LOCUS       NP_113981                752 aa            linear   ROD 17-JUL-2024
DEFINITION  peptidyl-prolyl cis-trans isomerase G [Rattus norvegicus].
ACCESSION   NP_113981 XP_346655
VERSION     NP_113981.2
DBSOURCE    REFSEQ: accession NM_031793.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Davis,T.L., Walker,J.R., Campagna-Slater,V., Finerty,P.J.,
            Paramanathan,R., Bernstein,G., MacKenzie,F., Tempel,W., Ouyang,H.,
            Lee,W.H., Eisenmesser,E.Z. and Dhe-Paganon,S.
  TITLE     Structural and biochemical characterization of the human
            cyclophilin family of peptidyl-prolyl isomerases
  JOURNAL   PLoS Biol 8 (7), e1000439 (2010)
   PUBMED   20676357
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Mesa,A., Somarelli,J.A. and Herrera,R.J.
  TITLE     Spliceosomal immunophilins
  JOURNAL   FEBS Lett 582 (16), 2345-2351 (2008)
   PUBMED   18544344
  REMARK    Review article
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Mortillaro,M.J. and Berezney,R.
  TITLE     Matrin CYP, an SR-rich cyclophilin that associates with the nuclear
            matrix and splicing factors
  JOURNAL   J Biol Chem 273 (14), 8183-8192 (1998)
   PUBMED   9525923
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Nov 26, 2020 this sequence version replaced NP_113981.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF043642.1, SRR26360181.1113206.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..752
                     /product="peptidyl-prolyl cis-trans isomerase G"
                     /EC_number="5.2.1.8"
                     /note="PPIase G; matrin-cyp; rotamase G; cyclophilin G;
                     peptidyl-prolyl isomerase G; matrin cyclophilin
                     (matrin-cyp)"
                     /calculated_mol_wt=88188
     Region          8..175
                     /region_name="cyclophilin"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerases. This family contains eukaryotic, bacterial and
                     archeal proteins which exhibit a peptidylprolyl cis- trans
                     isomerases activity (PPIase, Rotamase) and in addition
                     bind the immunosuppressive drug...; cl00197"
                     /db_xref="CDD:469651"
     Site            order(67,69,72..73,75,113..114,123,125,133..134,138)
                     /site_type="active"
                     /db_xref="CDD:238194"
     Region          182..752
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O55035.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            743
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13427; propagated from
                     UniProtKB/Swiss-Prot (O55035.2)"
     CDS             1..752
                     /gene="Ppig"
                     /coded_by="NM_031793.3:318..2576"
                     /db_xref="GeneID:83624"
                     /db_xref="RGD:620315"
ORIGIN      
        1 mgikvqrprc ffdiainnqp agrvvfelfs dvcpktcenf rclctgekgt gkstqkplhy
       61 ksclfhrvvk dfmvqggdfs egngrggesi yggffedesf avkhnkefll smanrgkdtn
      121 gsqffittkp tphldghhvv fgqvisgqev vreienqktd aaskpfaevr ilscgelvpk
      181 skvkkeekkr hkssssssss dsdsssdsqs ssdssdsesa seeksrkrkk khrknsrkhk
      241 kekkkrkksk kspssesead nvdaqpqstv rpeeippipe nrflmrkspp kaddkerknr
      301 erererecnp pnsqpasyqr rflvtrsgrk ikgrgprryr tpsrsrsrdr frrsetpphw
      361 rqemqraqrm rvssgerwik gdkselneik enqrspvrvk ekkitdhrhm sespnrkiek
      421 ekkvkdhkse skerdirrns ekddkynknk vkkrgksksr skskersksk erdskhsrhe
      481 dkrvrsrske rdhettkeke kqldskgkdq ersrskensk qvesksnehd hskskekdrr
      541 aqsrsrerdl tkskhsynsr trersrsrdr srrvrsrshd rdrsrskeyh ryreqeyrrr
      601 grsrsrdrrt pgrsrskdrr rrrrdsrsse reesqsrnke kyrsqdskss hrkensegek
      661 rmysksrdhs ssnnnrekka didqspvskt kqssqdnevk sstlknqede ktrspveken
      721 qkskgqendh vhdknkkcdh esspgtdedk sg
//
