P30405 (PPIF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Short name=PPIase F
EC=5.2.1.8

Alternative name(s):
Cyclophilin F
Rotamase F

Gene names

Name:	PPIF
Synonyms:	CYP3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Mitochondrion
Domain	Transit peptide
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane fraction Traceable author statement. Source: ProtInc mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

29

Mitochondrion Potential

Chain

30 – 207

178

Peptidyl-prolyl cis-trans isomerase F, mitochondrial

PRO_0000025489

Regions

Domain

49 – 205

157

PPIase cyclophilin-type

Amino acid modifications

Modified residue

167

1

N6-acetyllysine Ref.4

Secondary structure

1

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207

Helix Strand Turn

Details...

Beta strand

47 – 54

8

Beta strand

57 – 66

10

Turn

68 – 70

3

Helix

72 – 83

12

Turn

84 – 86

3

Beta strand

94 – 99

6

Turn

100 – 102

3

Beta strand

103 – 106

4

Turn

109 – 111

3

Beta strand

112 – 115

4

Beta strand

139 – 142

4

Beta strand

154 – 159

6

Helix

162 – 164

3

Turn

165 – 167

3

Beta strand

170 – 176

7

Helix

178 – 186

9

Beta strand

198 – 205

8

Sequences

	Sequence		Length	Mass (Da)
	P30405 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: D7C76F1D4049F16A	FASTA	207	22,040
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, MASS SPECTROMETRY.
[5]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M80254 mRNA. Translation: AAA58434.1.
AL133481, AL391665 Genomic DNA. Translation: CAH72725.1.
AL391665, AL133481 Genomic DNA. Translation: CAI40994.1.
BC005020 mRNA. Translation: AAH05020.1.

IPI

IPI00026519.

PIR

A41581.

RefSeq

NP_005720.1. NM_005729.3.

UniGene

Hs.381072.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BIT	X-ray	1.71	X	43-207	[»]
2BIU	X-ray	1.71	X	43-207	[»]
2Z6W	X-ray	0.96	A/B	44-207	[»]
3QYU	X-ray	1.54	A	44-207	[»]

ProteinModelPortal

P30405.

SMR

P30405. Positions 44-207.

ModBase

Search...

Protein-protein interaction databases

STRING

P30405.

PTM databases

PhosphoSite

P30405.

Polymorphism databases

DMDM

231968.

2D gel databases

OGP

P30405.

UCD-2DPAGE

P30405.

Proteomic databases

PeptideAtlas

P30405.

PRIDE

P30405.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000225174; ENSP00000225174; ENSG00000108179.

GeneID

10105.

KEGG

hsa:10105.

UCSC

uc001kai.1. human.

Organism-specific databases

CTD

10105.

GeneCards

GC10P081107.

H-InvDB

HIX0008969.

HGNC

HGNC:9259. PPIF.

MIM

604486. gene.

neXtProt

NX_P30405.

PharmGKB

PA33584.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05846.

GeneTree

ENSGT00530000062909.

HOGENOM

HBG610621.

HOVERGEN

HBG001065.

InParanoid

P30405.

OMA

RACSKGA.

OrthoDB

EOG4DJJXN.

PhylomeDB

P30405.

Gene expression databases

ArrayExpress

P30405.

Bgee

P30405.

CleanEx

HS_PPIF.

Genevestigator

P30405.

GermOnline

ENSG00000108179. Homo sapiens.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Gene3D

G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.

KO

K09565.

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PIRSF

PIRSF001467. Peptidylpro_ismrse. 1 hit.

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01093. Dimethyl sulfoxide.
DB00172. L-Proline.

NextBio

38221.

SOURCE

Search...

Entry information

Entry name

PPIF_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.