PPIC_BOVIN
ID PPIC_BOVIN Reviewed; 212 AA.
AC Q08E11;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase C {ECO:0000305};
DE Short=PPIase C {ECO:0000305};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:P45877};
DE AltName: Full=Cyclophilin C;
DE AltName: Full=Rotamase C;
GN Name=PPIC {ECO:0000250|UniProtKB:P45877};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding. {ECO:0000250|UniProtKB:P45877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000250|UniProtKB:P45877};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000250|UniProtKB:P45877}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30412}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; BC123474; AAI23475.1; -; mRNA.
DR RefSeq; NP_001070378.1; NM_001076910.1.
DR AlphaFoldDB; Q08E11; -.
DR SMR; Q08E11; -.
DR STRING; 9913.ENSBTAP00000002051; -.
DR PaxDb; Q08E11; -.
DR PeptideAtlas; Q08E11; -.
DR PRIDE; Q08E11; -.
DR Ensembl; ENSBTAT00000002051; ENSBTAP00000002051; ENSBTAG00000001568.
DR GeneID; 535494; -.
DR KEGG; bta:535494; -.
DR CTD; 5480; -.
DR VEuPathDB; HostDB:ENSBTAG00000001568; -.
DR VGNC; VGNC:33196; PPIC.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000159786; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; Q08E11; -.
DR OMA; CSIINSG; -.
DR OrthoDB; 1403619at2759; -.
DR TreeFam; TF354259; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000001568; Expressed in uterine cervix and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..212
FT /note="Peptidyl-prolyl cis-trans isomerase C"
FT /id="PRO_0000282592"
FT DOMAIN 41..198
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 212 AA; 22811 MW; B5C5A08A13613A53 CRC64;
MGPGLRPLLP LVLCVGLSAL VPSAGASGFR KRGPSVTAKV FFDVRIGDKD VGRIVIGLFG
KVVPKTVENF VALATGEKGY GYKGSKFHRV IKDFMIQGGD FTRGDGTGGI SIYGETFPDE
NFKLKHYGIG WVSMANAGPD TNGSQFFITL TKPTWLDGKH VVFGKVLDGM TVVHSIELQA
TDGHDRPFTD CSIVNSGKID VKTPFVVEVS DW
