[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Pancreas; PubMed=8509368 [NCBI, ExPASy, EBI, Israel, Japan] Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E., Bayney R.M.; "Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization."; J. Biol. Chem. 268:12303-12310(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Placenta; DOI=10.1006/geno.1996.0384; PubMed=8812478 [NCBI, ExPASy, EBI, Israel, Japan] Yokoi H., Shimizu Y., Anazawa H., Lefebvre C.A., Korneluk R.G., Ikeda J.E.; "The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene."; Genomics 35:448-455(1996).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-49; ILE-302 AND GLU-335. NIEHS SNPs program; Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; 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).
[5]	PROTEIN SEQUENCE OF 2-17. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[6]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

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).
ENZYME REGULATION: Less sensitive to inhibition by cyclosporin A than is CYP-18.
SUBUNIT: Binds ESR1 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Widely expressed.
SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.
SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
SIMILARITY: Contains 3 TPR repeats.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ppid/";.
WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry; URL="http://en.wikipedia.org/wiki/Cyclophilin";.

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

L11667; AAA35731.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D63861; BAA09923.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY714221; AAT97986.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030707; AAH30707.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00003927; -.

A45981; A45981.

NP_005029.1; -.

3D structure databases

HSSP

P26882; 1IHG. [HSSP ENTRY / PDB]

SMR

Q08752; 2-365.

ModBase

Q08752.

Protein-protein interaction databases

IntAct

Q08752; 3.

PTM databases

PhosphoSite

Q08752; -.

Enzyme and pathway databases

BRENDA

5.2.1.8; 247.

2D gel databases

REPRODUCTION-2DPAGE

IPI00003927; -.

Organism-specific databases

GC04M159849; -.

HIX0004599; -.

HGNC:9257; PPID.

601753; gene. [NCBI / EBI]

PharmGKB

PA33582; -.

Gene expression databases

Q08752; -.

Q08752; -.

HS_PPID; -.

ENSG00000171497; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016018;	Molecular function: cyclosporin A binding (traceable author statement from UniProtKB).
GO:0031072;	Molecular function: heat shock protein binding (inferred from physical interaction from UniProtKB).
GO:0003755;	Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006457;	Biological process: protein folding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002130; PPIase_cyclophilin.
IPR001440; TPR-1.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
IPR019734; TPR_repeat.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
G3DSA:1.25.40.10; TPR-like_helical; 1.

Pfam

PF00160; Pro_isomerase; 1.
PF00515; TPR_1; 2.
Pfam graphical view of domain structure.

PRINTS

PR00153; CSAPPISMRASE.

SMART

SM00028; TPR; 3.
SMART graphical view of domain structure.

PROSITE

PS00170; CSA_PPIASE_1; 1.
PS50072; CSA_PPIASE_2; 1.
PS50005; TPR; 3.
PS50293; TPR_REGION; 2.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

Q08752; -.

PRIDE

Q08752; -.

Genome annotation databases

Ensembl

ENSG00000171497; Homo sapiens. [Contig view]

GeneID

5481; -.

KEGG

hsa:5481; -.

Phylogenomic databases

HOGENOM

Q08752; -.

HOVERGEN

Q08752; -.

OMA

Q08752; IYAKMFA.

Other

21218; -.

PPID; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cyclosporin; Cytoplasm; Direct protein sequencing; Isomerase; Polymorphism; Repeat; Rotamase; TPR repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 370`	`369`	`40 kDa peptidyl-prolyl cis-trans isomerase.`	`PRO_0000064153`
`DOMAIN`	`19 183`	`165`	`PPIase cyclophilin-type.`
`REPEAT`	`223 256`	`34`	`TPR 1.`
`REPEAT`	`273 306`	`34`	`TPR 2.`
`REPEAT`	`307 340`	`34`	`TPR 3.`
`VARIANT`	`49 49`	`1`	`R -> C (in dbSNP:rs2070631 [NCBI]).`	`VAR_021021 [3D]`
`VARIANT`	`196 196`	`1`	`D -> V (in dbSNP:rs2230222 [NCBI]).`	`VAR_051771 [3D]`
`VARIANT`	`302 302`	`1`	`L -> I.`	`VAR_021022 [3D]`
`VARIANT`	`335 335`	`1`	`G -> E (in dbSNP:rs17843956 [NCBI]).`	`VAR_021023 [3D]`

Sequence information

Length: 370 AA [This is the length of the unprocessed precursor]

Molecular weight: 40764 Da [This is the MW of the unprocessed precursor]

CRC64: 39D4100748B35D48 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGH 

        70         80         90        100        110        120 
TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDREGLLSM 

       130        140        150        160        170        180 
ANAGRNTNGS QFFITTVPTP HLDGKHVVFG QVIKGIGVAR ILENVEVKGE KPAKLCVIAE 

       190        200        210        220        230        240 
CGELKEGDDG GIFPKDGSGD SHPDFPEDAD IDLKDVDKIL LITEDLKNIG NTFFKSQNWE 

       250        260        270        280        290        300 
MAIKKYAEVL RYVDSSKAVI ETADRAKLQP IALSCVLNIG ACKLKMSNWQ GAIDSCLEAL 

       310        320        330        340        350        360 
ELDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQGIAPED KAIQAELLKV KQKIKAQKDK 

       370 
EKAVYAKMFA

Q08752 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools