ID   MYL1_BOVIN              Reviewed;         192 AA.
AC   A0JNJ5; Q29436;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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 {ECO:0000312|EMBL:AAI26717.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAI26717.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI26717.1};
RC   TISSUE=Fetal muscle {ECO:0000312|EMBL:AAI26717.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAA86910.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-192.
RC   TISSUE=Longissimus dorsi muscle {ECO:0000312|EMBL:AAA86910.1};
RX   PubMed=7762638; DOI=10.1152/ajpendo.1995.268.5.e858;
RA   Smith S.B., Davis S.K., Wilson J.J., Stone R.T., Wu F.Y., Garcia D.K.,
RA   Lunt D.K., Schiavetta A.M.;
RT   "Bovine fast-twitch myosin light chain 1: cloning and mRNA amount in muscle
RT   of cattle treated with clenbuterol.";
RL   Am. J. Physiol. 268:E858-E865(1995).
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}.
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DR   EMBL; BC126716; AAI26717.1; -; mRNA.
DR   EMBL; U45430; AAA86910.1; -; mRNA.
DR   RefSeq; NP_001073046.1; NM_001079578.1.
DR   RefSeq; XP_005202773.1; XM_005202716.2.
DR   AlphaFoldDB; A0JNJ5; -.
DR   SMR; A0JNJ5; -.
DR   STRING; 9913.ENSBTAP00000049636; -.
DR   PaxDb; A0JNJ5; -.
DR   PRIDE; A0JNJ5; -.
DR   Ensembl; ENSBTAT00000054271; ENSBTAP00000049636; ENSBTAG00000009707.
DR   GeneID; 317657; -.
DR   KEGG; bta:317657; -.
DR   CTD; 4632; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009707; -.
DR   VGNC; VGNC:31799; MYL1.
DR   eggNOG; KOG0030; Eukaryota.
DR   GeneTree; ENSGT01030000234570; -.
DR   HOGENOM; CLU_061288_13_0_1; -.
DR   InParanoid; A0JNJ5; -.
DR   OMA; VAKHDDK; -.
DR   OrthoDB; 1470794at2759; -.
DR   TreeFam; TF351553; -.
DR   Reactome; R-BTA-390522; Striated Muscle Contraction.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000009707; Expressed in biceps femoris and 76 other tissues.
DR   GO; GO:0043292; C:contractile fiber; IBA:GO_Central.
DR   GO; GO:0030016; C:myofibril; IEA:Ensembl.
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:0006936; P:muscle contraction; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Methylation; Motor protein; Muscle protein; Myosin; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02602"
FT   CHAIN           2..192
FT                   /note="Myosin light chain 1/3, skeletal muscle isoform"
FT                   /id="PRO_0000283742"
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..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         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   CONFLICT        110
FT                   /note="Q -> E (in Ref. 2; AAA86910)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   192 AA;  20932 MW;  EF12E3D0BC90BACC CRC64;
     MAPKKDVKKP AAAAAPAPAP APAPAPAPAP PKEEKIDLSA IKIEFSKQQQ DEFKEAFLLF
     DRTGECKITL SQVGDVLRAL GTNPTNAEVK KVLGNPSNEE MNAKKIEFEQ FLPMLQAISN
     NKDQGTYEDF VEGLRVFDKE GNGTVMGAEL RHVLATLGEK MKEEEVEALM AGQEDSNGCI
     NYEAFVKHIM SN