MLC1_DROME
ID MLC1_DROME Reviewed; 155 AA.
AC P06742; P06743; P92155; P92156; P92157; P92183; P92187; P92196; Q24380;
AC Q24381; Q24382; Q24383; Q27304; Q27315; Q27381; Q27414; Q94988; Q9VB12;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Myosin light chain alkali;
GN Name=Mlc1; Synonyms=MLC-ALK; ORFNames=CG5596;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo, Larva, and Pupae;
RX PubMed=2982157; DOI=10.1073/pnas.82.2.449;
RA Falkenthal S., Parker V.P., Davidson N.;
RT "Developmental variations in the splicing pattern of transcripts from the
RT Drosophila gene encoding myosin alkali light chain result in different
RT carboxyl-terminal amino acid sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:449-453(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LARVAL-ADULT), DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Embryo, Flight muscle, and Pupae;
RX PubMed=6328279; DOI=10.1128/mcb.4.5.956-965.1984;
RA Falkenthal S., Parker V.P., Mattox W.W., Davidson N.;
RT "Drosophila melanogaster has only one myosin alkali light-chain gene which
RT encodes a protein with considerable amino acid sequence homology to chicken
RT myosin alkali light chains.";
RL Mol. Cell. Biol. 4:956-965(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LARVAL-ADULT).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-155, AND ALTERNATIVE SPLICING.
RC STRAIN=M171, M174, M179, M180, M192, M219, M223, M234, M237, M240, M241N,
RC M242, M245, M247, M249, and M86;
RX PubMed=7535717; DOI=10.1093/genetics/139.1.299;
RA Leicht B.G., Muse S.V., Hanczyc M., Clark A.G.;
RT "Constraints on intron evolution in the gene encoding the myosin alkali
RT light chain in Drosophila.";
RL Genetics 139:299-308(1995).
RN [7]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Abdomen, Flight muscle, Head, Muscle, and Pupae;
RX PubMed=3106119; DOI=10.1016/0012-1606(87)90158-8;
RA Falkenthal S., Graham M., Wilkinson J.;
RT "The indirect flight muscle of Drosophila accumulates a unique myosin
RT alkali light chain isoform.";
RL Dev. Biol. 121:263-272(1987).
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Larval-adult; Synonyms=Larval-non-IFM;
CC IsoId=P06742-1; Sequence=Displayed;
CC Name=Indirect flight muscle; Synonyms=Pupa, Adult flight muscle;
CC IsoId=P06742-2; Sequence=VSP_003367;
CC -!- TISSUE SPECIFICITY: Indirect flight muscle isoform is found only in the
CC indirect flight muscles. The larval and adult isoform is present in the
CC larval and adult musculature. {ECO:0000269|PubMed:3106119,
CC ECO:0000269|PubMed:6328279}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late embryogenesis, larval
CC instars, late stages of pupariation and adult.
CC {ECO:0000269|PubMed:2982157, ECO:0000269|PubMed:6328279}.
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DR EMBL; M10125; AAA28711.1; -; Genomic_DNA.
DR EMBL; M10125; AAA28712.1; -; Genomic_DNA.
DR EMBL; K01567; AAA28710.1; -; mRNA.
DR EMBL; AE014297; AAF56733.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN14121.1; -; Genomic_DNA.
DR EMBL; AY070972; AAL48594.1; -; mRNA.
DR EMBL; L37312; AAA53441.1; -; Genomic_DNA.
DR EMBL; L37312; AAA53442.1; -; Genomic_DNA.
DR EMBL; L37313; AAA53443.1; -; Genomic_DNA.
DR EMBL; L37313; AAA53444.1; -; Genomic_DNA.
DR EMBL; L37314; AAA53445.1; -; Genomic_DNA.
DR EMBL; L37314; AAA53446.1; -; Genomic_DNA.
DR EMBL; L37315; AAA53447.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L37315; AAA53448.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L37316; AAA56798.1; -; Genomic_DNA.
DR EMBL; L37316; AAA56799.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L37317; AAA53449.1; -; Genomic_DNA.
DR EMBL; L37317; AAA53450.1; -; Genomic_DNA.
DR EMBL; L37318; AAA53451.1; -; Genomic_DNA.
DR EMBL; L37318; AAA53452.1; -; Genomic_DNA.
DR EMBL; L37319; AAA53453.1; -; Genomic_DNA.
DR EMBL; L37319; AAA53454.1; -; Genomic_DNA.
DR EMBL; L37320; AAA53455.1; -; Genomic_DNA.
DR EMBL; L37320; AAA53456.1; -; Genomic_DNA.
DR EMBL; L37321; AAA53457.1; -; Genomic_DNA.
DR EMBL; L37321; AAA53458.1; -; Genomic_DNA.
DR EMBL; L37322; AAA53459.1; -; Genomic_DNA.
DR EMBL; L37322; AAA53460.1; -; Genomic_DNA.
DR EMBL; L37323; AAA53461.1; -; Genomic_DNA.
DR EMBL; L37323; AAA53462.1; -; Genomic_DNA.
DR EMBL; L37324; AAA53463.1; -; Genomic_DNA.
DR EMBL; L37324; AAA53464.1; -; Genomic_DNA.
DR EMBL; L37325; AAA53465.1; -; Genomic_DNA.
DR EMBL; L37325; AAA53466.1; -; Genomic_DNA.
DR EMBL; L37326; AAA53467.1; -; Genomic_DNA.
DR EMBL; L37326; AAA53468.1; -; Genomic_DNA.
DR EMBL; L37327; AAA53469.1; -; Genomic_DNA.
DR EMBL; L37327; AAA53470.1; -; Genomic_DNA.
DR RefSeq; NP_001287569.1; NM_001300640.1. [P06742-1]
DR RefSeq; NP_476639.1; NM_057291.4. [P06742-2]
DR RefSeq; NP_476640.1; NM_057292.4. [P06742-1]
DR PDB; 5W1A; X-ray; 2.23 A; B/D=1-151.
DR PDBsum; 5W1A; -.
DR AlphaFoldDB; P06742; -.
DR SMR; P06742; -.
DR BioGRID; 68205; 47.
DR DIP; DIP-23903N; -.
DR IntAct; P06742; 20.
DR STRING; 7227.FBpp0084565; -.
DR PaxDb; P06742; -.
DR DNASU; 43323; -.
DR EnsemblMetazoa; FBtr0085195; FBpp0084565; FBgn0002772. [P06742-2]
DR EnsemblMetazoa; FBtr0085196; FBpp0084566; FBgn0002772. [P06742-1]
DR EnsemblMetazoa; FBtr0344131; FBpp0310544; FBgn0002772. [P06742-1]
DR GeneID; 43323; -.
DR KEGG; dme:Dmel_CG5596; -.
DR CTD; 23209; -.
DR FlyBase; FBgn0002772; Mlc1.
DR VEuPathDB; VectorBase:FBgn0002772; -.
DR eggNOG; KOG0030; Eukaryota.
DR GeneTree; ENSGT01030000234570; -.
DR HOGENOM; CLU_061288_13_3_1; -.
DR InParanoid; P06742; -.
DR OMA; PIFSQCK; -.
DR PhylomeDB; P06742; -.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR SignaLink; P06742; -.
DR BioGRID-ORCS; 43323; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Mlc1; fly.
DR GenomeRNAi; 43323; -.
DR PRO; PR:P06742; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002772; Expressed in oviduct (Drosophila) and 29 other tissues.
DR ExpressionAtlas; P06742; baseline and differential.
DR Genevisible; P06742; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005859; C:muscle myosin complex; IDA:UniProtKB.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; NAS:UniProtKB.
DR GO; GO:0032036; F:myosin heavy chain binding; NAS:UniProtKB.
DR GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; NAS:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; NAS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR029655; Mlc1.
DR PANTHER; PTHR23048:SF33; PTHR23048:SF33; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Motor protein; Muscle protein; Myosin;
KW Reference proteome; Repeat.
FT CHAIN 1..155
FT /note="Myosin light chain alkali"
FT /id="PRO_0000198709"
FT DOMAIN 7..41
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 80..115
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 142..155
FT /note="QFVQRLMSDPVVFD -> PFLARMCDRPDQLK (in isoform
FT Indirect flight muscle)"
FT /evidence="ECO:0000305"
FT /id="VSP_003367"
FT CONFLICT 2
FT /note="A -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="L -> M (in Ref. 6; AAA53454/AAA53458/AAA53460/
FT AAA53466/AAA53468)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> H (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:5W1A"
SQ SEQUENCE 155 AA; 17524 MW; 65C92CD17995ECF5 CRC64;
MADVPKREVE NVEFVFEVMG SPGEGIDAVD LGDALRALNL NPTLALIEKL GGTKKRNEKK
IKLDEFLPIY SQVKKEKEQG CYEDFIECLK LYDKEENGTM LLAELQHALL ALGESLDDEQ
VETLFADCMD PEDDEGFIPY SQFVQRLMSD PVVFD
