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P40423 (SQH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin regulatory light chain sqh
Alternative name(s):
Myosin regulatory light chain, nonmuscle
Short name=MRLC-C
Protein spaghetti-squash
Gene names
Name:sqh
ORF Names:CG3595
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length174 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for cytokinesis, could regulate contractile ring function. Ref.1

Subunit structure

Myosin is a hexamer of 2 heavy chains and 4 light chains.

Post-translational modification

Phosphorylation plays a central role in myosin regulation By similarity.

Disruption phenotype

Mitotic defects including failure in cytokinesis. Ref.1

Miscellaneous

This chain binds calcium By similarity.

Sequence similarities

Contains 2 EF-hand domains.

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
Metal-binding
   Molecular functionMotor protein
Myosin
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament-based movement

Inferred by curator PubMed 16917818. Source: FlyBase

border follicle cell migration

Inferred from mutant phenotype PubMed 12198500. Source: FlyBase

cell elongation involved in imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 19366729. Source: FlyBase

cellularization

Non-traceable author statement PubMed 11258476. Source: FlyBase

cytoskeleton-dependent cytoplasmic transport, nurse cell to oocyte

Inferred from mutant phenotype PubMed 19005218. Source: FlyBase

establishment of planar polarity

Non-traceable author statement PubMed 12414186. Source: FlyBase

formation of a compartment boundary

Inferred from direct assay PubMed 19966783. Source: FlyBase

imaginal disc-derived wing hair organization

Inferred from genetic interaction PubMed 11301004. Source: FlyBase

mitotic cytokinesis

Inferred from mutant phenotype PubMed 12134082PubMed 15380073. Source: FlyBase

neurogenesis

Inferred from mutant phenotype PubMed 21549331. Source: FlyBase

nuclear axial expansion

Inferred from mutant phenotype PubMed 14657248. Source: FlyBase

ovarian follicle cell development

Traceable author statement PubMed 10822261. Source: FlyBase

ovarian nurse cell to oocyte transport

Traceable author statement PubMed 11139280. Source: FlyBase

regulation of actin cytoskeleton organization

Inferred from mutant phenotype PubMed 18207738. Source: FlyBase

regulation of tube length, open tracheal system

Inferred from mutant phenotype PubMed 19956736. Source: FlyBase

spiracle morphogenesis, open tracheal system

Inferred from mutant phenotype PubMed 17021037. Source: FlyBase

wound healing

Inferred from mutant phenotype PubMed 21518790. Source: FlyBase

   Cellular_componentadherens junction

Inferred from direct assay PubMed 20920606. Source: FlyBase

apical plasma membrane

Inferred from direct assay PubMed 20920606. Source: FlyBase

cell cortex

Inferred from direct assay PubMed 12105185PubMed 23707736. Source: FlyBase

cleavage furrow

Inferred from direct assay PubMed 16174742PubMed 20920606. Source: FlyBase

cytoplasm

Inferred from direct assay PubMed 16174742PubMed 20920606. Source: FlyBase

female germline ring canal inner rim

Inferred from direct assay PubMed 19005218. Source: FlyBase

midbody

Inferred from direct assay PubMed 16174742. Source: FlyBase

myosin II complex

Inferred from physical interaction PubMed 16917818. Source: FlyBase

plasma membrane

Inferred from direct assay PubMed 21169990. Source: FlyBase

spindle midzone

Inferred from direct assay PubMed 16174742. Source: FlyBase

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

myosin heavy chain binding

Inferred from physical interaction PubMed 16917818. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 174174Myosin regulatory light chain sqh
PRO_0000198747

Regions

Domain31 – 6636EF-hand 1
Domain100 – 13536EF-hand 2
Calcium binding44 – 5512 Potential

Amino acid modifications

Modified residue211Phosphothreonine Ref.5 Ref.6
Modified residue221Phosphoserine Ref.5 Ref.6

Sequences

Sequence LengthMass (Da)Tools
P40423 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 2D95C9F0460B8766

FASTA17419,954
        10         20         30         40         50         60 
MSSRKTAGRR ATTKKRAQRA TSNVFAMFDQ AQIAEFKEAF NMIDQNRDGF VEKEDLHDML 

        70         80         90        100        110        120 
ASLGKNPTDD YLDGMMNEAP GPINFTMFLT LFGERLQGTD PEDVIKNAFG CFDEENMGVL 

       130        140        150        160        170 
PEDRLRELLT TMGDRFTDED VDEMYREAPI KNGLFDYLEF TRILKHGAKD KDEQ 

« Hide

References

« Hide 'large scale' references
[1]"The regulatory light chain of nonmuscle myosin is encoded by spaghetti-squash, a gene required for cytokinesis in Drosophila."
Karess R.E., Chang X.J., Edwards K.A., Kulkarni S., Aguilera I., Kiehart D.P.
Cell 65:1177-1189(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M67494 Genomic DNA. Translation: AAC13367.1.
AE014298 Genomic DNA. Translation: AAF46132.1.
AY122159 mRNA. Translation: AAM52671.1.
PIRA39932.
RefSeqNP_511057.1. NM_078502.2.
UniGeneDm.3.

3D structure databases

ProteinModelPortalP40423.
SMRP40423. Positions 28-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58046. 13 interactions.
IntActP40423. 1 interaction.

Proteomic databases

PaxDbP40423.
PRIDEP40423.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070877; FBpp0070842; FBgn0003514.
GeneID31554.
KEGGdme:Dmel_CG3595.

Organism-specific databases

CTD31554.
FlyBaseFBgn0003514. sqh.

Phylogenomic databases

eggNOGCOG5126.
GeneTreeENSGT00730000110490.
InParanoidP40423.
KOK12757.
OMANEEHLRE.
OrthoDBEOG7992RX.
PhylomeDBP40423.

Gene expression databases

BgeeP40423.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi31554.
NextBio774178.

Entry information

Entry nameSQH_DROME
AccessionPrimary (citable) accession number: P40423
Secondary accession number(s): Q540V2, Q9W428
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase