PGAM5_DANRE
ID PGAM5_DANRE Reviewed; 289 AA.
AC Q502L2; A2CEB1; Q5U3B2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
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; ORFNames=si:dkey-69p22.1, zgc:92057;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Displays phosphatase activity for serine/threonine residues.
CC Has apparently no phosphoglycerate mutase activity. May be regulator of
CC mitochondrial dynamics (By similarity). May be a central mediator for
CC programmed necrosis (By similarity). {ECO:0000250}.
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 -!- 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; CR388061; CAM16277.1; -; Genomic_DNA.
DR EMBL; BC085627; AAH85627.1; -; mRNA.
DR EMBL; BC095654; AAH95654.1; -; mRNA.
DR RefSeq; NP_001007324.2; NM_001007323.2.
DR AlphaFoldDB; Q502L2; -.
DR SMR; Q502L2; -.
DR STRING; 7955.ENSDARP00000051620; -.
DR PaxDb; Q502L2; -.
DR Ensembl; ENSDART00000051621; ENSDARP00000051620; ENSDARG00000035608.
DR GeneID; 492357; -.
DR KEGG; dre:492357; -.
DR CTD; 192111; -.
DR ZFIN; ZDB-GENE-030131-683; pgam5.
DR eggNOG; KOG4609; Eukaryota.
DR GeneTree; ENSGT00390000004796; -.
DR HOGENOM; CLU_063130_0_1_1; -.
DR InParanoid; Q502L2; -.
DR OMA; WHSPLPR; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; Q502L2; -.
DR TreeFam; TF314977; -.
DR Reactome; R-DRE-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:Q502L2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000035608; Expressed in somite and 29 other tissues.
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:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
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 GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
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 Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane; Necrosis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Serine/threonine-protein phosphatase PGAM5,
FT mitochondrial"
FT /id="PRO_0000288785"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 68..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 82
FT /note="G -> S (in Ref. 2; AAH95654)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="A -> G (in Ref. 2; AAH85627)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="N -> T (in Ref. 2; AAH95654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32173 MW; 798F3A77AEFF0078 CRC64;
MSFRRALSLA CGFAGGSAVL VCAAVVADKN GYFGEGRRVT ETLAAVNAAH PPAWPTANGW
DYNWDKREPS SMVNGKRKES TGENGSQDAE NNKPRATRHI FLIRHSQYNL KGDGDKERFL
TPLGREQAEF TGQRLASFGL KYDTLIHSSM TRATETANII SKYLPGVELV SCDLLREGAP
IEPVPPVTHW KPEAVQYHED GARIEAAFRR YIHRADAKQK EDSYEIIVCH ANVIRYFVCR
ALQFPPEGWL RLGLNNGSIT WLTVRPSGRV SLRALGDSGF MPPDKLTRT
