CTA5_SCHPO
ID CTA5_SCHPO Reviewed; 1096 AA.
AC O14022;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cation-transporting ATPase 5;
DE EC=7.2.2.-;
GN Name=cta5; ORFNames=SPAC29A4.19c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19168988; DOI=10.1266/ggs.83.373;
RA Furune T., Hashimoto K., Ishiguro J.;
RT "Characterization of a fission yeast P(5)-type ATPase homologue that is
RT essential for Ca(2+)/Mn(2+) homeostasis in the absence of P(2)-type
RT ATPases.";
RL Genes Genet. Syst. 83:373-381(2008).
CC -!- FUNCTION: Plays a role in regulating calcium and manganese homeostasis
CC responsible for cell cycle progression. {ECO:0000269|PubMed:19168988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:19168988};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB10145.1; -; Genomic_DNA.
DR PIR; T38470; T38470.
DR RefSeq; NP_594863.1; NM_001020292.2.
DR AlphaFoldDB; O14022; -.
DR SMR; O14022; -.
DR BioGRID; 278553; 8.
DR STRING; 4896.SPAC29A4.19c.1; -.
DR TCDB; 3.A.3.10.13; the p-type atpase (p-atpase) superfamily.
DR MaxQB; O14022; -.
DR PaxDb; O14022; -.
DR PRIDE; O14022; -.
DR EnsemblFungi; SPAC29A4.19c.1; SPAC29A4.19c.1:pep; SPAC29A4.19c.
DR GeneID; 2542076; -.
DR KEGG; spo:SPAC29A4.19c; -.
DR PomBase; SPAC29A4.19c; cta5.
DR VEuPathDB; FungiDB:SPAC29A4.19c; -.
DR eggNOG; KOG0208; Eukaryota.
DR HOGENOM; CLU_001828_0_0_1; -.
DR InParanoid; O14022; -.
DR OMA; RCFQYMV; -.
DR PhylomeDB; O14022; -.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:O14022; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; TAS:PomBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:PomBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IGI:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Endoplasmic reticulum; Golgi apparatus; Magnesium;
KW Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1096
FT /note="Cation-transporting ATPase 5"
FT /id="PRO_0000046353"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..47
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..220
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..425
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 896..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..922
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..958
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 959..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..1003
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1004..1026
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1027..1040
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1041..1060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1061..1075
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1076..1096
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 480
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 838
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 842
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1096 AA; 121936 MW; 44BF98911481A543 CRC64;
MDSIELKQLV PENDSEPGTP RQLLFQHYDI SNEETIGIKP FKSIPAKVYI LRVTEILTLG
LLHLILTWLP EFRLKWIEAP CSNEDVEFVA ISDPSGTSSI EKVSSICLKN DIQTSSFVLP
SGKTRYFEYK KLRFYLEPLN LQWVLMPLET SAYSLVTSTP AYIQNGLDTF TIAKLRQVYG
SNSLVSTKKS IVTILLNEVL HPFYLFQAVS VLIWLCDSFV FYSCCIVFIS SYSIFLSVKE
SKESENRIHS IIGAPQPVTV IRNQVKQTVL ADDLVIGDLL YFSNLDLKTC PVDGILFSSS
CLLDESMVTG ESVPARKFPL EDNSLDSWMI ASCNIFSPHL IHAGTKFLKI DSTPSTPCLI
SVVRTGFRSN KGQLIRNLLY PNLRPSQLYL DSMSFLKTMA ILSFVSIVFI AIYLNLYNAS
FGHVVLRSLD VLTILVPPAL PATLSVGIAN SIARLSRALI YTTSPESIHN AGCLSTFVFD
KTGTLTENSV QLSCVYVKSG SNGLLKQVDA DSLSLDSTKL NAHAYRVATC SQSLELVGNE
LVGDPLEVTL FTQFNGTFCA TIRASNTPHP PLFSVSNSFD GPSQIFSIYK ALEFDPVLRR
MSVICSTSTE RSLMLFTKGA PESILAISSQ QSIPSNVQEV IHTLSSKGFR IIAFASKNLI
TPLQELIHLS RSTLESNVTF QGLFVLESPL RESSKDVISS LLRSKMEVSI CSGDSLFTSV
FVAKHCGALD SCNFIYTAEL ADSGDDCPQI HFEKIDLQTQ NFQPIPDGFS LKDVILEKDS
SLCMDGKLLQ RLLTMLSFNE IKILLSKLRV LARMSPFDKA TYVELCQKYG CKVGFCGDGA
NDCIALKQAD VGVSLSDSEA CAAASFVSKK KSIKDVFNVL LEGRCSLILS HRCFQYMVLC
AIVQFSGVFF LYLKNYNFND NQFLFMDLLI IFPLSAAMSY FDPAQNLTSN RPNSTLFGKG
RVKDLGIQSV LIWLSHGLLT LILHELNWVE LPEWQLEKSN TKNVLVTSIF LLSSLQYLGI
CIGINQSSEF LSPIWKKKTY VCLCTTIGLC NIYLCFANEN HIISRCLQIT RLPTLYRFII
LFMGVISCCL TSILNM
