Reviewed, UniProtKB/Swiss-Prot P26882 (PPID_BOVIN)

Names and origin

Protein names

Recommended name:
    40 kDa peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin-40
      Short name=CYP-40
    Cyclophilin-related protein
    Estrogen receptor-binding cyclophilin

Gene names

Name:	PPID
Synonyms:	CYPD

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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.
Subcellular location	Cytoplasm.
Tissue specificity	Detected in heart, thymis and brain.
Post-translational modification	The N-terminus is blocked.
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
Domain	Repeat TPR repeat
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from sequence or structural similarity. Source: AgBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 370

369

40 kDa peptidyl-prolyl cis-trans isomerase

PRO_0000064152

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

Secondary structure

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370

Helix Strand Turn

Details...

Beta strand

8 – 11

4

Beta strand

17 – 24

8

Beta strand

27 – 36

10

Turn

38 – 40

3

Helix

42 – 53

12

Turn

60 – 62

3

Beta strand

63 – 66

4

Beta strand

72 – 77

6

Turn

78 – 80

3

Beta strand

81 – 84

4

Turn

87 – 89

3

Beta strand

90 – 93

4

Beta strand

117 – 120

4

Beta strand

132 – 137

6

Helix

140 – 142

3

Turn

143 – 145

3

Beta strand

148 – 154

7

Helix

156 – 163

8

Beta strand

171 – 174

4

Beta strand

176 – 184

9

Beta strand

196 – 198

3

Helix

206 – 208

3

Beta strand

209 – 211

3

Helix

216 – 235

20

Helix

239 – 259

21

Helix

262 – 265

4

Helix

266 – 268

3

Helix

269 – 285

17

Helix

289 – 300

12

Helix

307 – 319

13

Helix

323 – 336

14

Helix

341 – 362

22

Sequences

	Sequence		Length	Mass (Da)
	P26882-1 [UniParc]. Last modified January 23, 2007. Version 6. Checksum: F278FDE1B9494241	FASTA	370	40,620
	10 20 30 40 50 60 MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGP 70 80 90 100 110 120 TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDKEGLLSM 130 140 150 160 170 180 ANAGSNTNGS QFFITTVPTP HLDGKHVVFG QVIKGMGVAK ILENVEVKGE KPAKLCVIAE 190 200 210 220 230 240 CGELKEGDDW GIFPKDGSGD SHPDFPEDAD VDLKDVDKIL LISEDLKNIG NTFFKSQNWE 250 260 270 280 290 300 MAIKKYTKVL RYVEGSRAAA EDADGAKLQP VALSCVLNIG ACKLKMSDWQ GAVDSCLEAL 310 320 330 340 350 360 EIDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQEIAPED KAIQAELLKV KQKIKAQKDK 370 EKAAYAKMFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)." Ratajczak T., Carrello A., Mark P.J., Warner B.J., Simpson R.J., Moritz R.L., House A.K. J. Biol. Chem. 268:13187-13192(1993) [PubMed: 8514757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH ESR1, TISSUE SPECIFICITY.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus.
[3]	"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] OF 37-345. Tissue: Brain.
[4]	"Isolation and characterization of a 40-kDa cyclophilin-related protein." Kieffer L.J., Thalhammer T., Handschumacher R.E. J. Biol. Chem. 267:5503-5507(1992) [PubMed: 1544925] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-42; 147-154; 199-219; 228-235 AND 309-312, FUNCTION. Tissue: Brain.
[5]	"Two structures of cyclophilin 40: folding and fidelity in the TPR domains." Taylor P., Dornan J., Carrello A., Minchin R.F., Ratajczak T., Walkinshaw M.D. Structure 9:431-438(2001) [PubMed: 11377203] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

D14074 mRNA. Translation: BAA03159.1.
BC113318 mRNA. Translation: AAI13319.1.
L11668 mRNA. Translation: AAA30484.1.

PIR

A46579.

RefSeq

NP_776578.1.

UniGene

Bt.7221

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IHG	X-ray	1.80	A	1-370	[»]
1IIP	X-ray	2.00	A	1-370	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSBTAG00000016680. Bos taurus. [Contig view]

GeneID

281420.

KEGG

bta:281420.

Phylogenomic databases

HOVERGEN

P26882.

Family and domain databases

InterPro

IPR002130. PPIase_cyclophilin.
IPR001440. TPR-1.
IPR011990. TPR-like_helical.
IPR013026. TPR_region.
[Graphical view]

Gene3D

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

PANTHER

PTHR11071. PPIase_cyclophilin. 1 hit.

Pfam

PF00160. Pro_isomerase. 1 hit.
PF00515. TPR_1. 3 hits.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

SMART

SM00028. TPR. 3 hits.
[Graphical view]

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...

Entry information

Entry name

PPID_BOVIN

Accession

Primary (citable) accession number: P26882
Secondary accession number(s): Q28077, Q2HJ45

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 75 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)