ID   MYL1_HUMAN              Reviewed;         194 AA.
AC   P05976; B2R4N6; B2R4T6; P06741; Q6IBD5;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Myosin light chain 1/3, skeletal muscle isoform;
DE            Short=MLC1/MLC3;
DE            Short=MLC1F/MLC3F;
DE   AltName: Full=Myosin light chain alkali 1/2;
DE            Short=Myosin light chain A1/A2;
GN   Name=MYL1;
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 [MRNA] (ISOFORMS MLC1 AND MLC3).
RC   TISSUE=Fetal muscle;
RX   PubMed=3601661; DOI=10.1093/nar/15.12.4989;
RA   Seidel U., Bober E., Winter B., Lenz S., Lohse P., Arnold H.H.;
RT   "The complete nucleotide sequences of cDNA clones coding for human myosin
RT   light chains 1 and 3.";
RL   Nucleic Acids Res. 15:4989-4989(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MLC1 AND MLC3).
RX   PubMed=2458299; DOI=10.1016/0378-1119(88)90231-4;
RA   Seidel U., Bober E., Winter B., Lenz S., Lohse P., Goedde H., Grzeschik K.,
RA   Arnold H.H.;
RT   "Alkali myosin light chains in man are encoded by a multigene family that
RT   includes the adult skeletal muscle, the embryonic or atrial, and
RT   nonsarcomeric isoforms.";
RL   Gene 66:135-146(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MLC1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MLC1 AND MLC3).
RC   TISSUE=Skeletal muscle;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MLC3).
RC   TISSUE=Liver;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RX   PubMed=2777779; DOI=10.1016/s0021-9258(18)71593-7;
RA   Seidel U., Arnold H.H.;
RT   "Identification of the functional promoter regions in the human gene
RT   encoding the myosin alkali light chains MLC1 and MLC3 of fast skeletal
RT   muscle.";
RL   J. Biol. Chem. 264:16109-16117(1989).
RN   [8]
RP   INVOLVEMENT IN CMYP14, FUNCTION, VARIANT CMYP14 ARG-163, AND
RP   CHARACTERIZATION OF VARIANT CMYP14 ARG-163.
RX   PubMed=30215711; DOI=10.1093/hmg/ddy320;
RG   UK10K Consortium;
RA   Ravenscroft G., Zaharieva I.T., Bortolotti C.A., Lambrughi M.,
RA   Pignataro M., Borsari M., Sewry C.A., Phadke R., Haliloglu G., Ong R.,
RA   Goullee H., Whyte T., Manzur A., Talim B., Kaya U., Osborn D.P.S.,
RA   Forrest A.R.R., Laing N.G., Muntoni F.;
RT   "Bi-allelic mutations in MYL1 cause a severe congenital myopathy.";
RL   Hum. Mol. Genet. 27:4263-4272(2018).
CC   -!- FUNCTION: Non-regulatory myosin light chain required for proper
CC       formation and/or maintenance of myofibers, and thus appropriate muscle
CC       function. {ECO:0000269|PubMed:30215711}.
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. Does
CC       not bind calcium. {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=MLC1;
CC         IsoId=P05976-1; Sequence=Displayed;
CC       Name=MLC3;
CC         IsoId=P05976-2, P06741-1; Sequence=VSP_038686;
CC   -!- PTM: [Isoform MLC3]: Acetylated at position 2. {ECO:0000250}.
CC   -!- DISEASE: Congenital myopathy 14 (CMYP14) [MIM:618414]: An autosomal
CC       recessive congenital myopathy characterized by decreased fetal
CC       movements, severe muscle weakness and respiratory failure. Additional
CC       features include delayed motor development, areflexia, facial weakness,
CC       normal eye movements, head lag, and mild contractures. Skeletal muscle
CC       biopsy shows variation in fiber size with atrophy of the fast-twitch
CC       type II fibers. {ECO:0000269|PubMed:30215711}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
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DR   EMBL; X05450; CAB42646.1; -; mRNA.
DR   EMBL; X05451; CAA29020.1; -; mRNA.
DR   EMBL; M20642; AAA59854.1; -; mRNA.
DR   EMBL; M20643; AAA59855.1; -; mRNA.
DR   EMBL; CR456869; CAG33150.1; -; mRNA.
DR   EMBL; AK311942; BAG34883.1; -; mRNA.
DR   EMBL; AK311892; BAG34833.1; -; mRNA.
DR   EMBL; CH471063; EAW70483.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70484.1; -; Genomic_DNA.
DR   EMBL; BC005318; AAH05318.1; -; mRNA.
DR   EMBL; J05026; AAA66960.1; -; Genomic_DNA.
DR   CCDS; CCDS2390.1; -. [P05976-1]
DR   CCDS; CCDS2391.1; -. [P05976-2]
DR   PIR; JS0431; MOHUA1.
DR   PIR; S07939; MOHUA2.
DR   RefSeq; NP_524144.1; NM_079420.2. [P05976-1]
DR   RefSeq; NP_524146.1; NM_079422.2. [P05976-2]
DR   AlphaFoldDB; P05976; -.
DR   SMR; P05976; -.
DR   BioGRID; 110716; 59.
DR   IntAct; P05976; 15.
DR   STRING; 9606.ENSP00000307280; -.
DR   GlyGen; P05976; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P05976; -.
DR   PhosphoSitePlus; P05976; -.
DR   BioMuta; MYL1; -.
DR   DMDM; 127128; -.
DR   EPD; P05976; -.
DR   jPOST; P05976; -.
DR   MassIVE; P05976; -.
DR   MaxQB; P05976; -.
DR   PaxDb; 9606-ENSP00000307280; -.
DR   PeptideAtlas; P05976; -.
DR   ProteomicsDB; 51863; -. [P05976-1]
DR   ProteomicsDB; 51864; -. [P05976-2]
DR   Pumba; P05976; -.
DR   Antibodypedia; 20019; 257 antibodies from 26 providers.
DR   DNASU; 4632; -.
DR   Ensembl; ENST00000341685.8; ENSP00000343321.4; ENSG00000168530.16. [P05976-2]
DR   Ensembl; ENST00000352451.4; ENSP00000307280.4; ENSG00000168530.16. [P05976-1]
DR   GeneID; 4632; -.
DR   KEGG; hsa:4632; -.
DR   MANE-Select; ENST00000352451.4; ENSP00000307280.4; NM_079420.3; NP_524144.1.
DR   UCSC; uc002veb.4; human. [P05976-1]
DR   AGR; HGNC:7582; -.
DR   CTD; 4632; -.
DR   DisGeNET; 4632; -.
DR   GeneCards; MYL1; -.
DR   HGNC; HGNC:7582; MYL1.
DR   HPA; ENSG00000168530; Group enriched (skeletal muscle, tongue).
DR   MalaCards; MYL1; -.
DR   MIM; 160780; gene.
DR   MIM; 618414; phenotype.
DR   neXtProt; NX_P05976; -.
DR   OpenTargets; ENSG00000168530; -.
DR   Orphanet; 544602; Congenital myopathy with reduced type 2 muscle fibers.
DR   PharmGKB; PA31379; -.
DR   VEuPathDB; HostDB:ENSG00000168530; -.
DR   eggNOG; KOG0030; Eukaryota.
DR   GeneTree; ENSGT01030000234570; -.
DR   HOGENOM; CLU_061288_13_0_1; -.
DR   InParanoid; P05976; -.
DR   OMA; NPTNEEM; -.
DR   OrthoDB; 3080916at2759; -.
DR   PhylomeDB; P05976; -.
DR   TreeFam; TF351553; -.
DR   PathwayCommons; P05976; -.
DR   Reactome; R-HSA-390522; Striated Muscle Contraction.
DR   SignaLink; P05976; -.
DR   SIGNOR; P05976; -.
DR   BioGRID-ORCS; 4632; 12 hits in 1144 CRISPR screens.
DR   ChiTaRS; MYL1; human.
DR   GeneWiki; MYL1; -.
DR   GenomeRNAi; 4632; -.
DR   Pharos; P05976; Tbio.
DR   PRO; PR:P05976; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P05976; Protein.
DR   Bgee; ENSG00000168530; Expressed in skeletal muscle tissue of biceps brachii and 108 other cell types or tissues.
DR   GO; GO:0043292; C:contractile fiber; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005859; C:muscle myosin complex; NAS:BHF-UCL.
DR   GO; GO:0030016; C:myofibril; IDA:BHF-UCL.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0030017; C:sarcomere; NAS:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; IDA:BHF-UCL.
DR   GO; GO:0030049; P:muscle filament sliding; NAS:BHF-UCL.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23048; MYOSIN LIGHT CHAIN 1, 3; 1.
DR   PANTHER; PTHR23048:SF3; MYOSIN LIGHT CHAIN 1_3, SKELETAL MUSCLE ISOFORM; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   SWISS-2DPAGE; P05976; -.
DR   Genevisible; P05976; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Disease variant; Methylation;
KW   Motor protein; Muscle protein; Myosin; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02602"
FT   CHAIN           2..194
FT                   /note="Myosin light chain 1/3, skeletal muscle isoform"
FT                   /id="PRO_0000198681"
FT   DOMAIN          50..85
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          127..162
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          162..194
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N,N,N-trimethylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P02602"
FT   MOD_RES         71
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02600"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02600"
FT   MOD_RES         87
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02600"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02600"
FT   VAR_SEQ         1..53
FT                   /note="MAPKKDVKKPVAAAAAAPAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQ
FT                   D -> MSFSADQIA (in isoform MLC3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2458299,
FT                   ECO:0000303|PubMed:3601661"
FT                   /id="VSP_038686"
FT   VARIANT         163
FT                   /note="M -> R (in CMYP14; no protein detected by western
FT                   blot in patient muscle; dbSNP:rs1259220084)"
FT                   /evidence="ECO:0000269|PubMed:30215711"
FT                   /id="VAR_082312"
FT   CONFLICT        45
FT                   /note="I -> M (in Ref. 1; CAB42646)"
FT                   /evidence="ECO:0000305"
FT   INIT_MET        P05976-2:1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         P05976-2:2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  21145 MW;  DA1F5C5E4C8A2124 CRC64;
     MAPKKDVKKP VAAAAAAPAP APAPAPAPAP AKPKEEKIDL SAIKIEFSKE QQDEFKEAFL
     LFDRTGDSKI TLSQVGDVLR ALGTNPTNAE VRKVLGNPSN EELNAKKIEF EQFLPMMQAI
     SNNKDQATYE DFVEGLRVFD KEGNGTVMGA ELRHVLATLG EKMKEEEVEA LMAGQEDSNG
     CINYEAFVKH IMSI
//