MYL1_RABIT
ID MYL1_RABIT Reviewed; 192 AA.
AC P02602; P02603;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MLC1 AND MLC3).
RC TISSUE=Fast-twitch skeletal muscle;
RX PubMed=2147476; DOI=10.1093/nar/18.22.6688;
RA Mueller B., Maeda K., Wittinghofer A.;
RT "Sequence of the myosin light chain 1/3 isolated from a rabbit fast
RT skeletal muscle lambda library.";
RL Nucleic Acids Res. 18:6688-6688(1990).
RN [2]
RP PROTEIN SEQUENCE OF 3-192 (ISOFORMS MLC1 AND MLC3), CLEAVAGE OF INITIATOR
RP METHIONINE (ISOFORM MLC3), AND ACETYLATION AT SER-2 (ISOFORM MLC3).
RC TISSUE=Skeletal muscle;
RX PubMed=4838672; DOI=10.1111/j.1432-1033.1974.tb03489.x;
RA Frank G., Weeds A.G.;
RT "The amino-acid sequence of the alkali light chains of rabbit skeletal-
RT muscle myosin.";
RL Eur. J. Biochem. 44:317-334(1974).
RN [3]
RP SEQUENCE REVISION TO 141-142.
RX PubMed=1227935; DOI=10.1016/0014-5793(75)80375-9;
RA Weeds A.G.;
RT "Cyanogen bromide fragments of the cardiac I light chain from bovine
RT myosin: evidence for sequence homology with rabbit skeletal myosin alkali
RT light chains.";
RL FEBS Lett. 59:203-208(1975).
RN [4]
RP METHYLATION.
RA Henry G.D., Dalgarno D.C., Levine B.A., Trayer I.P.;
RT "Discovery of alpha-N-trimethylalanine in myosin light chains and its role
RT in actomyosin interaction.";
RL Biochem. Soc. Trans. 10:362-363(1982).
RN [5]
RP METHYLATION AT ALA-2.
RX PubMed=7106295; DOI=10.1016/0014-5793(82)80558-9;
RA Henry G.D., Dalgarno D.C., Marcus G., Scott M., Levine B.A., Trayer I.P.;
RT "The occurrence of alpha-N-trimethylalanine as the N-terminal amino acid of
RT some myosin light chains.";
RL FEBS Lett. 144:11-15(1982).
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=P02602-1; Sequence=Displayed;
CC Name=MLC3;
CC IsoId=P02602-2, P02603-1;
CC Sequence=VSP_038688;
CC -!- PTM: Isoform MLC3 is acetylated at position 2.
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DR EMBL; X54041; CAA37974.1; -; mRNA.
DR EMBL; X54044; CAA37977.1; -; mRNA.
DR PIR; S12693; MORBL2.
DR PIR; S15061; MORBLA.
DR RefSeq; NP_001095183.1; NM_001101713.1. [P02602-1]
DR RefSeq; XP_008257145.1; XM_008258923.1. [P02602-2]
DR PDB; 5H53; EM; 5.20 A; C=41-192.
DR PDB; 6YSY; X-ray; 3.25 A; B=1-192.
DR PDBsum; 5H53; -.
DR PDBsum; 6YSY; -.
DR AlphaFoldDB; P02602; -.
DR SMR; P02602; -.
DR IntAct; P02602; 1.
DR MINT; P02602; -.
DR STRING; 9986.ENSOCUP00000022702; -.
DR iPTMnet; P02602; -.
DR Ensembl; ENSOCUT00000030846; ENSOCUP00000022702; ENSOCUG00000014182. [P02602-2]
DR Ensembl; ENSOCUT00000061230; ENSOCUP00000049094; ENSOCUG00000014182. [P02602-1]
DR GeneID; 100009400; -.
DR KEGG; ocu:100009400; -.
DR CTD; 4632; -.
DR eggNOG; KOG0030; Eukaryota.
DR GeneTree; ENSGT01030000234570; -.
DR InParanoid; P02602; -.
DR OrthoDB; 1470794at2759; -.
DR TreeFam; TF351553; -.
DR SABIO-RK; P02602; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000014182; Expressed in skeletal muscle tissue and 12 other tissues.
DR ExpressionAtlas; P02602; baseline.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Methylation; Motor protein; Muscle protein; Myosin; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..192
FT /note="Myosin light chain 1/3, skeletal muscle isoform"
FT /id="PRO_0000198683"
FT DOMAIN 48..83
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 125..160
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 160..192
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000269|PubMed:7106295"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02600"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02600"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02600"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02600"
FT VAR_SEQ 1..51
FT /note="MAPKKDVKKPAAAAAPAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQD
FT -> MSFSADQIA (in isoform MLC3)"
FT /evidence="ECO:0000303|PubMed:2147476"
FT /id="VSP_038688"
FT CONFLICT 6
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="A -> KA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..100
FT /note="NEE -> DEQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..145
FT /note="NGTV -> DTVG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:6YSY"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6YSY"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:6YSY"
FT INIT_MET P02602-2:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4838672"
FT MOD_RES P02602-2:2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:4838672"
SQ SEQUENCE 192 AA; 20949 MW; A2F57A179F2158D6 CRC64;
MAPKKDVKKP AAAAAPAPAP APAPAPAPAK PKEEKIDLSA IKIEFSKEQQ DEFKEAFLLY
DRTGDSKITL SQVGDVLRAL GTNPTNAEVK KVLGNPSNEE MNAKKIEFEQ FLPMLQAISN
NKDQGTYEDF VEGLRVFDKE GNGTVMGAEL RHVLATLGEK MKEEEVEALM AGQEDSNGCI
NYEAFVKHIM SI
