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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

Cyp1

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

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

GO - Molecular functioni

GO - Biological processi

  • autophagic cell death Source: FlyBase
  • protein folding Source: FlyBase
  • regulation of protein kinase activity Source: GOC
  • salivary gland cell autophagic cell death Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Cyclophilin
Cyclosporin A-binding protein
Rotamase
Gene namesi
Name:Cyp1
Synonyms:Cyp-1
ORF Names:CG9916
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004432. Cyp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytosol Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • nuclear cyclin-dependent protein kinase holoenzyme complex Source: FlyBase
  • nucleus Source: FlyBase
  • positive transcription elongation factor complex b Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Peptidyl-prolyl cis-trans isomerasePRO_0000064123Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei158 – 1581Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP25007.
PRIDEiP25007.

PTM databases

iPTMnetiP25007.

Expressioni

Gene expression databases

BgeeiP25007.
ExpressionAtlasiP25007. differential.
GenevisibleiP25007. DM.

Interactioni

Protein-protein interaction databases

BioGridi58935. 29 interactions.
DIPiDIP-18774N.
IntActiP25007. 4 interactions.
MINTiMINT-768076.
STRINGi7227.FBpp0074017.

Structurei

3D structure databases

ProteinModelPortaliP25007.
SMRiP25007. Positions 67-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 226157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
InParanoidiP25007.
KOiK09565.
OMAiDMTADNE.
OrthoDBiEOG79GT7W.
PhylomeDBiP25007.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25007-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFCATLIR QFRHRSAAAF QIAESAILAN KSITLASSAC SVNRGQLQFG
60 70 80 90 100
IQIVREYSKA SKMSTLPRVF FDMTADNEPL GRIVMELRSD VVPKTAENFR
110 120 130 140 150
ALCTGEKGFG YKGSIFHRVI PNFMCQGGDF TNHNGTGGKS IYGNKFPDEN
160 170 180 190 200
FELKHTGSGI LSMANAGANT NGSQFFICTV KTAWLDNKHV VFGEVVEGLD
210 220
VVKKIESYGS QSGKTSKKII VANSGSL
Length:227
Mass (Da):24,666
Last modified:May 10, 2004 - v2
Checksum:iB6D832E1409C1F4D
GO

Sequence cautioni

The sequence AAB03701.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAQ22415.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF48589.2.
BT009946 mRNA. Translation: AAQ22415.1. Different initiation.
M62398 mRNA. Translation: AAB03701.1. Different initiation.
PIRiB38388.
RefSeqiNP_523366.2. NM_078642.4.
UniGeneiDm.6167.

Genome annotation databases

EnsemblMetazoaiFBtr0074238; FBpp0074017; FBgn0004432.
GeneIDi32595.
KEGGidme:Dmel_CG9916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF48589.2.
BT009946 mRNA. Translation: AAQ22415.1. Different initiation.
M62398 mRNA. Translation: AAB03701.1. Different initiation.
PIRiB38388.
RefSeqiNP_523366.2. NM_078642.4.
UniGeneiDm.6167.

3D structure databases

ProteinModelPortaliP25007.
SMRiP25007. Positions 67-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58935. 29 interactions.
DIPiDIP-18774N.
IntActiP25007. 4 interactions.
MINTiMINT-768076.
STRINGi7227.FBpp0074017.

PTM databases

iPTMnetiP25007.

Proteomic databases

PaxDbiP25007.
PRIDEiP25007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074238; FBpp0074017; FBgn0004432.
GeneIDi32595.
KEGGidme:Dmel_CG9916.

Organism-specific databases

CTDi32595.
FlyBaseiFBgn0004432. Cyp1.

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
InParanoidiP25007.
KOiK09565.
OMAiDMTADNE.
OrthoDBiEOG79GT7W.
PhylomeDBiP25007.

Miscellaneous databases

GenomeRNAii32595.
PROiP25007.

Gene expression databases

BgeeiP25007.
ExpressionAtlasiP25007. differential.
GenevisibleiP25007. DM.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-227.
    Strain: Berkeley.
    Tissue: Embryo.
  4. "The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins."
    Stamnes M.A., Shieh B.-H., Chuman L., Harris G.L., Zuker C.S.
    Cell 65:219-227(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-227.
  5. "Identification of Drosophila wing imaginal disc proteins by two-dimensional gel analysis and microsequencing."
    Santaren J.F., van Damme J., Puype M., Vandekerckhove J., Garcia-Bellido A.
    Exp. Cell Res. 206:220-226(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 69-82.
    Strain: Vallecas.
    Tissue: Wing imaginal disk.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiPPIA_DROME
AccessioniPrimary (citable) accession number: P25007
Secondary accession number(s): Q9VXH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: May 10, 2004
Last modified: June 8, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.