SQH_DROME
ID SQH_DROME Reviewed; 174 AA.
AC P40423; Q540V2; Q9W428;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Myosin regulatory light chain sqh;
DE AltName: Full=Myosin regulatory light chain, nonmuscle;
DE Short=MRLC-C;
DE AltName: Full=Protein spaghetti-squash;
GN Name=sqh; ORFNames=CG3595;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1905980; DOI=10.1016/0092-8674(91)90013-o;
RA Karess R.E., Chang X.J., Edwards K.A., Kulkarni S., Aguilera I.,
RA Kiehart D.P.;
RT "The regulatory light chain of nonmuscle myosin is encoded by spaghetti-
RT squash, a gene required for cytokinesis in Drosophila.";
RL Cell 65:1177-1189(1991).
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; 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, AND
RP IDENTIFICATION BY 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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for cytokinesis, could regulate contractile ring
CC function. {ECO:0000269|PubMed:1905980}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- PTM: Phosphorylation plays a central role in myosin regulation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mitotic defects including failure in cytokinesis.
CC {ECO:0000269|PubMed:1905980}.
CC -!- MISCELLANEOUS: This chain binds calcium. {ECO:0000250}.
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DR EMBL; M67494; AAC13367.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46132.1; -; Genomic_DNA.
DR EMBL; AY122159; AAM52671.1; -; mRNA.
DR PIR; A39932; A39932.
DR RefSeq; NP_001284928.1; NM_001297999.1.
DR RefSeq; NP_001284929.1; NM_001298000.1.
DR RefSeq; NP_001284930.1; NM_001298001.1.
DR RefSeq; NP_001284931.1; NM_001298002.1.
DR RefSeq; NP_511057.1; NM_078502.3.
DR AlphaFoldDB; P40423; -.
DR SMR; P40423; -.
DR BioGRID; 58046; 50.
DR IntAct; P40423; 17.
DR STRING; 7227.FBpp0070842; -.
DR iPTMnet; P40423; -.
DR PaxDb; P40423; -.
DR PRIDE; P40423; -.
DR DNASU; 31554; -.
DR EnsemblMetazoa; FBtr0070877; FBpp0070842; FBgn0003514.
DR EnsemblMetazoa; FBtr0339502; FBpp0308586; FBgn0003514.
DR EnsemblMetazoa; FBtr0339503; FBpp0308587; FBgn0003514.
DR EnsemblMetazoa; FBtr0339504; FBpp0308588; FBgn0003514.
DR EnsemblMetazoa; FBtr0345294; FBpp0311461; FBgn0003514.
DR GeneID; 31554; -.
DR KEGG; dme:Dmel_CG3595; -.
DR CTD; 31554; -.
DR FlyBase; FBgn0003514; sqh.
DR VEuPathDB; VectorBase:FBgn0003514; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000155458; -.
DR HOGENOM; CLU_061288_9_3_1; -.
DR InParanoid; P40423; -.
DR OMA; FECFDEN; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P40423; -.
DR Reactome; R-DME-350416; Regulation of non-muscle Myosin II.
DR Reactome; R-DME-350480; Activation of non-muscle Myosin II.
DR Reactome; R-DME-3928664; Ephrin signaling.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR SignaLink; P40423; -.
DR BioGRID-ORCS; 31554; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31554; -.
DR PRO; PR:P40423; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003514; Expressed in saliva-secreting gland and 24 other tissues.
DR ExpressionAtlas; P40423; baseline and differential.
DR Genevisible; P40423; DM.
DR GO; GO:1903144; C:actomyosin contractile ring actin filament; IDA:FlyBase.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0106037; C:apicomedial cortex; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0110071; C:cellularization cleavage furrow invagination front; IDA:FlyBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0035183; C:female germline ring canal inner rim; IDA:FlyBase.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0016460; C:myosin II complex; IPI:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0051233; C:spindle midzone; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; IPI:FlyBase.
DR GO; GO:0030048; P:actin filament-based movement; IC:FlyBase.
DR GO; GO:0003384; P:apical constriction involved in gastrulation; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0060289; P:compartment boundary maintenance; IMP:FlyBase.
DR GO; GO:0019749; P:cytoskeleton-dependent cytoplasmic transport, nurse cell to oocyte; IMP:FlyBase.
DR GO; GO:0060288; P:formation of a compartment boundary; IDA:FlyBase.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IGI:FlyBase.
DR GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:FlyBase.
DR GO; GO:0031036; P:myosin II filament assembly; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0035191; P:nuclear axial expansion; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IGI:FlyBase.
DR GO; GO:0009791; P:post-embryonic development; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR GO; GO:0110069; P:syncytial embryo cellularization; IEP:FlyBase.
DR GO; GO:0035148; P:tube formation; IMP:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP: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 SMART; SM00054; EFh; 2.
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; Metal-binding; Motor protein; Myosin; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..174
FT /note="Myosin regulatory light chain sqh"
FT /id="PRO_0000198747"
FT DOMAIN 31..66
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 100..135
FT /note="EF-hand 2"
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 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
SQ SEQUENCE 174 AA; 19954 MW; 2D95C9F0460B8766 CRC64;
MSSRKTAGRR ATTKKRAQRA TSNVFAMFDQ AQIAEFKEAF NMIDQNRDGF VEKEDLHDML
ASLGKNPTDD YLDGMMNEAP GPINFTMFLT LFGERLQGTD PEDVIKNAFG CFDEENMGVL
PEDRLRELLT TMGDRFTDED VDEMYREAPI KNGLFDYLEF TRILKHGAKD KDEQ
