ID   PPID_HUMAN              Reviewed;         370 AA.
AC   Q08752; B2R9V2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-NOV-2009, entry version 94.
DE   RecName: Full=40 kDa peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            Short=Rotamase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-40;
DE            Short=CYP-40;
DE   AltName: Full=Cyclophilin-related protein;
GN   Name=PPID; Synonyms=CYP40, CYPD;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   MEDLINE=93286056; PubMed=8509368;
RA   Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E.,
RA   Bayney R.M.;
RT   "Cyclophilin-40, a protein with homology to the P59 component of the
RT   steroid receptor complex. Cloning of the cDNA and further
RT   characterization.";
RL   J. Biol. Chem. 268:12303-12310(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   MEDLINE=97001145; PubMed=8812478; DOI=10.1006/geno.1996.0384;
RA   Yokoi H., Shimizu Y., Anazawa H., Lefebvre C.A., Korneluk R.G.,
RA   Ikeda J.E.;
RT   "The structure and complete nucleotide sequence of the human
RT   cyclophilin 40 (PPID) gene.";
RL   Genomics 35:448-455(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-49; ILE-302 AND
RP   GLU-335.
RG   NIEHS SNPs program;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-17.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Less sensitive to inhibition by cyclosporin A
CC       than is CYP-18.
CC   -!- SUBUNIT: Binds ESR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC       D subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ppid/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry;
CC       URL="http://en.wikipedia.org/wiki/Cyclophilin";
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DR   EMBL; L11667; AAA35731.1; -; mRNA.
DR   EMBL; D63861; BAA09923.1; -; Genomic_DNA.
DR   EMBL; AY714221; AAT97986.1; -; Genomic_DNA.
DR   EMBL; AK313929; BAG36649.1; -; mRNA.
DR   EMBL; CH471056; EAX04853.1; -; Genomic_DNA.
DR   EMBL; BC030707; AAH30707.1; -; mRNA.
DR   IPI; IPI00003927; -.
DR   PIR; A45981; A45981.
DR   RefSeq; NP_005029.1; -.
DR   UniGene; Hs.155729; -.
DR   UniGene; Hs.581725; -.
DR   HSSP; P26882; 1IHG.
DR   SMR; Q08752; 2-365.
DR   IntAct; Q08752; 3.
DR   STRING; Q08752; -.
DR   PhosphoSite; Q08752; -.
DR   REPRODUCTION-2DPAGE; IPI00003927; -.
DR   PeptideAtlas; Q08752; -.
DR   PRIDE; Q08752; -.
DR   Ensembl; ENST00000307720; ENSP00000303754; ENSG00000171497; Homo sapiens.
DR   GeneID; 5481; -.
DR   KEGG; hsa:5481; -.
DR   UCSC; uc003iqc.1; human.
DR   CTD; 5481; -.
DR   GeneCards; GC04M159849; -.
DR   H-InvDB; HIX0004599; -.
DR   HGNC; HGNC:9257; PPID.
DR   HPA; HPA019520; -.
DR   HPA; HPA019692; -.
DR   MIM; 601753; gene.
DR   PharmGKB; PA33582; -.
DR   HOGENOM; Q08752; -.
DR   HOVERGEN; Q08752; -.
DR   OMA; IYAKMFA; -.
DR   BRENDA; 5.2.1.8; 247.
DR   NextBio; 21218; -.
DR   ArrayExpress; Q08752; -.
DR   Bgee; Q08752; -.
DR   CleanEx; HS_PPID; -.
DR   Genevestigator; Q08752; -.
DR   GermOnline; ENSG00000171497; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016018; F:cyclosporin A binding; TAS:UniProtKB.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR013026; TPR_region.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00028; TPR; 3.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Complete proteome; Cyclosporin; Cytoplasm; Direct protein sequencing;
KW   Isomerase; Polymorphism; Repeat; Rotamase; TPR repeat.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    370       40 kDa peptidyl-prolyl cis-trans
FT                                isomerase.
FT                                /FTId=PRO_0000064153.
FT   DOMAIN       19    183       PPIase cyclophilin-type.
FT   REPEAT      223    256       TPR 1.
FT   REPEAT      273    306       TPR 2.
FT   REPEAT      307    340       TPR 3.
FT   VARIANT      49     49       R -> C (in dbSNP:rs2070631).
FT                                /FTId=VAR_021021.
FT   VARIANT     196    196       D -> V (in dbSNP:rs2230222).
FT                                /FTId=VAR_051771.
FT   VARIANT     302    302       L -> I.
FT                                /FTId=VAR_021022.
FT   VARIANT     335    335       G -> E (in dbSNP:rs17843956).
FT                                /FTId=VAR_021023.
SQ   SEQUENCE   370 AA;  40764 MW;  39D4100748B35D48 CRC64;
     MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGH
     TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDREGLLSM
     ANAGRNTNGS QFFITTVPTP HLDGKHVVFG QVIKGIGVAR ILENVEVKGE KPAKLCVIAE
     CGELKEGDDG GIFPKDGSGD SHPDFPEDAD IDLKDVDKIL LITEDLKNIG NTFFKSQNWE
     MAIKKYAEVL RYVDSSKAVI ETADRAKLQP IALSCVLNIG ACKLKMSNWQ GAIDSCLEAL
     ELDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQGIAPED KAIQAELLKV KQKIKAQKDK
     EKAVYAKMFA
//