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Protein

Peptidyl-prolyl cis-trans isomerase G

Gene

Ppig

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Cyclosporin A (CsA)-sensitive.

GO - Molecular functioni

  • peptidyl-prolyl cis-trans isomerase activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase G (EC:5.2.1.8)
Short name:
PPIase G
Short name:
Peptidyl-prolyl isomerase G
Alternative name(s):
Cyclophilin G
Matrin cyclophilin
Short name:
Matrin-cyp
Rotamase G
Gene namesi
Name:Ppig
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620315. Ppig.

Subcellular locationi

  • Nucleus matrix 1 Publication
  • Nucleus speckle 1 Publication

  • Note: Colocalizes with splicing factors at nuclear speckles.

GO - Cellular componenti

  • nuclear matrix Source: RGD
  • nuclear speck Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641511 – 752Peptidyl-prolyl cis-trans isomerase GAdd BLAST752

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei252PhosphoserineBy similarity1
Modified residuei254PhosphoserineBy similarity1
Modified residuei255PhosphoserineBy similarity1
Modified residuei257PhosphoserineBy similarity1
Modified residuei288PhosphoserineBy similarity1
Modified residuei313PhosphoserineBy similarity1
Modified residuei354PhosphoserineCombined sources1
Modified residuei356PhosphothreonineCombined sources1
Modified residuei384PhosphoserineBy similarity1
Modified residuei395PhosphoserineCombined sources1
Modified residuei411PhosphoserineBy similarity1
Modified residuei413PhosphoserineBy similarity1
Modified residuei685PhosphoserineCombined sources1
Modified residuei688PhosphoserineBy similarity1
Modified residuei694PhosphoserineBy similarity1
Modified residuei742PhosphoserineBy similarity1
Modified residuei743PhosphoserineBy similarity1
Modified residuei746PhosphothreonineBy similarity1
Modified residuei751PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO55035.
PRIDEiO55035.

PTM databases

iPTMnetiO55035.
PhosphoSitePlusiO55035.

Interactioni

Subunit structurei

Interacts with CLK1, PNN and with the phosphorylated C-terminal domain of RNA polymerase II.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010216.

Structurei

3D structure databases

ProteinModelPortaliO55035.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 176PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST166

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi180 – 192Arg/Lys-rich (basic)Add BLAST13
Compositional biasi193 – 223Asp/Glu/Ser-richAdd BLAST31
Compositional biasi193 – 206Poly-SerAdd BLAST14
Compositional biasi224 – 251Arg/Lys-rich (basic)Add BLAST28
Compositional biasi539 – 637Arg/Ser-rich (RS domain)Add BLAST99
Compositional biasi619 – 624Poly-Arg6

Domaini

The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II.By similarity

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0546. Eukaryota.
COG0652. LUCA.
HOGENOMiHOG000115659.
HOVERGENiHBG048162.
InParanoidiO55035.
KOiK09566.
PhylomeDBiO55035.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O55035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT
60 70 80 90 100
GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF
110 120 130 140 150
AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV
160 170 180 190 200
VREIENQKTD AASKPFAEVR ILSCGELVPK SKVKKEEKKR HKSSSSSSSS
210 220 230 240 250
DSDSSSDSQS SSDSSDSESA SEEKSRKRKK KHRKNSRKHK KEKKKRKKSK
260 270 280 290 300
KSPSSESEAD NVDAQPQSTV RPEEIPPIPE NRFLMRKSPP KADDKERKNR
310 320 330 340 350
ERERERECNP PNSQPASYQR RFLVTRFGRK IKGRGPRRYR TPSRSRSRDR
360 370 380 390 400
FRRSETPPHW RQEMQRAQRM RVSSGERWIK GDKSELNEIK ENQRSPVRVK
410 420 430 440 450
EKKITDHRHM SESPNRKIEK EKKVKDHKSE SKERDIRRNS EKDDKYNKNK
460 470 480 490 500
VKKRGKSKSR SKSKERSKSK ERDSKHSRHE DKRVRSRSKE RDHETTKEKE
510 520 530 540 550
KQLDSKGKDQ ERSRSKENSK QVESKSNEHD HSKSKEKDRR AQSRSRERDL
560 570 580 590 600
TKSKHSYNSR TRERSRSRDR SRRVRSRSHD RDRSRSKEYH RYREQEYRRR
610 620 630 640 650
GRSRSRDRRT PGRSRSKDRR RRRRDSRSSE REESQSRNKE KYRSQDSKSS
660 670 680 690 700
HRKENSEGEK RMYSKSRDHS SSNNNREKKA DIDQSPVSKT KQSSQDNEVK
710 720 730 740 750
SSTLKNQEDE KTRSPVEKEN QKSKGQENDH VHDKNKKCDH ESSPGTDEDK

SG
Length:752
Mass (Da):88,379
Last modified:May 10, 2005 - v2
Checksum:i4EC4C0D07CCB76B9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti219S → T in AAC00191 (PubMed:9525923).Curated1
Sequence conflicti327F → S in AAC00191 (PubMed:9525923).Curated1
Sequence conflicti417K → G in AAC00191 (PubMed:9525923).Curated1
Sequence conflicti421 – 422EK → GG in AAC00191 (PubMed:9525923).Curated2
Sequence conflicti429S → L in AAC00191 (PubMed:9525923).Curated1
Sequence conflicti441E → G in AAC00191 (PubMed:9525923).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043642 mRNA. Translation: AAC00191.1.
BC085723 mRNA. Translation: AAH85723.1.
RefSeqiNP_113981.1. NM_031793.1.
UniGeneiRn.10898.

Genome annotation databases

GeneIDi83624.
KEGGirno:83624.
UCSCiRGD:620315. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043642 mRNA. Translation: AAC00191.1.
BC085723 mRNA. Translation: AAH85723.1.
RefSeqiNP_113981.1. NM_031793.1.
UniGeneiRn.10898.

3D structure databases

ProteinModelPortaliO55035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010216.

PTM databases

iPTMnetiO55035.
PhosphoSitePlusiO55035.

Proteomic databases

PaxDbiO55035.
PRIDEiO55035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83624.
KEGGirno:83624.
UCSCiRGD:620315. rat.

Organism-specific databases

CTDi9360.
RGDi620315. Ppig.

Phylogenomic databases

eggNOGiKOG0546. Eukaryota.
COG0652. LUCA.
HOGENOMiHOG000115659.
HOVERGENiHBG048162.
InParanoidiO55035.
KOiK09566.
PhylomeDBiO55035.

Miscellaneous databases

PROiO55035.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPIG_RAT
AccessioniPrimary (citable) accession number: O55035
Secondary accession number(s): Q5U346
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 10, 2005
Last modified: November 2, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.