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MLC2_DROME
ID   MLC2_DROME              Reviewed;         147 AA.
AC   P54357; C1C594; Q9W4A8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Myosin-2 essential light chain;
DE   AltName: Full=Myosin II essential light chain;
DE   AltName: Full=Non-muscle myosin essential light chain;
GN   Name=Mlc-c; ORFNames=CG3201;
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 [MRNA].
RX   PubMed=8567936; DOI=10.1007/bf00126433;
RA   Edwards K.A., Chang X., Kiehart D.P.;
RT   "Essential light chain of Drosophila nonmuscle myosin II.";
RL   J. Muscle Res. Cell Motil. 16:491-498(1995).
RN   [2]
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   [3]
RP   GENOME REANNOTATION.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC       {ECO:0000250}.
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DR   EMBL; U25057; AAA84897.1; -; mRNA.
DR   EMBL; AE014298; AAF46048.1; -; Genomic_DNA.
DR   EMBL; BT082023; ACO72860.1; -; mRNA.
DR   RefSeq; NP_511049.1; NM_078494.4.
DR   AlphaFoldDB; P54357; -.
DR   SMR; P54357; -.
DR   BioGRID; 57980; 20.
DR   DIP; DIP-19766N; -.
DR   IntAct; P54357; 7.
DR   STRING; 7227.FBpp0300803; -.
DR   iPTMnet; P54357; -.
DR   PaxDb; P54357; -.
DR   PRIDE; P54357; -.
DR   DNASU; 31474; -.
DR   EnsemblMetazoa; FBtr0070783; FBpp0070749; FBgn0004687.
DR   GeneID; 31474; -.
DR   KEGG; dme:Dmel_CG3201; -.
DR   CTD; 31474; -.
DR   FlyBase; FBgn0004687; Mlc-c.
DR   VEuPathDB; VectorBase:FBgn0004687; -.
DR   eggNOG; KOG0030; Eukaryota.
DR   GeneTree; ENSGT01030000234570; -.
DR   HOGENOM; CLU_061288_13_0_1; -.
DR   InParanoid; P54357; -.
DR   OMA; DIRYMLT; -.
DR   OrthoDB; 1470794at2759; -.
DR   PhylomeDB; P54357; -.
DR   Reactome; R-DME-350480; Activation of non-muscle Myosin II.
DR   Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR   SignaLink; P54357; -.
DR   BioGRID-ORCS; 31474; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 31474; -.
DR   PRO; PR:P54357; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0004687; Expressed in wing disc and 25 other tissues.
DR   ExpressionAtlas; P54357; baseline and differential.
DR   Genevisible; P54357; DM.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016460; C:myosin II complex; IPI:FlyBase.
DR   GO; GO:0031475; C:myosin V complex; IPI:FlyBase.
DR   GO; GO:0031476; C:myosin VI complex; IPI:FlyBase.
DR   GO; GO:0031477; C:myosin VII complex; IPI:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0017022; F:myosin binding; IPI:FlyBase.
DR   GO; GO:0032036; F:myosin heavy chain binding; IPI:FlyBase.
DR   GO; GO:0030048; P:actin filament-based movement; IDA:FlyBase.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13405; EF-hand_6; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
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; Metal-binding; Motor protein; Myosin; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..147
FT                   /note="Myosin-2 essential light chain"
FT                   /id="PRO_0000198717"
FT   DOMAIN          7..42
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   DOMAIN          115..147
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         97
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         99
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
SQ   SEQUENCE   147 AA;  16613 MW;  A37FA3C9DE942B90 CRC64;
     MAAYTEDQLA EFQEAFNLFD NRGDGKIQLS QVGECLRALG QNPTESDVKK CTHQLKPDER
     ISFEVFLPIY QAISKARSGD TADDFIEGLR HFDKDASGYI SSAELRHLLT TLGEKLTDEE
     VEQLLANMED QQGNINYEEF VRMVMSG
 
 
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