ID   MLC5_CAEEL              Reviewed;         142 AA.
AC   Q9XVI9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Myosin-2 essential light chain {ECO:0000303|PubMed:19675126};
GN   Name=mlc-5 {ECO:0000312|WormBase:T12D8.6};
GN   ORFNames=T12D8.6 {ECO:0000312|WormBase:T12D8.6};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19675126; DOI=10.1242/dev.039412;
RA   Gally C., Wissler F., Zahreddine H., Quintin S., Landmann F., Labouesse M.;
RT   "Myosin II regulation during C. elegans embryonic elongation: LET-502/ROCK,
RT   MRCK-1 and PAK-1, three kinases with different roles.";
RL   Development 136:3109-3119(2009).
CC   -!- FUNCTION: Required for cytokinesis and embryo elongation. May regulate
CC       myosin II complex formation and/or the association of myosin with
CC       actin. May be involved in the organization of mlc-4 and nmy-2 into
CC       bundles. {ECO:0000269|PubMed:19675126}.
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains (two
CC       regulatory light chains and two essential light chains).
CC       {ECO:0000305|PubMed:19675126}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19675126}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19675126}. Note=Forms a
CC       filamentous structure during 2-fold embryonic stage which may co-
CC       localize with actin and whose formation may be regulated by mlc-4.
CC       {ECO:0000269|PubMed:19675126}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis in seam cells as
CC       well as in the dorsal and ventral hypodermal cells where it co-
CC       localizes with actin bundles. {ECO:0000269|PubMed:19675126}.
CC   -!- DISRUPTION PHENOTYPE: Arrest at the 1-cell stage embryo due to a
CC       cytokinesis defect characterized by a failure to form a contractile
CC       ring. {ECO:0000269|PubMed:19675126}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z81120; CAB03346.1; -; Genomic_DNA.
DR   PIR; T24862; T24862.
DR   RefSeq; NP_499813.1; NM_067412.6.
DR   AlphaFoldDB; Q9XVI9; -.
DR   SMR; Q9XVI9; -.
DR   IntAct; Q9XVI9; 1.
DR   STRING; 6239.T12D8.6.2; -.
DR   EPD; Q9XVI9; -.
DR   PaxDb; Q9XVI9; -.
DR   PeptideAtlas; Q9XVI9; -.
DR   EnsemblMetazoa; T12D8.6.1; T12D8.6.1; WBGene00011734.
DR   GeneID; 176796; -.
DR   KEGG; cel:CELE_T12D8.6; -.
DR   UCSC; T12D8.6.1; c. elegans.
DR   CTD; 176796; -.
DR   WormBase; T12D8.6; CE16403; WBGene00011734; mlc-5.
DR   eggNOG; KOG0030; Eukaryota.
DR   GeneTree; ENSGT01030000234570; -.
DR   HOGENOM; CLU_061288_2_0_1; -.
DR   InParanoid; Q9XVI9; -.
DR   OMA; YDRTPKC; -.
DR   OrthoDB; 1470794at2759; -.
DR   PhylomeDB; Q9XVI9; -.
DR   Reactome; R-CEL-5627123; RHO GTPases activate PAKs.
DR   PRO; PR:Q9XVI9; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00011734; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
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; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Motor protein; Myosin;
KW   Reference proteome; Repeat.
FT   CHAIN           1..142
FT                   /note="Myosin-2 essential light chain"
FT                   /id="PRO_0000432386"
FT   DOMAIN          2..37
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          75..110
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   142 AA;  15971 MW;  F3C09D220C797F12 CRC64;
     MDDLADCREV FAYFDSKGDE RISVQQVGDV LRALGQNPTE AEIHKCVGSF DREARLSFED
     FVPIFQSVSK NREKHTVEEF VEGLSHFDKE GNGMINVAEL RHLLTTLGER LSDEDVDQLL
     SGHNDSHGNV NISDFVRAVM NS