PPIG_MOUSE
ID PPIG_MOUSE Reviewed; 752 AA.
AC A2AR02; O70134; Q3TP68; Q3UXE0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 117.
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:0000250|UniProtKB:Q13427};
DE AltName: Full=Cyclophilin G;
DE AltName: Full=Rotamase G;
GN Name=Ppig;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-74.
RC STRAIN=129/Sv;
RA Lee C.G., Hurwitz J.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-495 AND 549-752.
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-255 AND SER-257, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q13427}.
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:Q13427};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000250|UniProtKB:Q13427}.
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:0000250|UniProtKB:Q13427}.
CC Nucleus speckle {ECO:0000250|UniProtKB:Q13427}. Note=Colocalizes with
CC splicing factors at nuclear speckles. {ECO:0000250|UniProtKB:Q13427}.
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}.
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DR EMBL; AL845261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U91923; AAC05726.1; -; mRNA.
DR EMBL; AK135713; BAE22623.1; -; mRNA.
DR EMBL; AK164670; BAE37869.1; -; mRNA.
DR CCDS; CCDS38137.1; -.
DR RefSeq; NP_001074555.1; NM_001081086.1.
DR RefSeq; XP_006499247.1; XM_006499184.3.
DR RefSeq; XP_006499248.1; XM_006499185.3.
DR RefSeq; XP_006499249.1; XM_006499186.2.
DR RefSeq; XP_006499250.1; XM_006499187.3.
DR AlphaFoldDB; A2AR02; -.
DR SMR; A2AR02; -.
DR BioGRID; 230703; 3.
DR IntAct; A2AR02; 1.
DR MINT; A2AR02; -.
DR STRING; 10090.ENSMUSP00000045945; -.
DR iPTMnet; A2AR02; -.
DR PhosphoSitePlus; A2AR02; -.
DR EPD; A2AR02; -.
DR jPOST; A2AR02; -.
DR MaxQB; A2AR02; -.
DR PaxDb; A2AR02; -.
DR PeptideAtlas; A2AR02; -.
DR PRIDE; A2AR02; -.
DR ProteomicsDB; 289805; -.
DR Antibodypedia; 19292; 284 antibodies from 34 providers.
DR Ensembl; ENSMUST00000040915; ENSMUSP00000045945; ENSMUSG00000042133.
DR Ensembl; ENSMUST00000090858; ENSMUSP00000088370; ENSMUSG00000042133.
DR GeneID; 228005; -.
DR KEGG; mmu:228005; -.
DR UCSC; uc008jyl.1; mouse.
DR CTD; 9360; -.
DR MGI; MGI:2445173; Ppig.
DR VEuPathDB; HostDB:ENSMUSG00000042133; -.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000157954; -.
DR HOGENOM; CLU_012062_33_6_1; -.
DR InParanoid; A2AR02; -.
DR OMA; YDHYERS; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; A2AR02; -.
DR TreeFam; TF318563; -.
DR BioGRID-ORCS; 228005; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Ppig; mouse.
DR PRO; PR:A2AR02; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AR02; protein.
DR Bgee; ENSMUSG00000042133; Expressed in animal zygote and 248 other tissues.
DR ExpressionAtlas; A2AR02; baseline and differential.
DR Genevisible; A2AR02; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
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; 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 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_0000282597"
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..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..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:0007744|PubMed:21183079"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000250|UniProtKB:Q13427"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13427"
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:0000250|UniProtKB:Q13427"
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 21
FT /note="Missing (in Ref. 2; AAC05726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 88325 MW; A78CA4EEB0E0871B CRC64;
MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY
KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN
GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCGELIPK
SKVKKEEKKR HKSSSSSSSS DSDSSSDSQS SSESSDSESA SEEKSRKRKK KHRKNSRKHK
KEKKKRKKSK KSPSSESEAE NVDAQPQSTV RPEEIPPIPE NRFLMRKSPP KADDKERKNR
ERERERECNP PNSQPASYQR RFLVTRSGRK IKGRGPRRYR TPSRSRSRDR FRRSETPPHW
RQEMQRAQRM RVSSGERWIK GDKSELNEIK ENQRSPVRVK EKKITDHRHM SESPNRKVEK
EKKAKDHKSE SKERDIRRNS EKDDKYNKNK VKKRGKSKSR SKSKERSKSK ERDSKHSRHE
DKRVRSRSKE RDHETTKEKE KPLDPKGKDQ ERSRSKENSK QVESKSNEHD HSKSKEKDRR
AQSRSRERDL TKSKHSYNSR TRERSRSRDR SRRVRSRSHD RDRSRSKEYH RYREQEYRRR
GRSRSRDRRT PGRSRSKDRR RRRRDSRSSE REESQSRNKD KYRSQESKSS HRKENSEGEK
RTYSKSRDHN SSSNNREKKA DREQSPVSKT KQSSQDNEVK SSTLKNQEDE KTRSPVEKEN
QKSKGQENDH VHDKNKKCDH ESSPGTDEDK SG
