Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O59868 (ATC1_SCHPO)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Calcium-transporting ATPase 1
    EC=3.6.3.8
Alternative name(s):
    Golgi Ca(2+)-ATPase
Gene names
Name: pmr1
Synonyms: pgak2
ORF Names: SPBC31E1.02c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Hide | Top

Protein attributes

Sequence length899 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Transports calcium and manganese ions into the cell. Regulates cell morphogenesis through control of manganese and calcium homeostasis. Ref.1 Ref.4

Catalytic activity

ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans).

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Ref.1

Sequence similarities

Belongs to the cation transport ATPase (P-type) family.

Hide | Top

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   LigandATP-binding
Calcium
Manganese
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

calcium ion transmembrane transport Ref.4

Inferred from genetic interaction. Source: GeneDB_SPombe

cell wall organization Ref.1

Inferred from mutant phenotype. Source: GeneDB_SPombe

cellular calcium ion homeostasis Ref.1

Inferred from genetic interaction. Source: GeneDB_SPombe

cellular manganese ion homeostasis Ref.4

Inferred from mutant phenotype. Source: GeneDB_SPombe

cytokinesis Ref.1

Inferred from mutant phenotype. Source: GeneDB_SPombe

manganese ion transport Ref.4

Inferred from mutant phenotype. Source: GeneDB_SPombe

positive regulation of calcium-mediated signaling

Inferred from mutant phenotype. Source: GeneDB_SPombe

protein amino acid glycosylation Ref.1

Inferred from mutant phenotype. Source: GeneDB_SPombe

   Cellular componentintegral to endoplasmic reticulum membrane

Inferred by curator. Source: GeneDB_SPombe

   Molecular functionATP binding

Inferred by curator. Source: GeneDB_SPombe

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-transporting ATPase activity

Inferred from electronic annotation. Source: EC

manganese ion binding

Inferred by curator. Source: GeneDB_SPombe

manganese-transporting ATPase activity Ref.4

Traceable author statement. Source: GeneDB_SPombe

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 899899Calcium-transporting ATPase 1
PRO_0000046229

Regions

Transmembrane59 – 7921 Potential
Transmembrane80 – 10021 Potential
Transmembrane247 – 26721 Potential
Transmembrane282 – 30221 Potential
Transmembrane688 – 70821 Potential
Transmembrane757 – 77721 Potential
Transmembrane827 – 84721 Potential
Transmembrane854 – 87421 Potential

Sites

Active site32914-aspartylphosphate intermediate By similarity

Amino acid modifications

Modified residue8921Phosphoserine Ref.5

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
O59868-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 7E45E9180F36FD44

FASTA89998,359
        10         20         30         40         50         60 
MSVQYDAFSV EQTCADLETD MYNGLSSLQE ITRRNKVHGD NDLKVEDEEN MVVQFLKQFV 

        70         80         90        100        110        120 
KDPLILLLFA SSAISVTLGN IDDAISIALA IVIVVTVGFV QEYRSEQSLK ALNNLVPHYC 

       130        140        150        160        170        180 
NVIRSGKTEH IVASKLVPGD LVILQIGDRV PADLRIVEAT ELEIDESNLT GENSPRKKSS 

       190        200        210        220        230        240 
EAISSNISLT ERNNIAFMGT LVRHGHGRGI VVATGSDTEF GRVFLTMQQT EKPKTPLQNS 

       250        260        270        280        290        300 
MDDLGKQLSL ISLIGIAVIV LVGFFQGKNW LEMLTIGVSL AVAAIPEGLP IIVTVTLALG 

       310        320        330        340        350        360 
VLRMSKKRAI IRRLPSVETL GSVNVICSDK TGTLTMNHMT VTKIYTCGML AAFSLPESEH 

       370        380        390        400        410        420 
IELSVRRTVG IEKALLAAAL CNNSKVHNKA DSILDTTCPW AGFPVDVALI ECSERFGLKD 

       430        440        450        460        470        480 
PRETYSRISE VSFSSERKYM SVAVQYNSSK MNFMKGATEQ VLSSCAYFSD QDGVQHELTA 

       490        500        510        520        530        540 
EMKENIQRNE FEMAASGLRI IAVASGINTN KLVFHGLFGI NDPPRPQVRE SVQYLMTGGV 

       550        560        570        580        590        600 
RVIMITGDSV VTAISIARSL GMAIPSNDEE AIRNYALTGA QLDDLDSSSL RDAVSRVVVF 

       610        620        630        640        650        660 
ARTTPQHKMK IVEALQSLGD VVAMTGDGVN DAPALKLADI GIAMGRQGTD VAKEAADMIL 

       670        680        690        700        710        720 
TDDSFATILS AVEEGKGIFN NIKNFITFQL STSVAALSLI AISSVFGFQN PLNAMQILWI 

       730        740        750        760        770        780 
NILMDGPPAQ SLGVESVDED VMMKPPRPRN APIISVQLLQ RVLLSAFIIV TVTIVVFRVQ 

       790        800        810        820        830        840 
MQDGNVTARD TTMTFTCFVF FDMFNALACR SETKSVFKLG IFSNRMFNIA VGGSLIGQAL 

       850        860        870        880        890 
VVYASPFQRI FQTEAIGLKD VLILLACTSS VLWVDEIRKW YRRRKGLVRT KSNYLLRNV

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Schizosaccharomyces pombe Pmr1p is essential for cell wall integrity and is required for polarized cell growth and cytokinesis."
Cortes J.C.G., Katoh-Fukui R., Moto K., Ribas J.C., Ishiguro J.
Eukaryot. Cell 3:1124-1135(2004) [PubMed: 15470240] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"S. pombe genomic sequence PGAK, extension of cosmid 800, accession U41410."
Kaplan N., Gnoj L., Lodhi M., Johnson A.F., Dedhia N., Parnell L.D., McCombie W.R.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[4]"Pmr1, a P-type ATPase, and Pdt1, an Nramp homologue, cooperatively regulate cell morphogenesis in fission yeast: the importance of Mn2+ homeostasis."
Maeda T., Sugiura R., Kita A., Saito M., Deng L., He Y., Yabin L., Fujita Y., Takegawa K., Shuntoh H., Kuno T.
Genes Cells 9:71-82(2004) [PubMed: 14723709] [Abstract]
Cited for: FUNCTION.
[5]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-892, MASS SPECTROMETRY.

Hide | Top

Cross-references

Sequence databases

AC004698 Genomic DNA. Translation: AAC16669.1.
CU329671 Genomic DNA. Translation: CAB39136.1.
PIRT40199.
RefSeqNP_595098.1.

3D structure databases

HSSPHSSP built from PDB template 1SU4 based on UniProtKB P04191.
ModBaseSearch...

Protein-protein interaction databases

STRINGO59868.

Genome annotation databases

GeneID2540383.
GenomeReviewsGene locus pmr1 in contig CU329671_GR.
KEGGspo:SPBC31E1.02c.
NMPDRfig|4896.1.peg.964.

Organism-specific databases

GeneDB_SpombeSPBC31E1.02c.

Phylogenomic databases

OMAHYCHLIR.

Enzyme and pathway databases

BRENDA3.6.3.8. 653.

Gene expression databases

ArrayExpressO59868.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-reg.
IPR006413. ATPase_P-typ_Ca-transp_PMR1.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
TIGRFAMsTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameATC1_SCHPO
AccessionPrimary (citable) accession number: O59868
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents