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UniProtKB/Swiss-Prot entry P30405


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PPIF_HUMAN
Primary accession number P30405
Secondary accession number Q5W131
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 78)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase, mitochondrial [Precursor]
Synonyms PPIase
Rotamase
EC 5.2.1.8
Cyclophilin F
Gene name
Name: PPIF
Synonyms: CYP3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1744118 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms.";
J. Biol. Chem. 266:23204-23214(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M80254; AAA58434.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133481; CAH72725.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391665; CAH72725.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391665; CAI40994.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133481; CAI40994.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005020; AAH05020.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41581; A41581.
RefSeq NP_005720.1; -.
UniGene Hs.381072
3D structure databases
PDB
2BIT; X-ray; 1.71 A; X=43-207.[ExPASy / RCSB / EBI]
2BIU; X-ray; 1.71 A; X=43-207.[ExPASy / RCSB / EBI]
2Z6W; X-ray; 0.96 A; A/B=44-207.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2BIT; -.
2BIU; -.
2Z6W; -.
ModBase P30405.
PTM databases
PhosphoSite P30405; -.
2D gel databases
OGP P30405; -.
Organism-specific databases
HGNC HGNC:9259; PPIF.
GenAtlas PPIF.
MIM 604486; gene. [NCBI / EBI]
PharmGKB PA33584; -.
GeneCards P30405.
Gene expression databases
ArrayExpress P30405; -.
CleanEx HS_PPIF; -.
GermOnline ENSG00000108179; Homo sapiens.
Ontologies
GO
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002130; PPIase_cyclophilin.
Graphical view of domain structure.
Gene3D G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
PANTHER PTHR11071; PPIase_cyclophilin; 1.
Pfam PF00160; Pro_isomerase; 1.
Pfam graphical view of domain structure.
PRINTS PR00153; CSAPPISMRASE.
PROSITE PS00170; CSA_PPIASE_1; 1.
PS50072; CSA_PPIASE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P30405.
Proteomic databases
PeptideAtlas P30405; -.
Genome annotation databases
Ensembl ENSG00000108179; Homo sapiens. [Contig view]
GeneID 10105; -.
KEGG hsa:10105; -.
Phylogenomic databases
HOGENOM P30405; -.
HOVERGEN P30405; -.
Other
DrugBank DB01093; Dimethyl sulfoxide.
DB00172; L-Proline.
LinkHub P30405; -.
SOURCE PPIF; Homo sapiens.
ProtoNet P30405.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cyclosporin; Isomerase; Mitochondrion; Rotamase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    29  29     Mitochondrion (Potential). 
CHAIN   30   207  178     Peptidyl-prolyl cis-trans isomerase, mitochondrial. PRO_0000025489
DOMAIN   49   205  157     PPIase cyclophilin-type. 
STRAND   47    54  8      
STRAND   57    66  10      
TURN   68    70  3      
HELIX   72    83  12      
TURN   84    86  3      
STRAND   94    99  6      
TURN   100   102  3      
STRAND   103   106  4      
TURN   109   111  3      
STRAND   112   115  4      
STRAND   120   123  4      
STRAND   139   142  4      
STRAND   150   152  3      
STRAND   154   159  6      
HELIX   162   164  3      
TURN   165   167  3      
STRAND   170   176  7      
HELIX   178   186  9      
STRAND   198   205  8      
Sequence information
Length: 207 AA [This is the length of the unprocessed precursor] Molecular weight: 22040 Da [This is the MW of the unprocessed precursor] CRC64: D7C76F1D4049F16A [This is a checksum on the sequence]
        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 

P30405 in FASTA format

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