MLC1_YEAST
ID MLC1_YEAST Reviewed; 149 AA.
AC P53141; D6VU40;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Myosin light chain 1;
DE AltName: Full=Calmodulin-like myosin light chain MLC1;
DE AltName: Full=Myosin-2 light chain;
GN Name=MLC1; OrderedLocusNames=YGL106W; ORFNames=G3080;
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 [GENOMIC DNA].
RX PubMed=9046090;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<85::aid-yea53>3.0.co;2-e;
RA Paoluzi S., Minenkova O., Castagnoli L.;
RT "The genes encoding the transcription factor yTAFII60, the G4p1 protein and
RT a putative glucose transporter are contained in a 12.3 kb DNA fragment on
RT the left arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:85-91(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP FUNCTION, AND INTERACTION WITH MYO2.
RX PubMed=9700160; DOI=10.1083/jcb.142.3.711;
RA Stevens R.C., Davis T.N.;
RT "Mlc1p is a light chain for the unconventional myosin Myo2p in
RT Saccharomyces cerevisiae.";
RL J. Cell Biol. 142:711-722(1998).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH IQG1.
RX PubMed=10873803; DOI=10.1016/s0960-9822(00)00539-x;
RA Shannon K.B., Li R.;
RT "A myosin light chain mediates the localization of the budding yeast IQGAP-
RT like protein during contractile ring formation.";
RL Curr. Biol. 10:727-730(2000).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH IQG1 AND MYO1.
RX PubMed=11082046; DOI=10.1242/jcs.113.24.4533;
RA Boyne J.R., Yosuf H.M., Bieganowski P., Brenner C., Price C.;
RT "Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II
RT myosin to effect cytokinesis.";
RL J. Cell Sci. 113:4533-4543(2000).
RN [7]
RP FUNCTION, INTERACTION WITH MYO2 AND SEC4, AND MUTAGENESIS OF PHE-93 AND
RP PHE-142.
RX PubMed=12456647; DOI=10.1093/emboj/cdf650;
RA Wagner W., Bielli P., Wacha S., Ragnini-Wilson A.;
RT "Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the
RT vesicle motor Myo2p.";
RL EMBO J. 21:6397-6408(2002).
RN [8]
RP FUNCTION, INTERACTION WITH MYO1, AND MUTAGENESIS OF GLY-114 AND GLY-135.
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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-149 IN COMPLEX WITH MYO2.
RX PubMed=12351846; DOI=10.1107/s0907444902013951;
RA Terrak M., Otterbein L.R., Wu G., Palecanda L.A., Lu R.C., Dominguez R.;
RT "Crystallization, X-ray characterization and selenomethionine phasing of
RT Mlc1p bound to IQ motifs from myosin V.";
RL Acta Crystallogr. D 58:1882-1885(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-149 IN COMPLEX WITH MYO2.
RX PubMed=12554638; DOI=10.1093/emboj/cdg058;
RA Terrak M., Wu G., Stafford W.F., Lu R.C., Dominguez R.;
RT "Two distinct myosin light chain structures are induced by specific
RT variations within the bound IQ motifs-functional implications.";
RL EMBO J. 22:362-371(2003).
CC -!- FUNCTION: Essential light chain for the class II conventional myosin
CC MYO1. Acts also as light chain for the class V unconventional myosin
CC MYO2 and for IQG1. Involved in the assembly of the contractile
CC actomyosin ring at the bud neck during cytokinesis by recruiting IQG1
CC to the bud neck. Also required for chitin and MYO2-dependent secretory
CC vesicle deposition to the center of the bud neck for septum formation.
CC May stabilize MYO2 by binding to its IQ domains. Its major function is
CC probably not to regulate MYO1 activity, but rather to coordinate actin
CC ring formation and targeted membrane deposition during cytokinesis via
CC its interactions with MYO1, IQG1 and MYO2.
CC {ECO:0000269|PubMed:12456647, ECO:0000269|PubMed:15210731,
CC ECO:0000269|PubMed:9700160}.
CC -!- SUBUNIT: Interacts with MYO1, MYO2 and IQG1 by binding to their IQ
CC domains. Interacts with SEC4. {ECO:0000269|PubMed:10873803,
CC ECO:0000269|PubMed:11082046, ECO:0000269|PubMed:12351846,
CC ECO:0000269|PubMed:12456647, ECO:0000269|PubMed:12554638,
CC ECO:0000269|PubMed:15210731, ECO:0000269|PubMed:9700160}.
CC -!- INTERACTION:
CC P53141; Q12280: IQG1; NbExp=12; IntAct=EBI-10988, EBI-35351;
CC P53141; P53141: MLC1; NbExp=2; IntAct=EBI-10988, EBI-10988;
CC P53141; P08964: MYO1; NbExp=4; IntAct=EBI-10988, EBI-11650;
CC P53141; P19524: MYO2; NbExp=3; IntAct=EBI-10988, EBI-11659;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:10873803,
CC ECO:0000269|PubMed:11082046}. Bud tip {ECO:0000269|PubMed:10873803,
CC ECO:0000269|PubMed:11082046}. Note=Concentrates to sites of polarized
CC growth, namely to the incipient bud site in G1, to the bud tip during S
CC and G2 phases of the cell cycle and to the bud neck during cytokinesis.
CC {ECO:0000269|PubMed:11082046}.
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DR EMBL; X97644; CAA66246.1; -; Genomic_DNA.
DR EMBL; Z72628; CAA96813.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08001.1; -; Genomic_DNA.
DR PIR; S64114; S64114.
DR RefSeq; NP_011409.1; NM_001180971.1.
DR PDB; 1M45; X-ray; 1.65 A; A=2-149.
DR PDB; 1M46; X-ray; 2.10 A; A=2-149.
DR PDB; 1N2D; X-ray; 2.00 A; A/B=2-149.
DR PDB; 2FCD; NMR; -; A=2-79.
DR PDB; 2FCE; NMR; -; A=80-149.
DR PDBsum; 1M45; -.
DR PDBsum; 1M46; -.
DR PDBsum; 1N2D; -.
DR PDBsum; 2FCD; -.
DR PDBsum; 2FCE; -.
DR AlphaFoldDB; P53141; -.
DR BMRB; P53141; -.
DR SMR; P53141; -.
DR BioGRID; 33144; 107.
DR ComplexPortal; CPX-1426; Myosin class II complex.
DR ComplexPortal; CPX-1501; Myosin class V complex, MYO4 variant.
DR ComplexPortal; CPX-2225; Myosin class V complex, MYO2 variant.
DR ComplexPortal; CPX-3503; MIH complex.
DR DIP; DIP-5576N; -.
DR IntAct; P53141; 19.
DR MINT; P53141; -.
DR STRING; 4932.YGL106W; -.
DR iPTMnet; P53141; -.
DR MaxQB; P53141; -.
DR PaxDb; P53141; -.
DR PRIDE; P53141; -.
DR TopDownProteomics; P53141; -.
DR EnsemblFungi; YGL106W_mRNA; YGL106W; YGL106W.
DR GeneID; 852772; -.
DR KEGG; sce:YGL106W; -.
DR SGD; S000003074; MLC1.
DR VEuPathDB; FungiDB:YGL106W; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT01030000234570; -.
DR HOGENOM; CLU_061288_13_1_1; -.
DR InParanoid; P53141; -.
DR OMA; DIRYMLT; -.
DR BioCyc; YEAST:G3O-30605-MON; -.
DR Reactome; R-SCE-5627123; RHO GTPases activate PAKs.
DR EvolutionaryTrace; P53141; -.
DR PRO; PR:P53141; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53141; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0120155; C:MIH complex; IDA:SGD.
DR GO; GO:0016460; C:myosin II complex; IPI:SGD.
DR GO; GO:0031475; C:myosin V complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0031982; C:vesicle; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0032038; F:myosin II heavy chain binding; IPI:SGD.
DR GO; GO:0031489; F:myosin V binding; IDA:SGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:1903476; P:protein localization to cell division site involved in mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:0031991; P:regulation of actomyosin contractile ring contraction; IC:ComplexPortal.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; IC:ComplexPortal.
DR GO; GO:0032465; P:regulation of cytokinesis; IC:ComplexPortal.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IC:ComplexPortal.
DR GO; GO:0006903; P:vesicle targeting; IMP:SGD.
DR GO; GO:0030050; P:vesicle transport along actin filament; IC:ComplexPortal.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell cycle; Cell division; Isopeptide bond;
KW Metal-binding; Motor protein; Myosin; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..149
FT /note="Myosin light chain 1"
FT /id="PRO_0000198765"
FT DOMAIN 2..37
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 93
FT /note="F->A: In MLC1-1; causes a defect in septum
FT formation."
FT /evidence="ECO:0000269|PubMed:12456647"
FT MUTAGEN 114
FT /note="G->D: In MLC1-11; abolishes interaction with MYO2
FT and IQG1 and reduces interaction with MYO1. Leads to
FT mislocalization of IQG1 and a severe defect in
FT cytokinesis."
FT /evidence="ECO:0000269|PubMed:15210731"
FT MUTAGEN 135
FT /note="G->E: In MLC1-93; reduces interaction with MYO1, but
FT does not cause any defect in cytokinesis."
FT /evidence="ECO:0000269|PubMed:15210731"
FT MUTAGEN 142
FT /note="F->A: In MLC1-5; causes a defect in septum
FT formation."
FT /evidence="ECO:0000269|PubMed:12456647"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1M45"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:1N2D"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:1M45"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:1M45"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1N2D"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:1M45"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1M45"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:1M45"
SQ SEQUENCE 149 AA; 16444 MW; D7508123C101E4A6 CRC64;
MSATRANKDI FTLFDKKGQG AIAKDSLGDY LRAIGYNPTN QLVQDIINAD SSLRDASSLT
LDQITGLIEV NEKELDATTK AKTEDFVKAF QVFDKESTGK VSVGDLRYML TGLGEKLTDA
EVDELLKGVE VDSNGEIDYK KFIEDVLRQ
