ID   MLN_HUMAN               Reviewed;          46 AA.
AC   P0DMT0;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Myoregulin {ECO:0000303|PubMed:25640239};
GN   Name=MRLN {ECO:0000312|HGNC:HGNC:48649};
GN   Synonyms=MLN {ECO:0000303|PubMed:25640239};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Woessner J., Tan F., Marra M., Kucaba T., Yandell M., Martin J., Marth G.,
RA   Bowles L., Wylie T., Bowers Y., Steptoe M., Theising B., Geisel S.,
RA   Allen M., Underwood K., Chappell J., Person B., Gibbons M., Harvey N.,
RA   Pape D., Chamberlain A., Morales R., Schurk R., Ritter E., Kohn S.,
RA   Swaller T., Behymer K., Hillier L., Wilson R., Waterston R.;
RT   "Full clone sequencing of the longest available member from each UniGene
RT   cluster.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=25640239; DOI=10.1016/j.cell.2015.01.009;
RA   Anderson D.M., Anderson K.M., Chang C.L., Makarewich C.A., Nelson B.R.,
RA   McAnally J.R., Kasaragod P., Shelton J.M., Liou J., Bassel-Duby R.,
RA   Olson E.N.;
RT   "A micropeptide encoded by a putative long noncoding RNA regulates muscle
RT   performance.";
RL   Cell 160:595-606(2015).
CC   -!- FUNCTION: Inhibits the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic
CC       reticulum by decreasing the apparent affinity of the ATPase for Ca(2+),
CC       thereby acting as a key regulator of skeletal muscle activity. Its high
CC       expression in adult skeletal muscle, suggests that it constitutes the
CC       predominant regulator of ATP2A1/SERCA1 in adult skeletal muscle.
CC       {ECO:0000250|UniProtKB:Q9CV60, ECO:0000269|PubMed:25640239}.
CC   -!- SUBUNIT: Interacts with ATP2A1/SERCA1. {ECO:0000250|UniProtKB:Q9CV60}.
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9CV60}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9CV60}.
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DR   EMBL; AF086308; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC022027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS81467.1; -.
DR   RefSeq; NP_001291660.1; NM_001304731.1.
DR   RefSeq; NP_001291661.1; NM_001304732.1.
DR   AlphaFoldDB; P0DMT0; -.
DR   TCDB; 1.A.50.3.1; the phospholamban (ca(2+)-channel and ca(2+)-atpase regulator) (plb) family.
DR   BioMuta; MRLN; -.
DR   PRIDE; P0DMT0; -.
DR   Antibodypedia; 82464; 3 antibodies from 1 providers.
DR   DNASU; 100507027; -.
DR   Ensembl; ENST00000414264.6; ENSP00000488748.1; ENSG00000227877.7.
DR   Ensembl; ENST00000430431.5; ENSP00000488299.1; ENSG00000227877.7.
DR   Ensembl; ENST00000594536.5; ENSP00000488584.1; ENSG00000227877.7.
DR   Ensembl; ENST00000628562.1; ENSP00000488429.1; ENSG00000227877.7.
DR   GeneID; 100507027; -.
DR   KEGG; hsa:100507027; -.
DR   MANE-Select; ENST00000414264.6; ENSP00000488748.1; NM_001304731.2; NP_001291660.1.
DR   CTD; 100507027; -.
DR   DisGeNET; 100507027; -.
DR   GeneCards; MRLN; -.
DR   HGNC; HGNC:48649; MRLN.
DR   HPA; ENSG00000227877; Group enriched (skeletal muscle, tongue).
DR   MIM; 616246; gene.
DR   neXtProt; NX_P0DMT0; -.
DR   OpenTargets; ENSG00000227877; -.
DR   VEuPathDB; HostDB:ENSG00000227877; -.
DR   GeneTree; ENSGT01030000235256; -.
DR   HOGENOM; CLU_3191042_0_0_1; -.
DR   OrthoDB; 1632299at2759; -.
DR   PathwayCommons; P0DMT0; -.
DR   BioGRID-ORCS; 100507027; 1 hit in 64 CRISPR screens.
DR   Pharos; P0DMT0; Tdark.
DR   PRO; PR:P0DMT0; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000227877; Expressed in biceps brachii and 120 other tissues.
DR   Genevisible; P0DMT0; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
DR   GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:1901895; P:negative regulation of ATPase-coupled calcium transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:1901877; P:negative regulation of calcium ion binding; IEA:Ensembl.
DR   GO; GO:1902081; P:negative regulation of calcium ion import into sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
PE   3: Inferred from homology;
KW   Membrane; Reference proteome; Sarcoplasmic reticulum; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..46
FT                   /note="Myoregulin"
FT                   /id="PRO_0000432708"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..46
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   46 AA;  5194 MW;  A9EAAA73A24C49B8 CRC64;
     MTGKNWILIS TTTPKSLEDE IVGRLLKILF VIFVDLISII YVVITS