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Q562B5 (PGAM5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PGAM5, mitochondrial

EC=3.1.3.16
Alternative name(s):
Phosphoglycerate mutase family member 5
Gene names
Name:Pgam5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression By similarity. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore. Ref.2

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Dimer. Forms a ternary complex with NFE2L2 and KEAP1. Interacts with BCL2L1 and MAP3K5 By similarity. Upon TNF-induced necrosis, forms in complex with RIPK1, RIPK3 and MLKL; the formation of this complex leads to PGAM5 phosphorylation By similarity. Interacts with DNM1L; this interaction leads to DNM1L dephosphorylation and activation and eventually to mitochondria fragmentation By similarity.

Subcellular location

Mitochondrion outer membrane; Single-pass membrane protein By similarity.

Domain

The N-terminal 35 amino acids, including the potential transmembrane alpha-helix, function as a non-cleaved mitochondrial targeting sequence that targets the protein to the cytosolic side of the outer mitochondrial membrane By similarity.

Post-translational modification

Phosphorylated by the RIPK1/RIPK3 complex under necrotic conditions. This phosphorylation increases PGAM5 phosphatase activity By similarity.

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288Serine/threonine-protein phosphatase PGAM5, mitochondrial
PRO_0000288784

Regions

Transmembrane7 – 2923Helical; Potential
Region76 – 816Interaction with KEAP1 By similarity

Amino acid modifications

Modified residue1151N6-acetyllysine By similarity
Modified residue1431N6-acetyllysine By similarity
Modified residue1901N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q562B5 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: B4DD3F3D276A61C5

FASTA28832,060
        10         20         30         40         50         60 
MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRAGGDADTR TTEPLAWTGA RPGHGVWDSN 

        70         80         90        100        110        120 
WDRREPLSLI NLKKRNVEFG EDELASRLDH YKAKATRHIF LIRHSQYNVD GSMEKDRTLT 

       130        140        150        160        170        180 
PLGREQAELT GIRLASLGLK FNKIVHSSMT RAVETTDIIS KHLPGVCRVS TDLLREGAPI 

       190        200        210        220        230        240 
EPDPPVSHWK PEAVQYYEDG ARIEAAFRNY IHRADAKQEE DSYEIFICHA NVIRYIVCRA 

       250        260        270        280 
LQFPPEGWLR LSLNNGSITH LVIRPNGRVA LRTLGDTGFM PPDKITRS 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[2]"The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways."
Wang Z., Jiang H., Chen S., Du F., Wang X.
Cell 148:228-243(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC092607 mRNA. Translation: AAH92607.1.
RefSeqNP_001020443.1. NM_001025272.1.
UniGeneRn.23489.

3D structure databases

ProteinModelPortalQ562B5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000053513.

Proteomic databases

PaxDbQ562B5.
PRIDEQ562B5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID288731.
KEGGrno:288731.
UCSCRGD:1312028. rat.

Organism-specific databases

CTD192111.
RGD1312028. Pgam5.

Phylogenomic databases

eggNOGNOG71348.
HOGENOMHOG000261217.
HOVERGENHBG105576.
InParanoidQ562B5.
KOK15637.
PhylomeDBQ562B5.

Gene expression databases

GenevestigatorQ562B5.

Family and domain databases

InterProIPR013078. His_Pase_superF_clade-1.
[Graphical view]
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio628617.

Entry information

Entry namePGAM5_RAT
AccessionPrimary (citable) accession number: Q562B5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families