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Protein

Copper-transporting ATPase ccc2

Gene

ccc2

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

Functioni

Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone atx1 and incorporates it into trans-Golgi vesicles (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13CopperPROSITE-ProRule annotation1
Metal bindingi16CopperPROSITE-ProRule annotation1
Active sitei5294-aspartylphosphate intermediateBy similarity1
Metal bindingi742MagnesiumPROSITE-ProRule annotation1
Metal bindingi746MagnesiumPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • cellular copper ion homeostasis Source: PomBase
  • copper ion export Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Copper, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-936837. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.5.29. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-transporting ATPase ccc2 (EC:3.6.3.54)
Alternative name(s):
Cu(2+)-ATPase
Gene namesi
Name:ccc2
ORF Names:SPBC29A3.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC29A3.01.
PomBaseiSPBC29A3.01. ccc2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 172CytoplasmicBy similarityAdd BLAST172
Transmembranei173 – 193HelicalSequence analysisAdd BLAST21
Topological domaini194 – 197Lumenal, vesicleBy similarity4
Transmembranei198 – 218HelicalSequence analysisAdd BLAST21
Topological domaini219 – 246CytoplasmicBy similarityAdd BLAST28
Transmembranei247 – 267HelicalSequence analysisAdd BLAST21
Topological domaini268 – 278Lumenal, vesicleBy similarityAdd BLAST11
Transmembranei279 – 296HelicalSequence analysisAdd BLAST18
Topological domaini297 – 431CytoplasmicBy similarityAdd BLAST135
Transmembranei432 – 452HelicalSequence analysisAdd BLAST21
Topological domaini453 – 469Lumenal, vesicleBy similarityAdd BLAST17
Transmembranei470 – 490HelicalSequence analysisAdd BLAST21
Topological domaini491 – 805CytoplasmicBy similarityAdd BLAST315
Transmembranei806 – 826HelicalSequence analysisAdd BLAST21
Topological domaini827 – 828Lumenal, vesicleBy similarity2
Transmembranei829 – 849HelicalSequence analysisAdd BLAST21
Topological domaini850 – 904CytoplasmicBy similarityAdd BLAST55

GO - Cellular componenti

  • fungal-type vacuole membrane Source: PomBase
  • Golgi apparatus Source: PomBase
  • Golgi membrane Source: PomBase
  • integral component of plasma membrane Source: GO_Central
  • intracellular membrane-bounded organelle Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003147531 – 904Copper-transporting ATPase ccc2Add BLAST904

Proteomic databases

MaxQBiO59666.
PRIDEiO59666.

Interactioni

Protein-protein interaction databases

MINTiMINT-4675293.

Structurei

3D structure databases

ProteinModelPortaliO59666.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 69HMAPROSITE-ProRule annotationAdd BLAST67

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi480 – 483Poly-Val4
Compositional biasi645 – 648Poly-Ser4

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000250397.
InParanoidiO59666.
KOiK17686.
OMAiMPGYNWI.
OrthoDBiEOG092C0DN9.
PhylomeDBiO59666.

Family and domain databases

CDDicd00371. HMA. 1 hit.
Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59666-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYTTTLSVQG MTCTSCVASI QSMLEGVEGI EQFTISLLLE RAIAVHDPSI
60 70 80 90 100
ISPDQIAEKI EDCGFDASVI SSTEGEHGVM ANYLLLSPMQ AEQWTKVHNH
110 120 130 140 150
INELQGVLSV NCSSSPDAAI RVIYDSEITG PRSIMKEILS MGVKCTFQPV
160 170 180 190 200
DSSTSRILSL QRGSQIRVWK IRFIISISFS LAVMFLPQIF DSCDSMRAAF
210 220 230 240 250
LVPHYFGICA GHIISLVLSL PVQFGVGRVY YSAAYHALKR GTANMDVLVS
260 270 280 290 300
LGSTVAFAAS IFFMILYSAR HADNPAPIFF DTADMLLTFV TLGRYLESKA
310 320 330 340 350
KGSTSAALSQ LLSLAPSSAT IIEDNEQIEI LADLIERGDL ILVKPGEIIP
360 370 380 390 400
VDGTVVEGSS YVDESSVSGE PVPVHKTIDD ELLSGTANGN GRLLVKATKS
410 420 430 440 450
PRESQLAVIV DLVQRAQISH APIQQFADRV AGIFVPVIVA LSISTFTFWF
460 470 480 490 500
LFTKYSSKYP SVFDDPMGKF AVCLKLTISV VVVACPCALG LSTPTAVMVG
510 520 530 540 550
TGVGALNGII IKGGEILERL NQVDTVVFDK TGTLTVGKLS VTDISIVDNL
560 570 580 590 600
EELLDIPKNI FWAFVKASES SSEHPIGKAI TEKASEFTDV SEIGIESFNA
610 620 630 640 650
VPGEGVDVVL RWKERTFHAL LGNSLLLEHN NVSIPDDFDS KLKLSSSSGL
660 670 680 690 700
TCVRIAIDGQ FVGFLGCMDQ VRPDSYQTVS ALKQLGKKVC LLTGDQKATA
710 720 730 740 750
RRVAQGLEID FSDVYAEAVP SQKAEIIQKL KDQKHCVAMV GDGINDSPSL
760 770 780 790 800
VLADVGIAPI NGSGIALESA DVILVRKGVL LDTAVSFDLS RVIVKRIKMN
810 820 830 840 850
LVWACIYNFV MIPIAMGFFL PWGIYLNPMW ASAAMMFSSL SVLASSLLLR
860 870 880 890 900
RWKKPKSLIF SEADDVETES STNSSVLQKV YTATRSIFGR NKSSNKYQPV

ANEV
Length:904
Mass (Da):97,895
Last modified:August 1, 1998 - v1
Checksum:i546EE3C8AAECE146
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18378.1.
PIRiT40072.
RefSeqiNP_595829.1. NM_001021733.2.

Genome annotation databases

EnsemblFungiiSPBC29A3.01.1; SPBC29A3.01.1:pep; SPBC29A3.01.
GeneIDi2540525.
KEGGispo:SPBC29A3.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18378.1.
PIRiT40072.
RefSeqiNP_595829.1. NM_001021733.2.

3D structure databases

ProteinModelPortaliO59666.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4675293.

Protein family/group databases

TCDBi3.A.3.5.29. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBiO59666.
PRIDEiO59666.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC29A3.01.1; SPBC29A3.01.1:pep; SPBC29A3.01.
GeneIDi2540525.
KEGGispo:SPBC29A3.01.

Organism-specific databases

EuPathDBiFungiDB:SPBC29A3.01.
PomBaseiSPBC29A3.01. ccc2.

Phylogenomic databases

HOGENOMiHOG000250397.
InParanoidiO59666.
KOiK17686.
OMAiMPGYNWI.
OrthoDBiEOG092C0DN9.
PhylomeDBiO59666.

Enzyme and pathway databases

ReactomeiR-SPO-936837. Ion transport by P-type ATPases.

Miscellaneous databases

PROiO59666.

Family and domain databases

CDDicd00371. HMA. 1 hit.
Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATU2_SCHPO
AccessioniPrimary (citable) accession number: O59666
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 127 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.