MYL1_RAT
ID MYL1_RAT Reviewed; 189 AA.
AC P02600; P02601;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=6092382; DOI=10.1016/s0021-9258(18)90735-0;
RA Periasamy M., Strehler E.E., Garfinkel L.I., Gubits R.M., Ruiz-Opazo N.,
RA Nadal-Ginard B.;
RT "Fast skeletal muscle myosin light chains 1 and 3 are produced from a
RT single gene by a combined process of differential RNA transcription and
RT splicing.";
RL J. Biol. Chem. 259:13595-13604(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3018505; DOI=10.1128/mcb.5.11.3168-3182.1985;
RA Strehler E.E., Periasamy M., Strehler-Page M.-A., Nadal-Ginard B.;
RT "Myosin light-chain 1 and 3 gene has two structurally distinct and
RT differentially regulated promoters evolving at different rates.";
RL Mol. Cell. Biol. 5:3168-3182(1985).
RN [3]
RP PROTEIN SEQUENCE OF 119-131, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (DEC-2006) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66; SER-68; THR-82 AND
RP SER-94, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM MLC3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Non-regulatory myosin light chain required for proper
CC formation and/or maintenance of myofibers, and thus appropriate muscle
CC function. {ECO:0000250|UniProtKB:P05976}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains. Does
CC not bind calcium. {ECO:0000250|UniProtKB:P05976}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=MLC1;
CC IsoId=P02600-1; Sequence=Displayed;
CC Name=MLC3;
CC IsoId=P02600-2, P02601-1;
CC Sequence=VSP_038689;
CC -!- PTM: Isoform MLC3 is acetylated at position 2. {ECO:0000250}.
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DR EMBL; L00088; AAA98533.1; -; Genomic_DNA.
DR EMBL; K02423; AAA98533.1; JOINED; Genomic_DNA.
DR EMBL; K02426; AAA98533.1; JOINED; Genomic_DNA.
DR EMBL; L00085; AAA98533.1; JOINED; Genomic_DNA.
DR EMBL; L00086; AAA98533.1; JOINED; Genomic_DNA.
DR EMBL; L00087; AAA98533.1; JOINED; Genomic_DNA.
DR EMBL; L00088; AAA98534.1; -; Genomic_DNA.
DR EMBL; K02424; AAA98534.1; JOINED; Genomic_DNA.
DR EMBL; K02425; AAA98534.1; JOINED; Genomic_DNA.
DR EMBL; L00085; AAA98534.1; JOINED; Genomic_DNA.
DR EMBL; L00086; AAA98534.1; JOINED; Genomic_DNA.
DR EMBL; L00087; AAA98534.1; JOINED; Genomic_DNA.
DR EMBL; M12021; AAA41622.1; -; Genomic_DNA.
DR EMBL; M12017; AAA41622.1; JOINED; Genomic_DNA.
DR EMBL; M12018; AAA41622.1; JOINED; Genomic_DNA.
DR EMBL; M12019; AAA41622.1; JOINED; Genomic_DNA.
DR EMBL; M12020; AAA41622.1; JOINED; Genomic_DNA.
DR EMBL; M12021; AAA41623.1; -; Genomic_DNA.
DR EMBL; M12018; AAA41623.1; JOINED; Genomic_DNA.
DR EMBL; M12019; AAA41623.1; JOINED; Genomic_DNA.
DR EMBL; M12020; AAA41623.1; JOINED; Genomic_DNA.
DR PIR; A03034; MORTA1.
DR PIR; I57590; I57590.
DR PIR; I77418; MORTA2.
DR RefSeq; NP_001071124.1; NM_001077656.1. [P02600-1]
DR RefSeq; NP_064489.1; NM_020104.2. [P02600-2]
DR AlphaFoldDB; P02600; -.
DR SMR; P02600; -.
DR BioGRID; 248582; 3.
DR IntAct; P02600; 3.
DR MINT; P02600; -.
DR STRING; 10116.ENSRNOP00000017838; -.
DR iPTMnet; P02600; -.
DR PhosphoSitePlus; P02600; -.
DR jPOST; P02600; -.
DR PaxDb; P02600; -.
DR PRIDE; P02600; -.
DR Ensembl; ENSRNOT00000017838; ENSRNOP00000017838; ENSRNOG00000013262. [P02600-1]
DR GeneID; 56781; -.
DR KEGG; rno:56781; -.
DR UCSC; RGD:1598796; rat. [P02600-1]
DR CTD; 4632; -.
DR RGD; 1598796; Myl1.
DR eggNOG; KOG0030; Eukaryota.
DR GeneTree; ENSGT01030000234570; -.
DR HOGENOM; CLU_061288_13_0_1; -.
DR InParanoid; P02600; -.
DR OMA; VAKHDDK; -.
DR OrthoDB; 1470794at2759; -.
DR PhylomeDB; P02600; -.
DR TreeFam; TF351553; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P02600; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000013262; Expressed in quadriceps femoris and 16 other tissues.
DR Genevisible; P02600; RN.
DR GO; GO:0043292; C:contractile fiber; IDA:RGD.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:RGD.
DR GO; GO:0006936; P:muscle contraction; ISO:RGD.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing; 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..189
FT /note="Myosin light chain 1/3, skeletal muscle isoform"
FT /id="PRO_0000198684"
FT DOMAIN 45..80
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 122..157
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 157..189
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..30
FT /note="Disordered"
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 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..48
FT /note="MAPKKDVKKPAAAAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQE ->
FT MSFSADQIA (in isoform MLC3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038689"
FT CONFLICT 26
FT /note="A -> APA (in Ref. 1; AAA98533)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="T -> I (in Ref. 2; AAA41622/AAA41623)"
FT /evidence="ECO:0000305"
FT INIT_MET P02600-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES P02600-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT MOD_RES P02600-2:2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 189 AA; 20680 MW; C8FC83CA793220B4 CRC64;
MAPKKDVKKP AAAAPAPAPA PAPAPAKPKE EKIDLSAIKI EFSKEQQEEF KEAFLLFDRT
GECKITLSQV GDVLRALGTN PTNAEVKKVL GNPSNEEMNA KKIEFEQFLP MMQAISNNKD
QGGYEDFVEG LRVFDKEGNG TVMGAELRHV LATLGEKMKE EEVEALLAGQ EDSNGCINYE
AFVKHIMSV
