MLC2_YEAST
ID MLC2_YEAST Reviewed; 163 AA.
AC Q06580; D6W4I8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Myosin light chain 2;
DE AltName: Full=Calmodulin-like myosin light chain MLC2;
DE AltName: Full=MYO1 light chain 2;
DE AltName: Full=Myosin-1 light chain;
GN Name=MLC2; OrderedLocusNames=YPR188C; ORFNames=P9677.10;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYO1.
RX PubMed=15210731; DOI=10.1083/jcb.200401040;
RA Luo J., Vallen E.A., Dravis C., Tcheperegine S.E., Drees B., Bi E.;
RT "Identification and functional analysis of the essential and regulatory
RT light chains of the only type II myosin Myo1p in Saccharomyces
RT cerevisiae.";
RL J. Cell Biol. 165:843-855(2004).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Regulatory light chain for the class II conventional myosin
CC MYO1. May play a role in the disassembly of the MYO1 ring at the bud
CC neck at the end of its contraction during cytokinesis.
CC {ECO:0000269|PubMed:15210731}.
CC -!- SUBUNIT: Interacts with the IQ domain of MYO1.
CC {ECO:0000269|PubMed:15210731}.
CC -!- INTERACTION:
CC Q06580; P08964: MYO1; NbExp=3; IntAct=EBI-10999, EBI-11650;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15210731}. Note=Forms a ring at the bud neck in a
CC MYO1-dependent manner.
CC -!- MISCELLANEOUS: Present with 1127 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: This chain binds calcium. {ECO:0000305}.
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DR EMBL; U25841; AAB64617.1; -; Genomic_DNA.
DR EMBL; AY558057; AAS56383.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11604.1; -; Genomic_DNA.
DR PIR; S58818; S58818.
DR RefSeq; NP_015514.1; NM_001184285.1.
DR AlphaFoldDB; Q06580; -.
DR SMR; Q06580; -.
DR BioGRID; 36360; 43.
DR ComplexPortal; CPX-1426; Myosin class II complex.
DR DIP; DIP-2767N; -.
DR IntAct; Q06580; 8.
DR MINT; Q06580; -.
DR STRING; 4932.YPR188C; -.
DR iPTMnet; Q06580; -.
DR MaxQB; Q06580; -.
DR PaxDb; Q06580; -.
DR PRIDE; Q06580; -.
DR EnsemblFungi; YPR188C_mRNA; YPR188C; YPR188C.
DR GeneID; 856318; -.
DR KEGG; sce:YPR188C; -.
DR SGD; S000006392; MLC2.
DR VEuPathDB; FungiDB:YPR188C; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_9_2_1; -.
DR InParanoid; Q06580; -.
DR OMA; DAFQMID; -.
DR BioCyc; YEAST:G3O-34311-MON; -.
DR Reactome; R-SCE-5627123; RHO GTPases activate PAKs.
DR PRO; PR:Q06580; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06580; protein.
DR GO; GO:0005935; C:cellular bud neck; IC:ComplexPortal.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0016460; C:myosin II complex; IPI:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0140659; F:cytoskeletal motor regulator activity; IBA:GO_Central.
DR GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
DR GO; GO:0032038; F:myosin II heavy chain binding; IPI:SGD.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:1990274; P:mitotic actomyosin contractile ring disassembly; IMP:SGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IC:ComplexPortal.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Cell cycle; Cell division; Metal-binding; Motor protein; Myosin;
KW Reference proteome; Repeat.
FT CHAIN 1..163
FT /note="Myosin light chain 2"
FT /id="PRO_0000198766"
FT DOMAIN 15..50
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 92..127
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 163 AA; 18521 MW; 6BAE6EA0ADF66B9B CRC64;
MDHSESLTFN QLTQDYINKL KDAFQMLDED EDGLISRGDL TKIYATLGKT LTDEEWSKMV
PDNDTSTAEV GEEGVSFPIF LSIMGKNLSQ FPEREELEES LKAIGRGHDL NVPLNEVIDS
LKEAGFENPE EEFAKLFKLF TTNQQATEER TFRGKLFLDS ITD
