Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytochrome c-2

Gene

Cyt-c-p

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei19 – 191Heme (covalent)
Binding sitei22 – 221Heme (covalent)
Metal bindingi23 – 231Iron (heme axial ligand)
Metal bindingi85 – 851Iron (heme axial ligand)

GO - Molecular functioni

  1. electron carrier activity Source: FlyBase
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. mitochondrial electron transport, cytochrome c to oxygen Source: GO_Central
  2. mitochondrial electron transport, ubiquinol to cytochrome c Source: GO_Central
  3. oxidation-reduction process Source: UniProtKB
  4. oxidative phosphorylation Source: FlyBase
  5. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_275948. Formation of apoptosome.
REACT_278657. Detoxification of Reactive Oxygen Species.
REACT_327866. Orphan transporters.
REACT_342103. Respiratory electron transport.
REACT_345277. Activation of caspases through apoptosome-mediated cleavage.
REACT_353797. Transcriptional activation of mitochondrial biogenesis.
REACT_354694. Release of apoptotic factors from the mitochondria.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c-2
Alternative name(s):
Cytochrome c-proximal
Gene namesi
Name:Cyt-c-p
Synonyms:CYTC2, DC4
ORF Names:CG17903
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000409. Cyt-c-p.

Subcellular locationi

Mitochondrion intermembrane space 1 Publication
Note: Loosely associated with the inner membrane.

GO - Cellular componenti

  1. cytosol Source: FlyBase
  2. mitochondrial inner membrane Source: FlyBase
  3. mitochondrial intermembrane space Source: GO_Central
  4. mitochondrion Source: FlyBase
  5. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 108107Cytochrome c-2PRO_0000108261Add
BLAST

Post-translational modificationi

Binds 1 heme group per subunit.

Proteomic databases

PaxDbiP84029.
PRIDEiP84029.

Expressioni

Developmental stagei

Expressed at varying, but relatively high levels throughout development.1 Publication

Gene expression databases

BgeeiP84029.
ExpressionAtlasiP84029. differential.

Interactioni

Protein-protein interaction databases

BioGridi61003. 37 interactions.
IntActiP84029. 2 interactions.
MINTiMINT-305906.

Structurei

3D structure databases

SMRiP84029. Positions 6-107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome c family.Curated

Phylogenomic databases

eggNOGiCOG3474.
InParanoidiP84029.
KOiK08738.
OMAiRDYLHNP.
OrthoDBiEOG761BWX.
PhylomeDBiP84029.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
[Graphical view]
PANTHERiPTHR11961. PTHR11961. 1 hit.
PfamiPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSiPR00604. CYTCHRMECIAB.
SUPFAMiSSF46626. SSF46626. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P84029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVPAGDVEK GKKLFVQRCA QCHTVEAGGK HKVGPNLHGL IGRKTGQAAG
60 70 80 90 100
FAYTDANKAK GITWNEDTLF EYLENPKKYI PGTKMIFAGL KKPNERGDLI

AYLKSATK
Length:108
Mass (Da):11,735
Last modified:January 23, 2007 - v2
Checksum:i535FFBAF282D20D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01760 Genomic DNA. Translation: CAA25900.1.
M11381 Genomic DNA. Translation: AAA28437.1.
AE014134 Genomic DNA. Translation: AAF53554.1.
AY071701 mRNA. Translation: AAL49323.1.
PIRiA22945. CCFFDM.
RefSeqiNP_001285984.1. NM_001299055.1.
NP_477176.1. NM_057828.4.
UniGeneiDm.4850.

Genome annotation databases

EnsemblMetazoaiFBtr0080889; FBpp0080446; FBgn0000409.
FBtr0344849; FBpp0311164; FBgn0000409.
GeneIDi34996.
KEGGidme:Dmel_CG17903.

Cross-referencesi

Web resourcesi

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01760 Genomic DNA. Translation: CAA25900.1.
M11381 Genomic DNA. Translation: AAA28437.1.
AE014134 Genomic DNA. Translation: AAF53554.1.
AY071701 mRNA. Translation: AAL49323.1.
PIRiA22945. CCFFDM.
RefSeqiNP_001285984.1. NM_001299055.1.
NP_477176.1. NM_057828.4.
UniGeneiDm.4850.

3D structure databases

SMRiP84029. Positions 6-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61003. 37 interactions.
IntActiP84029. 2 interactions.
MINTiMINT-305906.

Proteomic databases

PaxDbiP84029.
PRIDEiP84029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080889; FBpp0080446; FBgn0000409.
FBtr0344849; FBpp0311164; FBgn0000409.
GeneIDi34996.
KEGGidme:Dmel_CG17903.

Organism-specific databases

CTDi34996.
FlyBaseiFBgn0000409. Cyt-c-p.

Phylogenomic databases

eggNOGiCOG3474.
InParanoidiP84029.
KOiK08738.
OMAiRDYLHNP.
OrthoDBiEOG761BWX.
PhylomeDBiP84029.

Enzyme and pathway databases

ReactomeiREACT_275948. Formation of apoptosome.
REACT_278657. Detoxification of Reactive Oxygen Species.
REACT_327866. Orphan transporters.
REACT_342103. Respiratory electron transport.
REACT_345277. Activation of caspases through apoptosome-mediated cleavage.
REACT_353797. Transcriptional activation of mitochondrial biogenesis.
REACT_354694. Release of apoptotic factors from the mitochondria.

Miscellaneous databases

GenomeRNAii34996.
NextBioi791302.
PROiP84029.

Gene expression databases

BgeeiP84029.
ExpressionAtlasiP84029. differential.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR002327. Cyt_c_1A/1B.
[Graphical view]
PANTHERiPTHR11961. PTHR11961. 1 hit.
PfamiPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PRINTSiPR00604. CYTCHRMECIAB.
SUPFAMiSSF46626. SSF46626. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of two Drosophila melanogaster cytochrome c genes and their transcripts."
    Limbach K.J., Wu R.
    Nucleic Acids Res. 13:631-644(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE.
  2. "Developmental expression of nuclear genes that encode mitochondrial proteins: insect cytochromes c."
    Swanson M.S., Zieminn S.M., Miller D.D., Garber E.A.E., Margoliash E.
    Proc. Natl. Acad. Sci. U.S.A. 82:1964-1968(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "Developmental variation and amino acid sequences of cytochromes c of the fruit fly Drosophila melanogaster and the flesh fly Boettcherisca peregrina."
    Inoue S., Inoue H., Hiroyoshi T., Matsubara H., Yamanaka T.
    J. Biochem. 100:955-965(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-108.

Entry informationi

Entry nameiCYC2_DROME
AccessioniPrimary (citable) accession number: P84029
Secondary accession number(s): P00033, P00034, Q9VJJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

There are two cytochrome C genes in Drosophila: Cyt-c-d (distal) and Cyt-c-p (proximal).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.