MYL3_MOUSE
ID MYL3_MOUSE Reviewed; 204 AA.
AC P09542; Q3UIF4; Q9CQZ2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Myosin light chain 3 {ECO:0000305};
DE AltName: Full=Myosin alkali light chain 1, ventricular/slow skeletal muscle isoform {ECO:0000305|PubMed:3194193};
DE AltName: Full=Myosin light chain 1, slow-twitch muscle B/ventricular isoform {ECO:0000250|UniProtKB:P08590};
DE Short=MLC1SB {ECO:0000250|UniProtKB:P08590};
GN Name=Myl3 {ECO:0000312|MGI:MGI:97268};
GN Synonyms=Mlc1v {ECO:0000312|MGI:MGI:97268},
GN Mylc {ECO:0000312|MGI:MGI:97268};
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=Embryo, Heart, and Kidney;
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 MRNA].
RC TISSUE=Heart, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RC STRAIN=C3H/HeJ; TISSUE=Spleen;
RX PubMed=3194193; DOI=10.1093/nar/16.21.10037;
RA Cohen A., Barton P.J.R., Robert B., Garner I., Alonso S., Buckingham M.E.;
RT "Promoter analysis of myosin alkali light chain genes expressed in mouse
RT striated muscle.";
RL Nucleic Acids Res. 16:10037-10052(1988).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-136 AND SER-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT ALA-2.
RX PubMed=20668449; DOI=10.1038/nature09343;
RA Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
RA Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
RT "NRMT is an alpha-N-methyltransferase that methylates RCC1 and
RT retinoblastoma protein.";
RL Nature 466:1125-1128(2010).
CC -!- FUNCTION: Regulatory light chain of myosin. Does not bind calcium.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1.
CC {ECO:0000269|PubMed:20668449}.
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DR EMBL; AK002312; BAB22006.1; -; mRNA.
DR EMBL; AK011518; BAB27672.1; -; mRNA.
DR EMBL; AK146943; BAE27552.1; -; mRNA.
DR EMBL; BC061222; AAH61222.1; -; mRNA.
DR EMBL; X12972; CAA31415.1; -; Genomic_DNA.
DR CCDS; CCDS23571.1; -.
DR PIR; S01945; S01945.
DR RefSeq; NP_034989.1; NM_010859.2.
DR AlphaFoldDB; P09542; -.
DR SMR; P09542; -.
DR BioGRID; 201654; 1.
DR IntAct; P09542; 2.
DR STRING; 10090.ENSMUSP00000078715; -.
DR iPTMnet; P09542; -.
DR PhosphoSitePlus; P09542; -.
DR UCD-2DPAGE; P09542; -.
DR EPD; P09542; -.
DR MaxQB; P09542; -.
DR PaxDb; P09542; -.
DR PeptideAtlas; P09542; -.
DR PRIDE; P09542; -.
DR ProteomicsDB; 286119; -.
DR Antibodypedia; 12839; 390 antibodies from 35 providers.
DR DNASU; 17897; -.
DR Ensembl; ENSMUST00000079784; ENSMUSP00000078715; ENSMUSG00000059741.
DR GeneID; 17897; -.
DR KEGG; mmu:17897; -.
DR UCSC; uc009rur.1; mouse.
DR CTD; 4634; -.
DR MGI; MGI:97268; Myl3.
DR VEuPathDB; HostDB:ENSMUSG00000059741; -.
DR eggNOG; KOG0030; Eukaryota.
DR GeneTree; ENSGT01030000234570; -.
DR HOGENOM; CLU_061288_13_0_1; -.
DR InParanoid; P09542; -.
DR OMA; YDRTPKC; -.
DR OrthoDB; 1470794at2759; -.
DR PhylomeDB; P09542; -.
DR TreeFam; TF351553; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 17897; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Myl3; mouse.
DR PRO; PR:P09542; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P09542; protein.
DR Bgee; ENSMUSG00000059741; Expressed in interventricular septum and 165 other tissues.
DR ExpressionAtlas; P09542; baseline and differential.
DR Genevisible; P09542; MM.
DR GO; GO:0031672; C:A band; ISO:MGI.
DR GO; GO:0031674; C:I band; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; ISO:MGI.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003774; F:cytoskeletal motor activity; ISO:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR GO; GO:0006942; P:regulation of striated muscle contraction; ISO:MGI.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:MGI.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Methylation; Motor protein; Muscle protein; Myosin; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20668449"
FT CHAIN 2..204
FT /note="Myosin light chain 3"
FT /id="PRO_0000198697"
FT DOMAIN 58..95
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 137..172
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 172..204
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine; by NTM1"
FT /evidence="ECO:0000269|PubMed:20668449"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16409"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16409"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16409"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 204 AA; 22422 MW; 3DF39389FF5BAB41 CRC64;
MAPKKPEPKK DDAKAAAPKA APAPAAAPAA APAAAPEPER PKEAEFDASK IKIEFTPEQI
EEFKEAFLLF DRTPKGEMKI TYGQCGDVLR ALGQNPTQAE VLRVLGKPKQ EELNSKMMDF
ETFLPMLQHI SKNKDTGTYE DFVEGLRVFD KEGNGTVMGA ELRHVLATLG ERLTEDEVEK
LMAGQEDSNG CINYEAFVKH IMAS
