Q08752 (PPID_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase D
Short name=PPIase D
EC=5.2.1.8

Alternative name(s):
40 kDa peptidyl-prolyl cis-trans isomerase
Cyclophilin-40
Short name=CYP-40
Cyclophilin-related protein
Rotamase D

Gene names

Name:	PPID
Synonyms:	CYP40, CYPD

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	370 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).
Enzyme regulation	Less sensitive to inhibition by cyclosporin A than is CYP-18.
Subunit structure	Binds ESR1 By similarity.
Subcellular location	Cytoplasm.
Tissue specificity	Widely expressed.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. Contains 1 PPIase cyclophilin-type domain. Contains 3 TPR repeats.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat TPR repeat
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell intermediate filament cytoskeleton Inferred from direct assay. Source: HPA
Molecular function	cyclosporin A binding Traceable author statement. Source: UniProtKB heat shock protein binding Inferred from physical interaction. Source: UniProtKB 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
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 370	369	Peptidyl-prolyl cis-trans isomerase D		PRO_0000064153
Regions
	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
Amino acid modifications
	Modified residue	198	1	Phosphoserine Ref.8
Natural variations
	Natural variant	49	1	R → C. Ref.3 Corresponds to variant rs2070631 [ dbSNP | Ensembl ].		VAR_021021
	Natural variant	196	1	D → V. Corresponds to variant rs2230222 [ dbSNP | Ensembl ].		VAR_051771
	Natural variant	302	1	L → I. Ref.3 Corresponds to variant rs9410 [ dbSNP | Ensembl ].		VAR_021022
	Natural variant	335	1	G → E. Ref.3 Corresponds to variant rs17843956 [ dbSNP | Ensembl ].		VAR_021023

Sequences

	Sequence		Length	Mass (Da)
	Q08752 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 39D4100748B35D48	FASTA	370	40,764
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization." Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E., Bayney R.M. J. Biol. Chem. 268:12303-12310(1993) [PubMed: 8509368] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Pancreas.
[2]	"The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene." Yokoi H., Shimizu Y., Anazawa H., Lefebvre C.A., Korneluk R.G., Ikeda J.E. Genomics 35:448-455(1996) [PubMed: 8812478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[3]	NIEHS SNPs program Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-49; ILE-302 AND GLU-335.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Brain.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17. Tissue: Platelet.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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.

Web resources

NIEHS-SNPs

Wikipedia

Cyclophilin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	L11667 mRNA. Translation: AAA35731.1. D63861 Genomic DNA. Translation: BAA09923.1. AY714221 Genomic DNA. Translation: AAT97986.1. AK313929 mRNA. Translation: BAG36649.1. CH471056 Genomic DNA. Translation: EAX04853.1. BC030707 mRNA. Translation: AAH30707.1.
IPI	IPI00003927.
PIR	A45981.
RefSeq	NP_005029.1. NM_005038.2.
UniGene	Hs.183958.
3D structure databases
ProteinModelPortal	Q08752.
SMR	Q08752. Positions 2-365.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q08752. 2 interactions.
MINT	MINT-1399772.
STRING	Q08752.
PTM databases
PhosphoSite	Q08752.
Polymorphism databases
DMDM	729274.
2D gel databases
REPRODUCTION-2DPAGE	IPI00003927.
Proteomic databases
PeptideAtlas	Q08752.
PRIDE	Q08752.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307720; ENSP00000303754; ENSG00000171497.
GeneID	5481.
KEGG	hsa:5481.
UCSC	uc003iqc.1. human.
Organism-specific databases
CTD	5481.
GeneCards	GC04M159630.
H-InvDB	HIX0004599.
HGNC	HGNC:9257. PPID.
HPA	HPA019520. HPA019692.
MIM	601753. gene.
neXtProt	NX_Q08752.
PharmGKB	PA33582.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG610621.
HOVERGEN	HBG053654.
InParanoid	Q08752.
OMA	KGMGVVK.
OrthoDB	EOG4B2SXF.
PhylomeDB	Q08752.
Gene expression databases
ArrayExpress	Q08752.
Bgee	Q08752.
CleanEx	HS_PPID.
Genevestigator	Q08752.
GermOnline	ENSG00000171497. Homo sapiens.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. IPR023114. Elongated_TPR_rpt_dom. IPR001440. TPR-1. IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
Gene3D	G3DSA:1.10.150.160. Elongated_TPR_rpt_dom. 1 hit. G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit. G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
KO	K05864.
Pfam	PF00160. Pro_isomerase. 1 hit. PF00515. TPR_1. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SMART	SM00028. TPR. 3 hits. [Graphical view]
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. PS50005. TPR. 3 hits. PS50293. TPR_REGION. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	21218.
SOURCE	Search...

Entry information

Entry name

PPID_HUMAN

Accession

Primary (citable) accession number: Q08752
Secondary accession number(s): B2R9V2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 114 of the entry and version 3 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.