PGAM5_RAT
ID PGAM5_RAT Reviewed; 288 AA.
AC Q562B5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Serine/threonine-protein phosphatase PGAM5, mitochondrial;
DE EC=3.1.3.16;
DE AltName: Full=Phosphoglycerate mutase family member 5;
GN Name=Pgam5;
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 [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [2]
RP FUNCTION.
RX PubMed=22265414; DOI=10.1016/j.cell.2011.11.030;
RA Wang Z., Jiang H., Chen S., Du F., Wang X.;
RT "The mitochondrial phosphatase PGAM5 functions at the convergence point of
RT multiple necrotic death pathways.";
RL Cell 148:228-243(2012).
CC -!- FUNCTION: Displays phosphatase activity for serine/threonine residues,
CC and, dephosphorylates and activates MAP3K5 kinase. Has apparently no
CC phosphoglycerate mutase activity. May be regulator of mitochondrial
CC dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex.
CC Contributes to the repression of NFE2L2-dependent gene expression (By
CC similarity). Acts as a central mediator for programmed necrosis induced
CC by TNF, by reactive oxygen species and by calcium ionophore.
CC {ECO:0000250, ECO:0000269|PubMed:22265414}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Dimer. Forms a ternary complex with NFE2L2 and KEAP1.
CC Interacts with BCL2L1 and MAP3K5 (By similarity). Upon TNF-induced
CC necrosis, forms in complex with RIPK1, RIPK3 and MLKL; the formation of
CC this complex leads to PGAM5 phosphorylation (By similarity). Interacts
CC with DNM1L; this interaction leads to DNM1L dephosphorylation and
CC activation and eventually to mitochondria fragmentation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The N-terminal 35 amino acids, including the potential
CC transmembrane alpha-helix, function as a non-cleaved mitochondrial
CC targeting sequence that targets the protein to the cytosolic side of
CC the outer mitochondrial membrane. {ECO:0000250}.
CC -!- PTM: Phosphorylated by the RIPK1/RIPK3 complex under necrotic
CC conditions. This phosphorylation increases PGAM5 phosphatase activity
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; BC092607; AAH92607.1; -; mRNA.
DR RefSeq; NP_001020443.1; NM_001025272.1.
DR AlphaFoldDB; Q562B5; -.
DR SMR; Q562B5; -.
DR BioGRID; 252666; 2.
DR IntAct; Q562B5; 1.
DR MINT; Q562B5; -.
DR STRING; 10116.ENSRNOP00000053513; -.
DR iPTMnet; Q562B5; -.
DR PhosphoSitePlus; Q562B5; -.
DR jPOST; Q562B5; -.
DR PaxDb; Q562B5; -.
DR PRIDE; Q562B5; -.
DR GeneID; 288731; -.
DR KEGG; rno:288731; -.
DR UCSC; RGD:1312028; rat.
DR CTD; 192111; -.
DR RGD; 1312028; Pgam5.
DR eggNOG; KOG4609; Eukaryota.
DR InParanoid; Q562B5; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; Q562B5; -.
DR Reactome; R-RNO-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:Q562B5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0070266; P:necroptotic process; ISS:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IBA:GO_Central.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Necrosis; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Serine/threonine-protein phosphatase PGAM5,
FT mitochondrial"
FT /id="PRO_0000288784"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 76..81
FT /note="Interaction with KEAP1"
FT /evidence="ECO:0000250"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HS1"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96HS1"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96HS1"
FT MOD_RES 190
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96HS1"
SQ SEQUENCE 288 AA; 32060 MW; B4DD3F3D276A61C5 CRC64;
MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRAGGDADTR TTEPLAWTGA RPGHGVWDSN
WDRREPLSLI NLKKRNVEFG EDELASRLDH YKAKATRHIF LIRHSQYNVD GSMEKDRTLT
PLGREQAELT GIRLASLGLK FNKIVHSSMT RAVETTDIIS KHLPGVCRVS TDLLREGAPI
EPDPPVSHWK PEAVQYYEDG ARIEAAFRNY IHRADAKQEE DSYEIFICHA NVIRYIVCRA
LQFPPEGWLR LSLNNGSITH LVIRPNGRVA LRTLGDTGFM PPDKITRS
