL031W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18530 Genomic DNA. Translation: AAB64508.1.
BK006939 Genomic DNA. Translation: DAA07622.1.
PIRiS50428.
RefSeqiNP_010883.3. NM_001178846.3.

3D structure databases

ProteinModelPortaliP39986.
SMRiP39986. Positions 225-865.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36698. 325 interactions.
DIPiDIP-6637N.
IntActiP39986. 3 interactions.
MINTiMINT-633403.
STRINGi4932.YEL031W.

Protein family/group databases

TCDBi3.A.3.10.3. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBiP39986.
PaxDbiP39986.
PeptideAtlasiP39986.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL031W; YEL031W; YEL031W.
GeneIDi856681.
KEGGisce:YEL031W.

Organism-specific databases

CYGDiYEL031w.
EuPathDBiFungiDB:YEL031W.
SGDiS000000757. SPF1.

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00550000075064.
HOGENOMiHOG000199432.
InParanoidiP39986.
KOiK14950.
OMAiYLYSEAQ.
OrthoDBiEOG74R1ZZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-30153-MONOMER.

Miscellaneous databases

NextBioi982710.
PROiP39986.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF82. PTHR24093:SF82. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-487.

Entry informationi

Entry nameiATC6_YEAST
AccessioniPrimary (citable) accession number: P39986
Secondary accession number(s): D3DLL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 24, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1870 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.