Protein CCC1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P47818 (CCC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein CCC1

Alternative name(s):
Cross-complementer of CSG1 protein 1

Gene names

Name:	CCC1
Ordered Locus Names:	YLR220W
ORF Names:	L8083.6

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a role in both calcium and manganese homeostasis. Involved in the transfer of iron and Mn²⁺ from the cytosol to the vacuole for storage of these metals. Ref.5 Ref.6 Ref.8
Subcellular location	Golgi apparatus membrane. Vacuole membrane; Multi-pass membrane protein Potential Ref.6 Ref.8 Ref.10.
Induction	Down-regulated under iron starvation by TIS11. Transcriptionally up-regulated by YAP5 in response to increased cytosolic iron. Ref.14 Ref.19
Disruption phenotype	Deletion causes an increase in metal sensitivity at 15 mM manganese, but does not affect invertase glycosylation. Deletion shows increased sensitivity to external iron, which is suppressed by MRS3 or MRS4 overexpression requiring oxygen but not respiration, and exacerbated by ectopic expression of the iron transporter FET4. Deletion also results in decreased vacuolar iron content and decreased iron stores, which affect cytosolic iron levels and cell growth. Deletion together with MRS3 and MRS4 restores cellular and mitochondrial iron homeostasis to near normal level, corrects the MRS3 and MRS4 double deletion phenotype (which shows increased resistance to cobalt but decreased resistance to copper and cadmium), and has near normal levels of aconitase activity. When overexpressed, maintains respiratory function in a YFH1 deletion mutant regardless of extracellular iron concentration, activates the iron-dependent transcription factor AFT1 resulting in an increase in iron uptake, cytosolic iron accumulation and a change in copper metabolism. Overexpression prevents excessive mitochondrial iron accumulation by limiting mitochondrial iron uptake and results in increased expression of the high affinity iron transport system composed of FET3 and FTR1. Overexpression also suppresses the rapamycin-resistant phenotype of PMR1 deletion mutant. Ref.6
Miscellaneous	Present with 2840 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the CCC1 family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Golgi apparatus Membrane Vacuole
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular calcium ion homeostasis Inferred from mutant phenotype Ref.1. Source: SGD cellular iron ion homeostasis Inferred from genetic interaction Ref.7. Source: SGD cellular manganese ion homeostasis Inferred from genetic interaction Ref.6. Source: SGD
Cellular_component	Golgi apparatus Inferred from direct assay Ref.6. Source: SGD Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell fungal-type vacuole membrane Inferred from direct assay Ref.8 PubMed 22842922. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD
Molecular_function	ferrous iron transmembrane transporter activity Inferred from mutant phenotype Ref.8. Source: SGD manganese ion transmembrane transporter activity Inferred from mutant phenotype Ref.8. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ECM4	P36156	1	EBI-2048372,EBI-2042717

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 322

322

Protein CCC1

PRO_0000089394

Regions

Topological domain

1 – 99

Cytoplasmic Potential

Transmembrane

100 – 120

Helical; Potential

Topological domain

121 – 129

Vacuolar Potential

Transmembrane

130 – 150

Helical; Potential

Topological domain

151 – 236

Cytoplasmic Potential

Transmembrane

237 – 257

Helical; Potential

Topological domain

258 – 259

Vacuolar Potential

Transmembrane

260 – 280

Helical; Potential

Topological domain

281 – 300

Cytoplasmic Potential

Transmembrane

301 – 321

Helical; Potential

Topological domain

322

Vacuolar Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.20

Modified residue

Phosphothreonine Ref.12

Modified residue

Phosphoserine Ref.9 Ref.20

Modified residue

Phosphoserine Ref.18

Modified residue

Phosphoserine Ref.18 Ref.20

Modified residue

Phosphoserine Ref.9 Ref.18 Ref.20

Modified residue

Phosphoserine Ref.18 Ref.20

Modified residue

Phosphoserine Ref.18 Ref.20

Modified residue

Phosphoserine Ref.18 Ref.20

Modified residue

Phosphoserine Ref.17 Ref.18 Ref.20

Sequences

Sequence

Length

Mass (Da)

Tools

P47818 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 374081A49F0C43D1
Show »

FASTA

322

34,250

        10         20         30         40         50         60 
MSIVALKNAV VTLIQKAKGS GGTSELGGSE STPLLRGSNS NSSRHDNLSS SSSDIIYGRN 

        70         80         90        100        110        120 
SAQDLENSPM SVGKDNRNGD NGSDNEKANL GFFQSVDPRV ISDLIIGLSD GLTVPFALTA 

       130        140        150        160        170        180 
GLSSLGDAKL VITGGFAELI SGAISMGLGG YLGAKSESDY YHAEVKKEKR KFYDNSNLIN 

       190        200        210        220        230        240 
REIEDILLEI NPNFSDETIV SFIKDLQRTP ELMVDFIIRY GRGLDEPAEN RELISAVTIG 

       250        260        270        280        290        300 
GGYLLGGLVP LVPYFFVSDV GTGLIYSIIV MVVTLFWFGY VKTKLSMGSG SSTSKKVTEG 

       310        320 
VEMVVVGGVA AGAAWFFVKL LG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence, mapping and disruption of CCC1, a gene that cross-complements the Ca(2+)-sensitive phenotype of csg1 mutants." Fu D., Beeler T.J., Dunn T.M. Yeast 10:515-521(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The product of HUM1, a novel yeast gene, is required for vacuolar Ca2+/H+ exchange and is related to mammalian Na+/Ca2+ exchangers." Pozos T.C., Sekler I., Cyert M.S. Mol. Cell. Biol. 16:3730-3741(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: S288c / YPH1.
[6]	"The role of the Saccharomyces cerevisiae CCC1 gene in the homeostasis of manganese ions." Lapinskas P.J., Lin S.-J., Culotta V.C. Mol. Microbiol. 21:519-528(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[7]	"CCC1 suppresses mitochondrial damage in the yeast model of Friedreich's ataxia by limiting mitochondrial iron accumulation." Chen O.S., Kaplan J. J. Biol. Chem. 275:7626-7632(2000) [PubMed] [Europe PMC] [Abstract] Cited for: OVEREXPRESSION PHENOTYPE.
[8]	"CCC1 is a transporter that mediates vacuolar iron storage in yeast." Li L., Chen O.S., McVey Ward D., Kaplan J. J. Biol. Chem. 276:29515-29519(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF DELETION MUTANT.
[9]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-52, MASS SPECTROMETRY. Strain: 2124.
[10]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, MASS SPECTROMETRY. Strain: SUB592.
[13]	"A mitochondrial-vacuolar signaling pathway in yeast that affects iron and copper metabolism." Li L., Kaplan J. J. Biol. Chem. 279:33653-33661(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF DELETION MUTANT.
[14]	"Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation." Puig S., Askeland E., Thiele D.J. Cell 120:99-110(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[15]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
[16]	"Golgi manganese transport is required for rapamycin signaling in Saccharomyces cerevisiae." Devasahayam G., Burke D.J., Sturgill T.W. Genetics 177:231-238(2007) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF OVEREXPRESSION.
[17]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Strain: ADR376.
[18]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-52; SER-53; SER-68; SER-71 AND SER-83, MASS SPECTROMETRY.
[19]	"Yap5 is an iron-responsive transcriptional activator that regulates vacuolar iron storage in yeast." Li L., Bagley D., Ward D.M., Kaplan J. Mol. Cell. Biol. 28:1326-1337(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[20]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-49; SER-51; SER-52; SER-53; SER-68; SER-71 AND SER-83, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L24112 mRNA. Translation: AAA62622.1. U14913 Genomic DNA. Translation: AAB67452.1. U19027 Genomic DNA. Translation: AAB67409.1. AY557952 Genomic DNA. Translation: AAS56278.1. BK006945 Genomic DNA. Translation: DAA09536.1.
PIR	S43453.
RefSeq	NP_013321.1. NM_001182107.1.
3D structure databases
ProteinModelPortal	P47818.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-782N.
STRING	4932.YLR220W.
Protein family/group databases
TCDB	2.A.89.1.1. vacuolar iron transporter (VIT) family.
Proteomic databases
PaxDb	P47818.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR220W; YLR220W; YLR220W.
GeneID	850917.
KEGG	sce:YLR220W.
Organism-specific databases
CYGD	YLR220w.
SGD	S000004210. CCC1.
Phylogenomic databases
eggNOG	COG1814.
HOGENOM	HOG000096548.
OMA	ITGGMAE.
OrthoDB	EOG4WQ4C4.
Gene expression databases
Genevestigator	P47818.
GermOnline	YLR220W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008217. DUF125_TM. [Graphical view]
Pfam	PF01988. VIT1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967332.

Entry information

Entry name

CCC1_YEAST

Accession

Primary (citable) accession number: P47818
Secondary accession number(s): D6VYM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents