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P40423

- SQH_DROME

UniProt

P40423 - SQH_DROME

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Protein
Myosin regulatory light chain sqh
Gene
sqh, CG3595
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi44 – 5512 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. myosin heavy chain binding Source: FlyBase
Complete GO annotation...

GO - Biological processi

  1. actin filament-based movement Source: FlyBase
  2. border follicle cell migration Source: FlyBase
  3. cell elongation involved in imaginal disc-derived wing morphogenesis Source: FlyBase
  4. cellularization Source: FlyBase
  5. cytoskeleton-dependent cytoplasmic transport, nurse cell to oocyte Source: FlyBase
  6. establishment of planar polarity Source: FlyBase
  7. formation of a compartment boundary Source: FlyBase
  8. imaginal disc-derived wing hair organization Source: FlyBase
  9. mitotic cytokinesis Source: FlyBase
  10. neurogenesis Source: FlyBase
  11. nuclear axial expansion Source: FlyBase
  12. ovarian follicle cell development Source: FlyBase
  13. ovarian nurse cell to oocyte transport Source: FlyBase
  14. regulation of actin cytoskeleton organization Source: FlyBase
  15. regulation of tube length, open tracheal system Source: FlyBase
  16. spiracle morphogenesis, open tracheal system Source: FlyBase
  17. wound healing Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_211028. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin regulatory light chain sqh
Alternative name(s):
Myosin regulatory light chain, nonmuscle
Short name:
MRLC-C
Protein spaghetti-squash
Gene namesi
Name:sqh
ORF Names:CG3595
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003514. sqh.

Subcellular locationi

GO - Cellular componenti

  1. adherens junction Source: FlyBase
  2. apical plasma membrane Source: FlyBase
  3. cell cortex Source: FlyBase
  4. cleavage furrow Source: FlyBase
  5. cytoplasm Source: FlyBase
  6. female germline ring canal inner rim Source: FlyBase
  7. midbody Source: FlyBase
  8. myosin II complex Source: FlyBase
  9. plasma membrane Source: FlyBase
  10. spindle midzone Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mitotic defects including failure in cytokinesis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 174174Myosin regulatory light chain sqh
PRO_0000198747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphothreonine2 Publications
Modified residuei22 – 221Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation plays a central role in myosin regulation By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP40423.
PRIDEiP40423.

Expressioni

Gene expression databases

BgeeiP40423.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi58046. 13 interactions.
IntActiP40423. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP40423.
SMRiP40423. Positions 28-169.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 6636EF-hand 1
Add
BLAST
Domaini100 – 13536EF-hand 2
Add
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00730000110490.
InParanoidiP40423.
KOiK12757.
OMAiNEEHLRE.
OrthoDBiEOG7992RX.
PhylomeDBiP40423.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40423-1 [UniParc]FASTAAdd to Basket

« Hide

MSSRKTAGRR ATTKKRAQRA TSNVFAMFDQ AQIAEFKEAF NMIDQNRDGF    50
VEKEDLHDML ASLGKNPTDD YLDGMMNEAP GPINFTMFLT LFGERLQGTD 100
PEDVIKNAFG CFDEENMGVL PEDRLRELLT TMGDRFTDED VDEMYREAPI 150
KNGLFDYLEF TRILKHGAKD KDEQ 174
Length:174
Mass (Da):19,954
Last modified:February 1, 1995 - v1
Checksum:i2D95C9F0460B8766
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M67494 Genomic DNA. Translation: AAC13367.1.
AE014298 Genomic DNA. Translation: AAF46132.1.
AY122159 mRNA. Translation: AAM52671.1.
PIRiA39932.
RefSeqiNP_511057.1. NM_078502.2.
UniGeneiDm.3.

Genome annotation databases

EnsemblMetazoaiFBtr0070877; FBpp0070842; FBgn0003514.
GeneIDi31554.
KEGGidme:Dmel_CG3595.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M67494 Genomic DNA. Translation: AAC13367.1 .
AE014298 Genomic DNA. Translation: AAF46132.1 .
AY122159 mRNA. Translation: AAM52671.1 .
PIRi A39932.
RefSeqi NP_511057.1. NM_078502.2.
UniGenei Dm.3.

3D structure databases

ProteinModelPortali P40423.
SMRi P40423. Positions 28-169.
ModBasei Search...

Protein-protein interaction databases

BioGridi 58046. 13 interactions.
IntActi P40423. 1 interaction.

Proteomic databases

PaxDbi P40423.
PRIDEi P40423.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0070877 ; FBpp0070842 ; FBgn0003514 .
GeneIDi 31554.
KEGGi dme:Dmel_CG3595.

Organism-specific databases

CTDi 31554.
FlyBasei FBgn0003514. sqh.

Phylogenomic databases

eggNOGi COG5126.
GeneTreei ENSGT00730000110490.
InParanoidi P40423.
KOi K12757.
OMAi NEEHLRE.
OrthoDBi EOG7992RX.
PhylomeDBi P40423.

Enzyme and pathway databases

Reactomei REACT_211028. Smooth Muscle Contraction.

Miscellaneous databases

GenomeRNAii 31554.
NextBioi 774178.

Gene expression databases

Bgeei P40423.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF13499. EF-hand_7. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 2 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiSQH_DROME
AccessioniPrimary (citable) accession number: P40423
Secondary accession number(s): Q540V2, Q9W428
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

This chain binds calcium By similarity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi