ID   MP31_MOUSE              Reviewed;          35 AA.
AC   C0HLV9;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=PTEN upstream open reading frame MP31 {ECO:0000305};
DE   AltName: Full=Micropeptide 31 {ECO:0000303|PubMed:33406399};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=33406399; DOI=10.1016/j.cmet.2020.12.008;
RA   Huang N., Li F., Zhang M., Zhou H., Chen Z., Ma X., Yang L., Wu X.,
RA   Zhong J., Xiao F., Yang X., Zhao K., Li X., Xia X., Liu Z., Gao S.,
RA   Zhang N.;
RT   "An Upstream Open Reading Frame in Phosphatase and Tensin Homolog Encodes a
RT   Circuit Breaker of Lactate Metabolism.";
RL   Cell Metab. 33:128-144(2021).
RN   [3] {ECO:0000305}
RP   ERRATUM OF PUBMED:33406399.
RX   PubMed=33535099; DOI=10.1016/j.cmet.2021.01.008;
RA   Huang N., Li F., Zhang M., Zhou H., Chen Z., Ma X., Yang L., Wu X.,
RA   Zhong J., Xiao F., Yang X., Zhao K., Li X., Xia X., Liu Z., Gao S.,
RA   Zhang N.;
RL   Cell Metab. 33:454-454(2021).
CC   -!- FUNCTION: Inhibits lactate dehydrogenase (LDH)-mediated conversion of
CC       lactate to pyruvate in mitochondria by competing with mitochondrial LDH
CC       for binding to NAD(+). Also inhibits cellular lactate utilization.
CC       {ECO:0000250|UniProtKB:C0HLV8}.
CC   -!- SUBUNIT: Interacts with lactate dehydrogenases LDHA and LDHB;
CC       interaction with mitochondrial LDH leads to inhibition of lactate
CC       dehydrogenase activity, preventing conversion of lactate to pyruvate.
CC       {ECO:0000250|UniProtKB:C0HLV8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:C0HLV8}.
CC   -!- TISSUE SPECIFICITY: Detected in brain, kidney and liver (at protein
CC       level). {ECO:0000269|PubMed:33406399}.
CC   -!- DISRUPTION PHENOTYPE: Enhanced global lactate metabolism with elevated
CC       glucose consumption, increased ATP production and decreased perigonadal
CC       fat pad weight and fat/body weight ratio (PubMed:33406399). Elevated
CC       serum and secreted lactate levels (PubMed:33406399). Conditional
CC       knockout in astrocytes results in initiation of gliomagenesis and
CC       development of neurological symptoms that include seizure, ataxia
CC       and/or paralysis at 55-65 weeks of age (PubMed:33406399).
CC       {ECO:0000269|PubMed:33406399}.
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DR   EMBL; AC162887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; C0HLV9; -.
DR   SMR; C0HLV9; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0019516; P:lactate oxidation; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Mitochondrion; Reference proteome.
FT   CHAIN           1..35
FT                   /note="PTEN upstream open reading frame MP31"
FT                   /id="PRO_0000453001"
SQ   SEQUENCE   35 AA;  3689 MW;  13F74F7600875D54 CRC64;
     MWRDSLCTAA GYALGRRDAA ALSSLLSEAA AMMEV