PPIG_RAT
ID PPIG_RAT Reviewed; 752 AA.
AC O55035; Q5U346;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase G;
DE Short=PPIase G;
DE Short=Peptidyl-prolyl isomerase G;
DE EC=5.2.1.8 {ECO:0000269|PubMed:9525923};
DE AltName: Full=Cyclophilin G;
DE AltName: Full=Matrin cyclophilin;
DE Short=Matrin-cyp;
DE AltName: Full=Rotamase G;
GN Name=Ppig;
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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Insulinoma;
RX PubMed=9525923; DOI=10.1074/jbc.273.14.8183;
RA Mortillaro M.J., Berezney R.;
RT "Matrin CYP, an SR-rich cyclophilin that associates with the nuclear matrix
RT and splicing factors.";
RL J. Biol. Chem. 273:8183-8192(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND THR-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-685, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding. May be implicated in the folding, transport, and assembly of
CC proteins. May play an important role in the regulation of pre-mRNA
CC splicing. {ECO:0000269|PubMed:9525923}.
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; Evidence={ECO:0000269|PubMed:9525923};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000269|PubMed:9525923}.
CC -!- SUBUNIT: Interacts with CLK1, PNN and with the phosphorylated C-
CC terminal domain of RNA polymerase II. {ECO:0000250|UniProtKB:Q13427}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:9525923}.
CC Nucleus speckle {ECO:0000269|PubMed:9525923}. Note=Colocalizes with
CC splicing factors at nuclear speckles. {ECO:0000269|PubMed:9525923}.
CC -!- DOMAIN: The RS domain is required for the interaction with the
CC phosphorylated C-terminal domain of RNA polymerase II.
CC {ECO:0000250|UniProtKB:Q13427}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF043642; AAC00191.1; -; mRNA.
DR EMBL; BC085723; AAH85723.1; -; mRNA.
DR RefSeq; NP_113981.1; NM_031793.1.
DR AlphaFoldDB; O55035; -.
DR SMR; O55035; -.
DR IntAct; O55035; 1.
DR STRING; 10116.ENSRNOP00000010216; -.
DR iPTMnet; O55035; -.
DR PhosphoSitePlus; O55035; -.
DR jPOST; O55035; -.
DR PaxDb; O55035; -.
DR PRIDE; O55035; -.
DR GeneID; 83624; -.
DR KEGG; rno:83624; -.
DR UCSC; RGD:620315; rat.
DR CTD; 9360; -.
DR RGD; 620315; Ppig.
DR eggNOG; KOG0546; Eukaryota.
DR InParanoid; O55035; -.
DR PhylomeDB; O55035; -.
DR PRO; PR:O55035; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; 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 Isomerase; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Rotamase; Ubl conjugation.
FT CHAIN 1..752
FT /note="Peptidyl-prolyl cis-trans isomerase G"
FT /id="PRO_0000064151"
FT DOMAIN 11..176
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 182..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..250
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..347
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..622
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 746
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT CROSSLNK 691
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT CONFLICT 219
FT /note="S -> T (in Ref. 1; AAC00191)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="F -> S (in Ref. 1; AAC00191)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="K -> G (in Ref. 1; AAC00191)"
FT /evidence="ECO:0000305"
FT CONFLICT 421..422
FT /note="EK -> GG (in Ref. 1; AAC00191)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="S -> L (in Ref. 1; AAC00191)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="E -> G (in Ref. 1; AAC00191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 88379 MW; 4EC4C0D07CCB76B9 CRC64;
MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY
KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN
GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCGELVPK
SKVKKEEKKR HKSSSSSSSS DSDSSSDSQS SSDSSDSESA SEEKSRKRKK KHRKNSRKHK
KEKKKRKKSK KSPSSESEAD NVDAQPQSTV RPEEIPPIPE NRFLMRKSPP KADDKERKNR
ERERERECNP PNSQPASYQR RFLVTRFGRK IKGRGPRRYR TPSRSRSRDR FRRSETPPHW
RQEMQRAQRM RVSSGERWIK GDKSELNEIK ENQRSPVRVK EKKITDHRHM SESPNRKIEK
EKKVKDHKSE SKERDIRRNS EKDDKYNKNK VKKRGKSKSR SKSKERSKSK ERDSKHSRHE
DKRVRSRSKE RDHETTKEKE KQLDSKGKDQ ERSRSKENSK QVESKSNEHD HSKSKEKDRR
AQSRSRERDL TKSKHSYNSR TRERSRSRDR SRRVRSRSHD RDRSRSKEYH RYREQEYRRR
GRSRSRDRRT PGRSRSKDRR RRRRDSRSSE REESQSRNKE KYRSQDSKSS HRKENSEGEK
RMYSKSRDHS SSNNNREKKA DIDQSPVSKT KQSSQDNEVK SSTLKNQEDE KTRSPVEKEN
QKSKGQENDH VHDKNKKCDH ESSPGTDEDK SG
