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Reviewed, UniProtKB/Swiss-Prot P30405 (PPIF_HUMAN)

Last modified July 7, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase, mitochondrial
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin F
Gene names
Name: PPIF
Synonyms: CYP3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmembrane fraction Ref.1

Traceable author statement. Source: ProtInc

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Potential
Chain30 – 207178Peptidyl-prolyl cis-trans isomerase, mitochondrial
PRO_0000025489

Regions

Domain49 – 205157PPIase cyclophilin-type

Secondary structure

.............................. 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30405-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: D7C76F1D4049F16A

FASTA20722,040
        10         20         30         40         50         60 
MLALRCGSRW LGLLSVPRSV PLRLPAARAC SKGSGDPSSS SSSGNPLVYL DVDANGKPLG 

        70         80         90        100        110        120 
RVVLELKADV VPKTAENFRA LCTGEKGFGY KGSTFHRVIP SFMCQAGDFT NHNGTGGKSI 

       130        140        150        160        170        180 
YGSRFPDENF TLKHVGPGVL SMANAGPNTN GSQFFICTIK TDWLDGKHVV FGHVKEGMDV 

       190        200 
VKKIESFGSK SGRTSKKIVI TDCGQLS 

« Hide

References

« Hide 'large scale' references
[1]"The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms."
Bergsma D.J., Eder C., Gross M., Kersten H., Sylvester D., Appelbaum E., Cusimano D., Livi G.P., McLauglin M.M., Kasyan K., Porter T.G., Silverman C., Dunnington D., Hand A., Prichett W.P., Bossard M.J., Brandt M., Levy M.A.
J. Biol. Chem. 266:23204-23214(1991) [PubMed: 1744118] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed: 15164054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

M80254 mRNA. Translation: AAA58434.1.
AL133481, AL391665 Genomic DNA. Translation: CAH72725.1.
AL391665, AL133481 Genomic DNA. Translation: CAI40994.1.
BC005020 mRNA. Translation: AAH05020.1.
IPIIPI00026519.
PIRA41581.
RefSeqNP_005720.1.
UniGeneHs.381072

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2BITX-ray1.71X43-207[»]
2BIUX-ray1.71X43-207[»]
2Z6WX-ray0.96A/B44-207[»]
ModBaseSearch...

PTM databases

PhosphoSiteP30405.

2-D gel databases

OGPP30405.

Proteomic databases

PeptideAtlasP30405.
PRIDEP30405.

Genome annotation databases

EnsemblENSG00000108179. Homo sapiens. [Contig view]
GeneID10105.
KEGGhsa:10105.
UCSCuc001kai.1. human.

Organism-specific databases

GeneCardsGC10P080777.
HGNCHGNC:9259. PPIF.
MIM604486. gene.
PharmGKBPA33584.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP30405.
HOVERGENP30405.
OMAP30405. PAGRVEM.

Enzyme and pathway databases

BRENDA5.2.1.8. 247.

Gene expression databases

ArrayExpressP30405.
BgeeP30405.
CleanExHS_PPIF.
GermOnlineENSG00000108179. Homo sapiens.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01093. Dimethyl sulfoxide.
DB00172. L-Proline.
NextBio38221.
SOURCESearch...

Entry information

Entry namePPIF_HUMAN
AccessionPrimary (citable) accession number: P30405
Secondary accession number(s): Q5W131
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 7, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents