MLN_MOUSE
ID MLN_MOUSE Reviewed; 46 AA.
AC Q9CV60;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Myoregulin {ECO:0000303|PubMed:25640239};
GN Name=Mrln {ECO:0000312|MGI:MGI:1916813};
GN Synonyms=Mln {ECO:0000303|PubMed:25640239};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATP2A1, AND MUTAGENESIS
RP OF LYS-27; LEU-29; PHE-30; PHE-33 AND ASP-35.
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).
RN [4]
RP FUNCTION.
RX PubMed=26816378; DOI=10.1126/science.aad4076;
RA Nelson B.R., Makarewich C.A., Anderson D.M., Winders B.R., Troupes C.D.,
RA Wu F., Reese A.L., McAnally J.R., Chen X., Kavalali E.T., Cannon S.C.,
RA Houser S.R., Bassel-Duby R., Olson E.N.;
RT "Muscle physiology. A peptide encoded by a transcript annotated as long
RT noncoding RNA enhances SERCA activity in muscle.";
RL Science 351:271-275(2016).
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:0000269|PubMed:25640239, ECO:0000269|PubMed:26816378}.
CC -!- SUBUNIT: Interacts with ATP2A1/SERCA1. {ECO:0000269|PubMed:25640239}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25640239}; Single-pass membrane protein
CC {ECO:0000305|PubMed:25640239}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in all skeletal muscles. Not
CC expressed in cardiac or smooth muscles. {ECO:0000269|PubMed:25640239}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, expressed in the myotomal
CC compartment of the somites and the anlagen of skeletal muscle. During
CC fetal and adult stages, strongly expressed in all skeletal muscles. Not
CC detectable in cardiac or smooth muscles. {ECO:0000269|PubMed:25640239}.
CC -!- INDUCTION: Expression is regulated by MYEF2 and MYOD1.
CC {ECO:0000269|PubMed:25640239}.
CC -!- DISRUPTION PHENOTYPE: Mice were born at expected Mendelian ratios and
CC did not show no obvious morphological abnormalities or differences in
CC body or muscle weights. They however show enhanced Ca(2+) handling in
CC skeletal muscle and improved exercise performance.
CC {ECO:0000269|PubMed:25640239}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26234.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDL31981.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK009351; BAB26234.1; ALT_INIT; mRNA.
DR EMBL; CH466553; EDL31981.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS88021.1; -.
DR RefSeq; NP_001291668.1; NM_001304739.1.
DR RefSeq; XP_017169565.1; XM_017314076.1.
DR AlphaFoldDB; Q9CV60; -.
DR PaxDb; Q9CV60; -.
DR PRIDE; Q9CV60; -.
DR Antibodypedia; 82464; 3 antibodies from 1 providers.
DR Ensembl; ENSMUST00000020090; ENSMUSP00000150523; ENSMUSG00000019933.
DR GeneID; 69563; -.
DR KEGG; mmu:69563; -.
DR CTD; 100507027; -.
DR MGI; MGI:1916813; Mrln.
DR VEuPathDB; HostDB:ENSMUSG00000019933; -.
DR GeneTree; ENSGT01030000235256; -.
DR InParanoid; Q9CV60; -.
DR OrthoDB; 1632299at2759; -.
DR BioGRID-ORCS; 69563; 0 hits in 2 CRISPR screens.
DR ChiTaRS; Mrln; mouse.
DR PRO; PR:Q9CV60; -.
DR Proteomes; UP000000589; Chromosome 10.
DR Bgee; ENSMUSG00000019933; Expressed in knee joint and 132 other tissues.
DR ExpressionAtlas; Q9CV60; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; IMP:MGI.
DR GO; GO:1901895; P:negative regulation of ATPase-coupled calcium transmembrane transporter activity; IDA:MGI.
DR GO; GO:1901877; P:negative regulation of calcium ion binding; IDA:MGI.
DR GO; GO:1902081; P:negative regulation of calcium ion import into sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0009611; P:response to wounding; IEP:MGI.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Sarcoplasmic reticulum; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..46
FT /note="Myoregulin"
FT /id="PRO_0000432709"
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"
FT MUTAGEN 27
FT /note="K->A: Does not affect interaction with ATP2A1."
FT /evidence="ECO:0000269|PubMed:25640239"
FT MUTAGEN 29
FT /note="L->A: Abolishes interaction with ATP2A1/SERCA1."
FT /evidence="ECO:0000269|PubMed:25640239"
FT MUTAGEN 30
FT /note="F->A: Abolishes interaction with ATP2A1/SERCA1."
FT /evidence="ECO:0000269|PubMed:25640239"
FT MUTAGEN 33
FT /note="F->A: Abolishes interaction with ATP2A1/SERCA1."
FT /evidence="ECO:0000269|PubMed:25640239"
FT MUTAGEN 35
FT /note="D->A: Does not affect interaction with ATP2A1."
FT /evidence="ECO:0000269|PubMed:25640239"
SQ SEQUENCE 46 AA; 5175 MW; A5B8AC1E0DFA904A CRC64;
MSGKSWVLIS TTSPQSLEDE ILGRLLKILF VLFVDLMSIM YVVITS
