ATU2_SCHPO
ID ATU2_SCHPO Reviewed; 904 AA.
AC O59666;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Copper-transporting ATPase ccc2;
DE EC=7.2.2.8;
DE AltName: Full=Cu(2+)-ATPase;
GN Name=ccc2; ORFNames=SPBC29A3.01;
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).
CC -!- FUNCTION: Probably involved in copper transport and in the regulation
CC of cellular copper level. Retrieves copper from the metallochaperone
CC atx1 and incorporates it into trans-Golgi vesicles (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB 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; CU329671; CAA18378.1; -; Genomic_DNA.
DR PIR; T40072; T40072.
DR RefSeq; NP_595829.1; NM_001021733.2.
DR AlphaFoldDB; O59666; -.
DR SMR; O59666; -.
DR BioGRID; 277053; 2.
DR STRING; 4896.SPBC29A3.01.1; -.
DR TCDB; 3.A.3.5.29; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; O59666; -.
DR MaxQB; O59666; -.
DR PaxDb; O59666; -.
DR PRIDE; O59666; -.
DR EnsemblFungi; SPBC29A3.01.1; SPBC29A3.01.1:pep; SPBC29A3.01.
DR GeneID; 2540525; -.
DR KEGG; spo:SPBC29A3.01; -.
DR PomBase; SPBC29A3.01; ccc2.
DR VEuPathDB; FungiDB:SPBC29A3.01; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR InParanoid; O59666; -.
DR OMA; ITFFGWM; -.
DR PhylomeDB; O59666; -.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:O59666; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; ISS:PomBase.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; ISO:PomBase.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0006878; P:cellular copper ion homeostasis; TAS:PomBase.
DR GO; GO:0060003; P:copper ion export; ISO:PomBase.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 1.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Copper; Copper transport; Golgi apparatus; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..904
FT /note="Copper-transporting ATPase ccc2"
FT /id="PRO_0000314753"
FT TOPO_DOM 1..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..197
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..278
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250"
FT TRANSMEM 279..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..469
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 806..826
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 827..828
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 850..904
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 529
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 742
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 904 AA; 97895 MW; 546EE3C8AAECE146 CRC64;
MYTTTLSVQG MTCTSCVASI QSMLEGVEGI EQFTISLLLE RAIAVHDPSI ISPDQIAEKI
EDCGFDASVI SSTEGEHGVM ANYLLLSPMQ AEQWTKVHNH INELQGVLSV NCSSSPDAAI
RVIYDSEITG PRSIMKEILS MGVKCTFQPV DSSTSRILSL QRGSQIRVWK IRFIISISFS
LAVMFLPQIF DSCDSMRAAF LVPHYFGICA GHIISLVLSL PVQFGVGRVY YSAAYHALKR
GTANMDVLVS LGSTVAFAAS IFFMILYSAR HADNPAPIFF DTADMLLTFV TLGRYLESKA
KGSTSAALSQ LLSLAPSSAT IIEDNEQIEI LADLIERGDL ILVKPGEIIP VDGTVVEGSS
YVDESSVSGE PVPVHKTIDD ELLSGTANGN GRLLVKATKS PRESQLAVIV DLVQRAQISH
APIQQFADRV AGIFVPVIVA LSISTFTFWF LFTKYSSKYP SVFDDPMGKF AVCLKLTISV
VVVACPCALG LSTPTAVMVG TGVGALNGII IKGGEILERL NQVDTVVFDK TGTLTVGKLS
VTDISIVDNL EELLDIPKNI FWAFVKASES SSEHPIGKAI TEKASEFTDV SEIGIESFNA
VPGEGVDVVL RWKERTFHAL LGNSLLLEHN NVSIPDDFDS KLKLSSSSGL TCVRIAIDGQ
FVGFLGCMDQ VRPDSYQTVS ALKQLGKKVC LLTGDQKATA RRVAQGLEID FSDVYAEAVP
SQKAEIIQKL KDQKHCVAMV GDGINDSPSL VLADVGIAPI NGSGIALESA DVILVRKGVL
LDTAVSFDLS RVIVKRIKMN LVWACIYNFV MIPIAMGFFL PWGIYLNPMW ASAAMMFSSL
SVLASSLLLR RWKKPKSLIF SEADDVETES STNSSVLQKV YTATRSIFGR NKSSNKYQPV
ANEV
