ID PPID_BOVIN Reviewed; 370 AA. AC P26882; Q28077; Q2HJ45; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 6. DT 03-NOV-2009, entry version 84. 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; DE AltName: Full=Estrogen receptor-binding cyclophilin; GN Name=PPID; Synonyms=CYPD; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH RP ESR1, AND TISSUE SPECIFICITY. RX MEDLINE=93293832; PubMed=8514757; RA Ratajczak T., Carrello A., Mark P.J., Warner B.J., Simpson R.J., RA Moritz R.L., House A.K.; RT "The cyclophilin component of the unactivated estrogen receptor RT contains a tetratricopeptide repeat domain and shares identity with RT p59 (FKBP59)."; RL J. Biol. Chem. 268:13187-13192(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Uterus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-345. RC TISSUE=Brain; 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 [4] RP PROTEIN SEQUENCE OF 18-42; 147-154; 199-219; 228-235 AND 309-312, AND RP FUNCTION. RC TISSUE=Brain; RX MEDLINE=92184809; PubMed=1544925; RA Kieffer L.J., Thalhammer T., Handschumacher R.E.; RT "Isolation and characterization of a 40-kDa cyclophilin-related RT protein."; RL J. Biol. Chem. 267:5503-5507(1992). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=11377203; DOI=10.1016/S0969-2126(01)00603-7; RA Taylor P., Dornan J., Carrello A., Minchin R.F., Ratajczak T., RA Walkinshaw M.D.; RT "Two structures of cyclophilin 40: folding and fidelity in the TPR RT domains."; RL Structure 9:431-438(2001). 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Detected in heart, thymis and brain. CC -!- PTM: The N-terminus is blocked. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D14074; BAA03159.1; -; mRNA. DR EMBL; BC113318; AAI13319.1; -; mRNA. DR EMBL; L11668; AAA30484.1; -; mRNA. DR IPI; IPI00703731; -. DR PIR; A46579; A46579. DR RefSeq; NP_776578.1; -. DR UniGene; Bt.7221; -. DR PDB; 1IHG; X-ray; 1.80 A; A=1-370. DR PDB; 1IIP; X-ray; 2.00 A; A=1-370. DR PDBsum; 1IHG; -. DR PDBsum; 1IIP; -. DR STRING; P26882; -. DR Ensembl; ENSBTAT00000022180; ENSBTAP00000022180; ENSBTAG00000016680; Bos taurus. DR GeneID; 281420; -. DR KEGG; bta:281420; -. DR CTD; 281420; -. DR HOVERGEN; P26882; -. DR OMA; IYAKMFA; -. DR BRENDA; 5.2.1.8; 251. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW. 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; 3. 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 3D-structure; Cyclosporin; Cytoplasm; Direct protein sequencing; KW Isomerase; Repeat; Rotamase; TPR repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 370 40 kDa peptidyl-prolyl cis-trans FT isomerase. FT /FTId=PRO_0000064152. 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 STRAND 8 11 FT STRAND 17 24 FT STRAND 27 36 FT TURN 38 40 FT HELIX 42 53 FT TURN 60 62 FT STRAND 63 66 FT STRAND 72 77 FT TURN 78 80 FT STRAND 81 84 FT TURN 87 89 FT STRAND 90 93 FT STRAND 117 120 FT STRAND 132 137 FT HELIX 140 142 FT TURN 143 145 FT STRAND 148 154 FT HELIX 156 163 FT STRAND 171 174 FT STRAND 176 184 FT STRAND 196 198 FT HELIX 206 208 FT STRAND 209 211 FT HELIX 216 235 FT HELIX 239 259 FT HELIX 262 265 FT HELIX 266 268 FT HELIX 269 285 FT HELIX 289 300 FT HELIX 307 319 FT HELIX 323 336 FT HELIX 341 362 SQ SEQUENCE 370 AA; 40620 MW; F278FDE1B9494241 CRC64; MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGP TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDKEGLLSM ANAGSNTNGS QFFITTVPTP HLDGKHVVFG QVIKGMGVAK ILENVEVKGE KPAKLCVIAE CGELKEGDDW GIFPKDGSGD SHPDFPEDAD VDLKDVDKIL LISEDLKNIG NTFFKSQNWE MAIKKYTKVL RYVEGSRAAA EDADGAKLQP VALSCVLNIG ACKLKMSDWQ GAVDSCLEAL EIDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQEIAPED KAIQAELLKV KQKIKAQKDK EKAAYAKMFA //