ID   PGAM5_XENLA             Reviewed;         275 AA.
AC   Q5FWM4; Q8AVL5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg, and Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH41756.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC041756; AAH41756.1; ALT_FRAME; mRNA.
DR   EMBL; BC089282; AAH89282.1; -; mRNA.
DR   RefSeq; NP_001082456.1; NM_001088987.1.
DR   AlphaFoldDB; Q5FWM4; -.
DR   SMR; Q5FWM4; -.
DR   DNASU; 398484; -.
DR   GeneID; 398484; -.
DR   KEGG; xla:398484; -.
DR   AGR; Xenbase:XB-GENE-6256307; -.
DR   CTD; 398484; -.
DR   Xenbase; XB-GENE-6256307; pgam5.S.
DR   OrthoDB; 2994603at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 398484; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR20935; PHOSPHOGLYCERATE MUTASE-RELATED; 1.
DR   PANTHER; PTHR20935:SF0; SERINE_THREONINE-PROTEIN PHOSPHATASE PGAM5, MITOCHONDRIAL; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane; Necrosis;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..275
FT                   /note="Serine/threonine-protein phosphatase PGAM5,
FT                   mitochondrial"
FT                   /id="PRO_0000288786"
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   275 AA;  30986 MW;  79FC0F89F205D48E CRC64;
     MYLRRALIAG GSAAAAILGV VAAGKSKGGS DSEILSVAPP ATGQWDRNWD RREPISMVNL
     SKINAETGEE ELQLHLNKHK PKATRHIFLI RHSQYKLDGK TDFDRVLTPL GREQADLTGQ
     RLASLGHKYN HIVYSTMTRA KETTEIISKY LPDVNKSSSD LLREGAPIRP EPQVCHWKPD
     FVYYEDGPRI EAAFRHFIHR ADPKQEEDSY EILICHANVI RYVVCRALQF PPEAWLRISL
     NNGSITYLVI RPNGNVSIRM LGDSGFMPAE KISRT
//