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Protein

Calcium-transporting ATPase 2

Gene

pmc1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports the calcium to the vacuole and participates in the control of the cytosolic free calcium.1 Publication

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei545 – 54514-aspartylphosphate intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

  • calcium ion transmembrane transport Source: PomBase
  • cellular calcium ion homeostasis Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-418359. Reduction of cytosolic Ca++ levels.
R-SPO-5578775. Ion homeostasis.
R-SPO-936837. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.2.35. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-transporting ATPase 2 (EC:3.6.3.8)
Gene namesi
Name:pmc1
ORF Names:SPAPB2B4.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAPB2B4.04c.
PomBaseiSPAPB2B4.04c. pmc1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 236236CytoplasmicSequence analysisAdd
BLAST
Transmembranei237 – 25721HelicalSequence analysisAdd
BLAST
Topological domaini258 – 27316ExtracellularSequence analysisAdd
BLAST
Transmembranei274 – 29421HelicalSequence analysisAdd
BLAST
Topological domaini295 – 448154CytoplasmicSequence analysisAdd
BLAST
Transmembranei449 – 46921HelicalSequence analysisAdd
BLAST
Topological domaini470 – 48819ExtracellularSequence analysisAdd
BLAST
Transmembranei489 – 50921HelicalSequence analysisAdd
BLAST
Topological domaini510 – 938429CytoplasmicSequence analysisAdd
BLAST
Transmembranei939 – 95921HelicalSequence analysisAdd
BLAST
Topological domaini960 – 9667ExtracellularSequence analysis
Transmembranei967 – 98721HelicalSequence analysisAdd
BLAST
Topological domaini988 – 101629CytoplasmicSequence analysisAdd
BLAST
Transmembranei1017 – 103721HelicalSequence analysisAdd
BLAST
Topological domaini1038 – 108447ExtracellularSequence analysisAdd
BLAST
Transmembranei1085 – 110521HelicalSequence analysisAdd
BLAST
Topological domaini1106 – 111510CytoplasmicSequence analysis
Transmembranei1116 – 113621HelicalSequence analysisAdd
BLAST
Topological domaini1137 – 1292156ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12921292Calcium-transporting ATPase 2PRO_0000362141Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HDW7.

Interactioni

Protein-protein interaction databases

BioGridi279897. 17 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9HDW7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 94Poly-Asp
Compositional biasi10 – 10596Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000265623.
InParanoidiQ9HDW7.
KOiK01537.
OMAiARTHATQ.
OrthoDBiEOG7BS4JT.
PhylomeDBiQ9HDW7.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HDW7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTYNDDDDS SRPPSVHSER NQKPSSSQFL GVPSSNYNQR ENSSRSGSST
60 70 80 90 100
ISREPSSSGT MYPMASRDSM KESYDKNKGT PPDYTSYVSH SDAEPEQASS
110 120 130 140 150
KSSTSIEDLL HTEYDDAPFA FSIPLLQRLQ DPKNTSLLHA IHGLKGLCKG
160 170 180 190 200
LKVDPSTGIS THEPHYADKL QMSDILNDDS NPKLVVHLDR IRSQDNNPEA
210 220 230 240 250
KVSHDSDRVK YYGKNVLPEH DSKGLIRLML EAFKDKVLIL LSIAAVVSLA
260 270 280 290 300
LGLYQTFGQP PTLDPITGKP EPRVEWVEGV AIMAAIVIVV TVGGVNDWQK
310 320 330 340 350
ELQFKKLNAK VSNFDVQVLR DGAVHSTSVF DLVVGDVLFV EAGDVVPVDG
360 370 380 390 400
VLIESNNLVL DESAMTGETD NIKKVDANTA IERTSPDVEY RKNADPYLIS
410 420 430 440 450
GTTILEGNGK LLVTAVGVNS FNGRTTMAMR TEGQATPLQL RLSRVADAIA
460 470 480 490 500
KLGGAASALL FIVLLIEFLV RLKSNDSSSK NKGQEFLQIL IVSVTLLVVA
510 520 530 540 550
VPEGLPLAVT LALAFATNRM QKDNNLVRHL QACETMGTAT NICSDKTGTL
560 570 580 590 600
TQNRMTVVAG GFGTDVLFFD HNDETPTNVD QGSDSSKFED AGASAFAFKR
610 620 630 640 650
LSPELRDLTL YSIAVNSTCR QLFEDNSDTP RFIGSKTETA LLDMSVKELG
660 670 680 690 700
LTNVDSMRSS VDIKQFFSFS SDRKASGAIF EYKDKYYFVV KGMPERVLQQ
710 720 730 740 750
STSVITNGSL DEVEDMHSHA DYFKEMITGY AKRSLRTLGL CYRVFDSWPP
760 770 780 790 800
KDIPTNDEDS SNPLKWEDAF TDMTFLGFFG IMDPIRPDVP LAVKVCQGAG
810 820 830 840 850
VTVRMVTGDN IVTAKAIASQ CGIYTEDGIS MEGPEFRSLS DEKRLEILPK
860 870 880 890 900
LDVLARSSPL DKQLLIEGLQ KLGNVVAVTG DGTNDAPALK KANVGFSMGK
910 920 930 940 950
SGTEVAKEAS DIILMDDNFS SIVKAIAWGR TVNDAVKKFL QFQITVNITA
960 970 980 990 1000
VFLTIISAVA STDQSSVLTA VQLLWVNLIM DTLAALALAT DPPTPEVLKR
1010 1020 1030 1040 1050
KPEKPGASLF TFDMWKMIIC QSMYQLAVTL VLHFAGNSIF HYPSNTADMN
1060 1070 1080 1090 1100
TIVFNTFVWL QLFNEINNRR LDNKLNIFER INHNFLFIAI FVIVAGIQVI
1110 1120 1130 1140 1150
IVFFGGAAFS VKRIDGKGWA ISIVFGVISI PLGALIRCVP NNFLRKVLPV
1160 1170 1180 1190 1200
KTIDTVFSWI LNPRFRSKRR STDHDVESLS LIPYEPTSPN EVIDSIRHSL
1210 1220 1230 1240 1250
GFVQRIRGGR IRHLLNNSKF DKQMEALPER LRPRVKQRFM KIRSPSVSSA
1260 1270 1280 1290
TSVALMIPIS TLVSEASGRL GGHDIWISHN RQALDKKSSN VH
Length:1,292
Mass (Da):142,235
Last modified:March 1, 2001 - v1
Checksum:i1499E90144A2B07B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC21470.1.
AB027950 Genomic DNA. Translation: BAA87254.1.
RefSeqiNP_593890.1. NM_001019320.2.

Genome annotation databases

EnsemblFungiiSPAPB2B4.04c.1; SPAPB2B4.04c.1:pep; SPAPB2B4.04c.
GeneIDi2543477.
KEGGispo:SPAPB2B4.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC21470.1.
AB027950 Genomic DNA. Translation: BAA87254.1.
RefSeqiNP_593890.1. NM_001019320.2.

3D structure databases

ProteinModelPortaliQ9HDW7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279897. 17 interactions.

Protein family/group databases

TCDBi3.A.3.2.35. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBiQ9HDW7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAPB2B4.04c.1; SPAPB2B4.04c.1:pep; SPAPB2B4.04c.
GeneIDi2543477.
KEGGispo:SPAPB2B4.04c.

Organism-specific databases

EuPathDBiFungiDB:SPAPB2B4.04c.
PomBaseiSPAPB2B4.04c. pmc1.

Phylogenomic databases

HOGENOMiHOG000265623.
InParanoidiQ9HDW7.
KOiK01537.
OMAiARTHATQ.
OrthoDBiEOG7BS4JT.
PhylomeDBiQ9HDW7.

Enzyme and pathway databases

ReactomeiR-SPO-418359. Reduction of cytosolic Ca++ levels.
R-SPO-5578775. Ion homeostasis.
R-SPO-936837. Ion transport by P-type ATPases.

Miscellaneous databases

PROiQ9HDW7.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 161-331.
    Strain: ATCC 38364 / 968.
  3. "An inventory of the P-type ATPases in the fission yeast Schizosaccharomyces pombe."
    Okorokova-Facanha A.L., Okorokov L.A., Ekwall K.
    Curr. Genet. 43:273-280(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiATC2_SCHPO
AccessioniPrimary (citable) accession number: Q9HDW7
Secondary accession number(s): Q9UTX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.