PPIB_RAT
ID PPIB_RAT Reviewed; 216 AA.
AC P24368; O88541;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE Short=PPIase B;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:P23284};
DE AltName: Full=CYP-S1;
DE AltName: Full=Cyclophilin B;
DE AltName: Full=Rotamase B;
DE AltName: Full=S-cyclophilin;
DE Short=SCYLP;
DE Flags: Precursor;
GN Name=Ppib;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2194066; DOI=10.1038/ki.1990.136;
RA Iwai N., Inagami T.;
RT "Molecular cloning of a complementary DNA to rat cyclophilin-like protein
RT mRNA.";
RL Kidney Int. 37:1460-1465(1990).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=1530944; DOI=10.1083/jcb.116.1.113;
RA Arber S., Krause K.-H., Caroni P.;
RT "S-cyclophilin is retained intracellularly via a unique COOH-terminal
RT sequence and colocalizes with the calcium storage protein calreticulin.";
RL J. Cell Biol. 116:113-125(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar Kyoto; TISSUE=Kidney;
RX PubMed=10775569; DOI=10.1161/01.hyp.35.4.958;
RA Kainer D.B., Doris P.A.;
RT "Cyclophilin B expression in renal proximal tubules of hypertensive rats.";
RL Hypertension 35:958-964(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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:P23284}.
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:P23284};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- SUBUNIT: Interacts with DYM. Interacts with CALR, CLGN and CANX. Part
CC of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1,
CC HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small
CC amounts of ERP29, but not, or at very low levels, CALR nor CANX.
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- INTERACTION:
CC P24368; P38659: Pdia4; NbExp=2; IntAct=EBI-916926, EBI-917435;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P23284}. Melanosome
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in kidney.
CC {ECO:0000269|PubMed:10775569}.
CC -!- POLYMORPHISM: Higher levels occur in the proximal convoluted tubule of
CC strain SHR than strain Wistar Kyoto. {ECO:0000269|PubMed:10775569}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF071225; AAC25590.1; ALT_INIT; mRNA.
DR EMBL; BC061971; AAH61971.1; -; mRNA.
DR PIR; S71547; S71547.
DR RefSeq; NP_071981.1; NM_022536.2.
DR AlphaFoldDB; P24368; -.
DR SMR; P24368; -.
DR BioGRID; 249051; 1.
DR IntAct; P24368; 8.
DR MINT; P24368; -.
DR STRING; 10116.ENSRNOP00000022828; -.
DR iPTMnet; P24368; -.
DR PhosphoSitePlus; P24368; -.
DR SwissPalm; P24368; -.
DR jPOST; P24368; -.
DR PaxDb; P24368; -.
DR PRIDE; P24368; -.
DR Ensembl; ENSRNOT00000022828; ENSRNOP00000022828; ENSRNOG00000016781.
DR GeneID; 64367; -.
DR KEGG; rno:64367; -.
DR UCSC; RGD:620312; rat.
DR CTD; 5479; -.
DR RGD; 620312; Ppib.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000158007; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P24368; -.
DR OMA; GEGYPGS; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P24368; -.
DR TreeFam; TF354259; -.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:P24368; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000016781; Expressed in pancreas and 20 other tissues.
DR Genevisible; P24368; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISS:CAFA.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
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:0070063; F:RNA polymerase binding; ISO:RGD.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:CAFA.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0051169; P:nuclear transport; TAS:RGD.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:RGD.
DR GO; GO:0044794; P:positive regulation by host of viral process; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Isomerase; Reference proteome;
KW Rotamase; S-nitrosylation; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000250"
FT CHAIN 34..216
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000025481"
FT DOMAIN 47..204
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOTIF 213..216
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 202
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 209
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24369"
FT MOD_RES 209
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24369"
FT CONFLICT 54..70
FT /note="DEPVGRVTFGLFGKTVP -> GRTCRTSDLWTLWKDCS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..96
FT /note="RV -> HM (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 23803 MW; 8750D541754380D5 CRC64;
MLRLSERNMK VLFAAALIVG SVVFLLLPGP SVANDKKKGP KVTVKVYFDF QIGDEPVGRV
TFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG
ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTS WLDGKHVVFG KVLEGMDVVR
KVENTKTDSR DKPLKDVIIV DCGKIEVEKP FAIAKE
