MYMX_MOUSE
ID MYMX_MOUSE Reviewed; 84 AA.
AC Q2Q5T5; E9PXI1;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein myomixer {ECO:0000303|PubMed:28386024};
DE AltName: Full=Embryonic stem cell- and germ cell-specific protein {ECO:0000303|PubMed:16331322};
DE Short=ESGP {ECO:0000303|PubMed:16331322};
DE AltName: Full=Microprotein inducer of fusion {ECO:0000303|PubMed:28569745};
DE Short=Protein minion {ECO:0000303|PubMed:28569745};
DE AltName: Full=Protein myomerger {ECO:0000303|PubMed:28569755, ECO:0000303|PubMed:30197239};
GN Name=Mymx {ECO:0000312|MGI:MGI:3649059};
GN Synonyms=Gm7325 {ECO:0000312|MGI:MGI:3649059};
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RX PubMed=16331322; DOI=10.1111/j.1745-7270.2005.00120.x;
RA Chen Y.M., Du Z.W., Yao Z.;
RT "Molecular cloning and functional analysis of ESGP, an embryonic stem cell
RT and germ cell specific protein.";
RL Acta Biochim. Biophys. Sin. 37:789-796(2005).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=28569745; DOI=10.1038/ncomms15664;
RA Zhang Q., Vashisht A.A., O'Rourke J., Corbel S.Y., Moran R., Romero A.,
RA Miraglia L., Zhang J., Durrant E., Schmedt C., Sampath S.C., Sampath S.C.;
RT "The microprotein Minion controls cell fusion and muscle formation.";
RL Nat. Commun. 8:15664-15664(2017).
RN [4]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28569755; DOI=10.1038/ncomms15665;
RA Quinn M.E., Goh Q., Kurosaka M., Gamage D.G., Petrany M.J., Prasad V.,
RA Millay D.P.;
RT "Myomerger induces fusion of non-fusogenic cells and is required for
RT skeletal muscle development.";
RL Nat. Commun. 8:15665-15665(2017).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION
RP PHENOTYPE, INTERACTION WITH MYMK, AND MUTAGENESIS OF ARG-34; ARG-38; ARG-46
RP AND CYS-52.
RX PubMed=28386024; DOI=10.1126/science.aam9361;
RA Bi P., Ramirez-Martinez A., Li H., Cannavino J., McAnally J.R.,
RA Shelton J.M., Sanchez-Ortiz E., Bassel-Duby R., Olson E.N.;
RT "Control of muscle formation by the fusogenic micropeptide myomixer.";
RL Science 356:323-327(2017).
RN [6]
RP FUNCTION.
RX PubMed=29581287; DOI=10.1073/pnas.1800052115;
RA Bi P., McAnally J.R., Shelton J.M., Sanchez-Ortiz E., Bassel-Duby R.,
RA Olson E.N.;
RT "Fusogenic micropeptide Myomixer is essential for satellite cell fusion and
RT muscle regeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3864-3869(2018).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=30197239; DOI=10.1016/j.devcel.2018.08.006;
RA Leikina E., Gamage D.G., Prasad V., Goykhberg J., Crowe M., Diao J.,
RA Kozlov M.M., Chernomordik L.V., Millay D.P.;
RT "Myomaker and Myomerger work independently to control distinct steps of
RT membrane remodeling during myoblast fusion.";
RL Dev. Cell 46:767-780(2018).
CC -!- FUNCTION: Myoblast-specific protein that mediates myoblast fusion, an
CC essential step for the formation of multi-nucleated muscle fibers
CC (PubMed:28386024, PubMed:28569745, PubMed:28569755, PubMed:30197239).
CC Involved in membrane fusion downstream of the lipid mixing step
CC mediated by MYMK (PubMed:30197239). Acts by generating membrane
CC stresses via its extracellular C-terminus, leading to drive fusion pore
CC formation (PubMed:30197239). Acts independently of MYMK
CC (PubMed:30197239). Involved in skeletal muscle regeneration in response
CC to injury by mediating the fusion of satellite cells, a population of
CC muscle stem cells, with injured myofibers (PubMed:29581287).
CC {ECO:0000269|PubMed:28386024, ECO:0000269|PubMed:28569745,
CC ECO:0000269|PubMed:28569755, ECO:0000269|PubMed:29581287,
CC ECO:0000269|PubMed:30197239}.
CC -!- SUBUNIT: Interacts with MYMK (PubMed:28386024).
CC {ECO:0000269|PubMed:28386024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28386024,
CC ECO:0000269|PubMed:28569745, ECO:0000269|PubMed:28569755}; Single-pass
CC membrane protein {ECO:0000269|PubMed:30197239}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=myomerger-short {ECO:0000303|PubMed:28569755}, S
CC {ECO:0000303|PubMed:28569755};
CC IsoId=Q2Q5T5-1; Sequence=Displayed;
CC Name=2; Synonyms=myomerger-long {ECO:0000303|PubMed:28569755}, L
CC {ECO:0000303|PubMed:28569755};
CC IsoId=Q2Q5T5-2; Sequence=VSP_059105;
CC -!- TISSUE SPECIFICITY: Specifically expressed in developing skeletal
CC muscles throughout the limbs and body wall (PubMed:28569745,
CC PubMed:28569755, PubMed:28386024). {ECO:0000269|PubMed:28386024,
CC ECO:0000269|PubMed:28569745, ECO:0000269|PubMed:28569755}.
CC -!- INDUCTION: Up-regulated during differentiation of myoblasts
CC (PubMed:28569745, PubMed:28569755, PubMed:28386024). During muscle
CC regeneration (PubMed:28569745, PubMed:28569755, PubMed:28386024).
CC {ECO:0000269|PubMed:28386024, ECO:0000269|PubMed:28569745,
CC ECO:0000269|PubMed:28569755}.
CC -!- DOMAIN: The AxLyCxL motif is required for myoblast fusion.
CC {ECO:0000250|UniProtKB:P0DP88}.
CC -!- DISRUPTION PHENOTYPE: Perinatal death due to a reduction in fused
CC muscle fibers (PubMed:28569745). Embryos are motionless and lack
CC skeletal muscle: they are nearly transparent so that internal organs
CC and bones are apparent (PubMed:28386024). Myocytes differentiate and
CC harbor organized sarcomeres but are fusion-incompetent
CC (PubMed:28386024, PubMed:28569745, PubMed:28569755). Myoblast fusion is
CC impaired downstream of membrane lipid mixing step mediated by Mymk and
CC defects caused by the absence of Mymx are due to impaired fusion pore
CC formation (PubMed:30197239). Conditional deletion in activated muscle
CC stem cells (satellite cells) in adults abolishes satellite cell fusion
CC and prevents muscle regeneration, resulting in severe muscle
CC degeneration after injury (PubMed:29581287).
CC {ECO:0000269|PubMed:28386024, ECO:0000269|PubMed:28569745,
CC ECO:0000269|PubMed:28569755, ECO:0000269|PubMed:29581287,
CC ECO:0000269|PubMed:30197239}.
CC -!- SIMILARITY: Belongs to the MYMX family. {ECO:0000305}.
CC -!- CAUTION: Was initially reported to be specifically expressed in
CC embryonic stem cells and germ cells (PubMed:16331322). However, it was
CC later shown by different groups that it is specifically expressed in
CC myoblasts where it promotes myoblast fusion (PubMed:28569745,
CC PubMed:28569755, PubMed:28386024). {ECO:0000269|PubMed:16331322,
CC ECO:0000269|PubMed:28386024, ECO:0000269|PubMed:28569745,
CC ECO:0000269|PubMed:28569755}.
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DR EMBL; DQ190000; ABA86951.1; -; mRNA.
DR EMBL; AC163677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50119.1; -. [Q2Q5T5-1]
DR CCDS; CCDS50120.1; -. [Q2Q5T5-2]
DR RefSeq; NP_001170939.1; NM_001177468.1. [Q2Q5T5-1]
DR RefSeq; NP_001170940.1; NM_001177469.1. [Q2Q5T5-1]
DR RefSeq; NP_001170941.1; NM_001177470.1. [Q2Q5T5-2]
DR RefSeq; XP_006524852.1; XM_006524789.2. [Q2Q5T5-1]
DR RefSeq; XP_006524853.1; XM_006524790.1. [Q2Q5T5-1]
DR AlphaFoldDB; Q2Q5T5; -.
DR SMR; Q2Q5T5; -.
DR STRING; 10090.ENSMUSP00000126690; -.
DR PRIDE; Q2Q5T5; -.
DR ProteomicsDB; 287534; -. [Q2Q5T5-1]
DR ProteomicsDB; 287535; -. [Q2Q5T5-2]
DR Antibodypedia; 78826; 5 antibodies from 3 providers.
DR Ensembl; ENSMUST00000113529; ENSMUSP00000109157; ENSMUSG00000079471. [Q2Q5T5-1]
DR Ensembl; ENSMUST00000169137; ENSMUSP00000126690; ENSMUSG00000079471. [Q2Q5T5-2]
DR Ensembl; ENSMUST00000178858; ENSMUSP00000137630; ENSMUSG00000079471. [Q2Q5T5-1]
DR Ensembl; ENSMUST00000208801; ENSMUSP00000146823; ENSMUSG00000079471. [Q2Q5T5-1]
DR GeneID; 653016; -.
DR KEGG; mmu:653016; -.
DR UCSC; uc008crg.2; mouse. [Q2Q5T5-1]
DR CTD; 101929726; -.
DR MGI; MGI:3649059; Mymx.
DR VEuPathDB; HostDB:ENSMUSG00000079471; -.
DR eggNOG; ENOG502T3SF; Eukaryota.
DR GeneTree; ENSGT00490000044373; -.
DR HOGENOM; CLU_2460615_0_0_1; -.
DR OMA; CLGSQDM; -.
DR OrthoDB; 1636462at2759; -.
DR PhylomeDB; Q2Q5T5; -.
DR BioGRID-ORCS; 653016; 3 hits in 65 CRISPR screens.
DR PRO; PR:Q2Q5T5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q2Q5T5; protein.
DR Bgee; ENSMUSG00000079471; Expressed in internal carotid artery and 104 other tissues.
DR ExpressionAtlas; Q2Q5T5; baseline and differential.
DR Genevisible; E9PXI1; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; IDA:UniProtKB.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:0045026; P:plasma membrane fusion; IDA:UniProtKB.
DR GO; GO:0060538; P:skeletal muscle organ development; IMP:UniProtKB.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:UniProtKB.
DR InterPro; IPR039014; Myomixer.
DR PANTHER; PTHR41686; PTHR41686; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Myogenesis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..84
FT /note="Protein myomixer"
FT /id="PRO_5010681111"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30197239"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..84
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30197239"
FT REGION 60..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..57
FT /note="AxLyCxL"
FT /evidence="ECO:0000250|UniProtKB:P0DP88"
FT COMPBIAS 69..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1
FT /note="M -> MPEESCTVKLIQLKTGEYRGAGPAM (in isoform 2)"
FT /id="VSP_059105"
FT MUTAGEN 34
FT /note="R->E: Decreased interaction with MYMK without
FT affecting localization to the cell membrane."
FT /evidence="ECO:0000269|PubMed:28386024"
FT MUTAGEN 38
FT /note="R->E: Decreased interaction with MYMK without
FT affecting localization to the cell membrane."
FT /evidence="ECO:0000269|PubMed:28386024"
FT MUTAGEN 46
FT /note="R->E: Decreased interaction with MYMK without
FT affecting localization to the cell membrane."
FT /evidence="ECO:0000269|PubMed:28386024"
FT MUTAGEN 52
FT /note="C->A: Abolishes the ability to mediate myoblast
FT fusion; does not affect interaction with MYMK; does not
FT affect localization to the cell membrane."
FT /evidence="ECO:0000269|PubMed:28386024"
SQ SEQUENCE 84 AA; 9598 MW; 437421DE3152FA47 CRC64;
MPVPLLPMVL RSLLSRLLLP VARLARQHLL PLLRRLARRL SSQDMREALL SCLLFVLSQQ
QPPDSGEASR VDHSQRKERL GPQK
