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Protein

Cation-transporting ATPase 5

Gene

cta5

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

Functioni

Plays a role in regulating calcium and manganese homeostasis responsible for cell cycle progression.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei480 – 48014-aspartylphosphate intermediateBy similarity
Metal bindingi838 – 8381MagnesiumBy similarity
Metal bindingi842 – 8421MagnesiumBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cation-transporting ATPase activity Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

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

Protein family/group databases

TCDBi3.A.3.10.13. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cation-transporting ATPase 5 (EC:3.6.3.-)
Gene namesi
Name:cta5
ORF Names:SPAC29A4.19c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC29A4.19c.
PomBaseiSPAC29A4.19c. cta5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence analysisAdd
BLAST
Transmembranei20 – 4122HelicalSequence analysisAdd
BLAST
Topological domaini42 – 476LumenalSequence analysis
Transmembranei48 – 7023HelicalSequence analysisAdd
BLAST
Topological domaini71 – 193123CytoplasmicSequence analysisAdd
BLAST
Transmembranei194 – 21623HelicalSequence analysisAdd
BLAST
Topological domaini217 – 2204LumenalSequence analysis
Transmembranei221 – 23818HelicalSequence analysisAdd
BLAST
Topological domaini239 – 391153CytoplasmicSequence analysisAdd
BLAST
Transmembranei392 – 41221HelicalSequence analysisAdd
BLAST
Topological domaini413 – 42513LumenalSequence analysisAdd
BLAST
Transmembranei426 – 44722HelicalSequence analysisAdd
BLAST
Topological domaini448 – 895448CytoplasmicSequence analysisAdd
BLAST
Transmembranei896 – 91520HelicalSequence analysisAdd
BLAST
Topological domaini916 – 9227LumenalSequence analysis
Transmembranei923 – 94018HelicalSequence analysisAdd
BLAST
Topological domaini941 – 95818CytoplasmicSequence analysisAdd
BLAST
Transmembranei959 – 98224HelicalSequence analysisAdd
BLAST
Topological domaini983 – 100321LumenalSequence analysisAdd
BLAST
Transmembranei1004 – 102623HelicalSequence analysisAdd
BLAST
Topological domaini1027 – 104014CytoplasmicSequence analysisAdd
BLAST
Transmembranei1041 – 106020HelicalSequence analysisAdd
BLAST
Topological domaini1061 – 107515LumenalSequence analysisAdd
BLAST
Transmembranei1076 – 109621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: PomBase
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10961096Cation-transporting ATPase 5PRO_0000046353Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14022.

Interactioni

Protein-protein interaction databases

BioGridi278553. 8 interactions.
MINTiMINT-4669857.

Structurei

3D structure databases

ProteinModelPortaliO14022.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiO14022.
KOiK14951.
OrthoDBiEOG74R1ZZ.
PhylomeDBiO14022.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. 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]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 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.

O14022-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSIELKQLV PENDSEPGTP RQLLFQHYDI SNEETIGIKP FKSIPAKVYI
60 70 80 90 100
LRVTEILTLG LLHLILTWLP EFRLKWIEAP CSNEDVEFVA ISDPSGTSSI
110 120 130 140 150
EKVSSICLKN DIQTSSFVLP SGKTRYFEYK KLRFYLEPLN LQWVLMPLET
160 170 180 190 200
SAYSLVTSTP AYIQNGLDTF TIAKLRQVYG SNSLVSTKKS IVTILLNEVL
210 220 230 240 250
HPFYLFQAVS VLIWLCDSFV FYSCCIVFIS SYSIFLSVKE SKESENRIHS
260 270 280 290 300
IIGAPQPVTV IRNQVKQTVL ADDLVIGDLL YFSNLDLKTC PVDGILFSSS
310 320 330 340 350
CLLDESMVTG ESVPARKFPL EDNSLDSWMI ASCNIFSPHL IHAGTKFLKI
360 370 380 390 400
DSTPSTPCLI SVVRTGFRSN KGQLIRNLLY PNLRPSQLYL DSMSFLKTMA
410 420 430 440 450
ILSFVSIVFI AIYLNLYNAS FGHVVLRSLD VLTILVPPAL PATLSVGIAN
460 470 480 490 500
SIARLSRALI YTTSPESIHN AGCLSTFVFD KTGTLTENSV QLSCVYVKSG
510 520 530 540 550
SNGLLKQVDA DSLSLDSTKL NAHAYRVATC SQSLELVGNE LVGDPLEVTL
560 570 580 590 600
FTQFNGTFCA TIRASNTPHP PLFSVSNSFD GPSQIFSIYK ALEFDPVLRR
610 620 630 640 650
MSVICSTSTE RSLMLFTKGA PESILAISSQ QSIPSNVQEV IHTLSSKGFR
660 670 680 690 700
IIAFASKNLI TPLQELIHLS RSTLESNVTF QGLFVLESPL RESSKDVISS
710 720 730 740 750
LLRSKMEVSI CSGDSLFTSV FVAKHCGALD SCNFIYTAEL ADSGDDCPQI
760 770 780 790 800
HFEKIDLQTQ NFQPIPDGFS LKDVILEKDS SLCMDGKLLQ RLLTMLSFNE
810 820 830 840 850
IKILLSKLRV LARMSPFDKA TYVELCQKYG CKVGFCGDGA NDCIALKQAD
860 870 880 890 900
VGVSLSDSEA CAAASFVSKK KSIKDVFNVL LEGRCSLILS HRCFQYMVLC
910 920 930 940 950
AIVQFSGVFF LYLKNYNFND NQFLFMDLLI IFPLSAAMSY FDPAQNLTSN
960 970 980 990 1000
RPNSTLFGKG RVKDLGIQSV LIWLSHGLLT LILHELNWVE LPEWQLEKSN
1010 1020 1030 1040 1050
TKNVLVTSIF LLSSLQYLGI CIGINQSSEF LSPIWKKKTY VCLCTTIGLC
1060 1070 1080 1090
NIYLCFANEN HIISRCLQIT RLPTLYRFII LFMGVISCCL TSILNM
Length:1,096
Mass (Da):121,936
Last modified:January 1, 1998 - v1
Checksum:i44BF98911481A543
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB10145.1.
PIRiT38470.
RefSeqiNP_594863.1. NM_001020292.2.

Genome annotation databases

EnsemblFungiiSPAC29A4.19c.1; SPAC29A4.19c.1:pep; SPAC29A4.19c.
GeneIDi2542076.
KEGGispo:SPAC29A4.19c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB10145.1.
PIRiT38470.
RefSeqiNP_594863.1. NM_001020292.2.

3D structure databases

ProteinModelPortaliO14022.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278553. 8 interactions.
MINTiMINT-4669857.

Protein family/group databases

TCDBi3.A.3.10.13. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBiO14022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC29A4.19c.1; SPAC29A4.19c.1:pep; SPAC29A4.19c.
GeneIDi2542076.
KEGGispo:SPAC29A4.19c.

Organism-specific databases

EuPathDBiFungiDB:SPAC29A4.19c.
PomBaseiSPAC29A4.19c. cta5.

Phylogenomic databases

InParanoidiO14022.
KOiK14951.
OrthoDBiEOG74R1ZZ.
PhylomeDBiO14022.

Miscellaneous databases

PROiO14022.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. 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]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 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. "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. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. "Characterization of a fission yeast P(5)-type ATPase homologue that is essential for Ca(2+)/Mn(2+) homeostasis in the absence of P(2)-type ATPases."
    Furune T., Hashimoto K., Ishiguro J.
    Genes Genet. Syst. 83:373-381(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.

Entry informationi

Entry nameiCTA5_SCHPO
AccessioniPrimary (citable) accession number: O14022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 126 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.