MLRH_CAEEL
ID MLRH_CAEEL Reviewed; 172 AA.
AC Q09510;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Myosin regulatory light chain {ECO:0000303|PubMed:10427096};
DE AltName: Full=Non-muscle myosin regulatory light chain {ECO:0000303|PubMed:10427096};
DE Short=nmRLC {ECO:0000303|PubMed:10427096};
GN Name=mlc-4 {ECO:0000312|WormBase:C56G7.1};
GN ORFNames=C56G7.1 {ECO:0000312|WormBase:C56G7.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10427096; DOI=10.1083/jcb.146.2.439;
RA Shelton C.A., Carter J.C., Ellis G.C., Bowerman B.;
RT "The nonmuscle myosin regulatory light chain gene mlc-4 is required for
RT cytokinesis, anterior-posterior polarity, and body morphology during
RT Caenorhabditis elegans embryogenesis.";
RL J. Cell Biol. 146:439-451(1999).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-17 AND SER-18, AND
RP MUTAGENESIS OF THR-17 AND SER-18.
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: Regulates myosin II activity and organization during embryo
CC elongation. May be involved in the organization of mlc-5 into bundles
CC (PubMed:19675126). Required maternally for cytokinesis during meiosis
CC and mitosis in the early embryo and for the establishment of embryonic
CC anterior-posterior polarity (PubMed:10427096).
CC {ECO:0000269|PubMed:10427096, 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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19675126}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19675126}. Note=Forms a
CC filamentous structure which may co-localize with actin.
CC {ECO:0000269|PubMed:19675126}.
CC -!- TISSUE SPECIFICITY: Expressed in the spermathecal and uterine walls.
CC Weak expression in gonadal sheath and intestinal muscle. Not detected
CC in vulval, pharyngeal or body wall muscles.
CC {ECO:0000269|PubMed:10427096}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the bean stage in the lateral
CC hypodermal seam cells and then throughout embryogenesis and into larval
CC stages. {ECO:0000269|PubMed:10427096}.
CC -!- PTM: May be phosphorylated by let-502 or/and pak-1 and dephosphorylated
CC by mel-11 to regulate its activation and myosin II-mediated
CC contraction. {ECO:0000305|PubMed:19675126}.
CC -!- DISRUPTION PHENOTYPE: Arrest at the 2-fold embryonic stage which is
CC associated with a defect in embryo elongation and failure of seam cells
CC to elongate to a narrow morphology. No abnormalities in body wall or
CC pharyngeal muscles and in the number of hypodermal cells.
CC {ECO:0000269|PubMed:10427096}.
CC -!- MISCELLANEOUS: This chain binds calcium. {ECO:0000250}.
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; Z46793; CAA86772.1; -; Genomic_DNA.
DR EMBL; Z34801; CAA86772.1; JOINED; Genomic_DNA.
DR PIR; T20273; T20273.
DR RefSeq; NP_497700.1; NM_065299.4.
DR AlphaFoldDB; Q09510; -.
DR SMR; Q09510; -.
DR BioGRID; 40682; 8.
DR DIP; DIP-25307N; -.
DR IntAct; Q09510; 1.
DR STRING; 6239.C56G7.1; -.
DR iPTMnet; Q09510; -.
DR EPD; Q09510; -.
DR PaxDb; Q09510; -.
DR PeptideAtlas; Q09510; -.
DR EnsemblMetazoa; C56G7.1.1; C56G7.1.1; WBGene00003372.
DR GeneID; 175440; -.
DR KEGG; cel:CELE_C56G7.1; -.
DR UCSC; C56G7.1.1; c. elegans.
DR CTD; 175440; -.
DR WormBase; C56G7.1; CE01531; WBGene00003372; mlc-4.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000155458; -.
DR HOGENOM; CLU_061288_9_3_1; -.
DR InParanoid; Q09510; -.
DR OMA; FECFDEN; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; Q09510; -.
DR Reactome; R-CEL-3928664; Ephrin signaling.
DR Reactome; R-CEL-5627123; RHO GTPases activate PAKs.
DR SignaLink; Q09510; -.
DR PRO; PR:Q09510; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003372; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0031941; C:filamentous actin; IDA:WormBase.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR GO; GO:0007110; P:meiosis I cytokinesis; IMP:WormBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Cytoskeleton; Metal-binding; Motor protein; Myosin;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..172
FT /note="Myosin regulatory light chain"
FT /evidence="ECO:0000305|PubMed:10427096"
FT /id="PRO_0000198762"
FT DOMAIN 27..62
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 98..133
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 134..168
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19675126"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19675126"
FT MUTAGEN 17..18
FT /note="TS->AA: Impaired embryo elongation."
FT /evidence="ECO:0000269|PubMed:19675126"
FT MUTAGEN 17..18
FT /note="TS->DD: Phosphomimetic mutant which shows no defect
FT in embryo elongation."
FT /evidence="ECO:0000269|PubMed:19675126"
FT MUTAGEN 17
FT /note="T->A: Partial defect in embryo elongation."
FT /evidence="ECO:0000269|PubMed:19675126"
FT MUTAGEN 18
FT /note="S->A: Partial defect in embryo elongation."
FT /evidence="ECO:0000269|PubMed:19675126"
SQ SEQUENCE 172 AA; 19940 MW; CEE733AD3D57ABFD CRC64;
MASRKTVNRR QRPQRATSNV FAMFDQAQIQ EFKEAFNMID QNRDGFIDQE DLKDMFASLG
KEVTEQFIDS MINEAPGAQP INFTMFLTLF GEKLTGTDPE EVIRNAFQCF DEDNSGKLNE
EHLRELLTTM GERYSEEQVD ELFRDAPIKG GQFDYVEFTR MLKHGTKDKD EA
