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Reviewed, UniProtKB/Swiss-Prot P42325 (NCAH_DROME)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Neurocalcin homolog
      Short name=DrosNCa
Gene names
Name: Nca
ORF Names: CG7641
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Inhibits the phosphorylation of rhodopsin in a calcium-dependent manner. Probably binds two or three calcium ions. Ref.1 Ref.5

Tissue specificity

Expressed in neuronal tissues. High level expression seen in the cortical regions of the central brain and lower levels in the lamina, the first optic lobe of the brain. It is also found in the thoracic ganglia. Ref.1

Developmental stage

Found in the embryos, larvae and pupae. Expression in the adult heads is higher than in the bodies. Ref.1

Sequence similarities

Belongs to the recoverin family.

Contains 4 EF-hand domains.

Mass spectrometry

Molecular mass is 21975.51 Da from positions 2 - 190. Determined by ESI. Ref.5

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
   PTMLipoprotein
Myristate
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functioncalcium ion binding Ref.1

Inferred from direct assay. Source: FlyBase

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 190189Neurocalcin homolog
PRO_0000073801

Regions

Domain23 – 5836EF-hand 1
Domain60 – 9536EF-hand 2
Domain96 – 13136EF-hand 3
Domain144 – 17936EF-hand 4
Calcium binding73 – 84121 Potential
Calcium binding109 – 120122 Potential
Calcium binding157 – 168123 Potential

Amino acid modifications

Lipidation21N-myristoyl glycine

Sequences

Sequence LengthMass (Da)Tools
P42325-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F1158FEB8CF13F64

FASTA19021,894
        10         20         30         40         50         60 
MGKQNSKLKP EVLEDLKQNT EFTDAEIQEW YKGFLKDCPS GHLSVEEFKK IYGNFFPYGD 

        70         80         90        100        110        120 
ASKFAEHVFR TFDANGDGTI DFREFLCALS VTSRGKLEQK LKWAFSMYDL DGNGYISRQE 

       130        140        150        160        170        180 
MLEIVTAIYK MVGSVMKMPE DESTPEKRTD KIFRQMDRNK DGKLSLEEFI EGAKSDPSIV 

       190 
RLLQCDPQSH 

« Hide

References

« Hide 'large scale' references
[1]"A highly conserved homologue of bovine neurocalcin in Drosophila melanogaster is a Ca(2+)-binding protein expressed in neuronal tissues."
Teng D.H.-F., Chen C.-K., Hurley J.B.
J. Biol. Chem. 269:31900-31907(1994) [PubMed: 7989365] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Canton-S.
[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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Drosophila neurocalcin, a fatty acylated, Ca2+-binding protein that associates with membranes and inhibits in vitro phosphorylation of bovine rhodopsin."
Faurobert E., Chen C.-K., Hurley J.B., Teng D.H.-F.
J. Biol. Chem. 271:10256-10262(1996) [PubMed: 8626592] [Abstract]
Cited for: FUNCTION, MASS SPECTROMETRY, MYRISTOYLATION AT GLY-2.

Cross-references

Sequence databases

U15735 mRNA. Translation: AAA62152.1.
AE014296 Genomic DNA. Translation: AAF49082.1.
AY071612 mRNA. Translation: AAL49234.1.
PIRA55666.
RefSeqNP_788543.1.
UniGeneDm.6656

3D structure databases

HSSPHSSP built from PDB template 1BJF based on UniProtKB P29554.
SMRP42325. Positions 5-185.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:19235N.
IntActP42325. 16 interactions.

Genome annotation databases

EnsemblFBgn0013303. Drosophila melanogaster. [Contig view]
GeneID40186.
KEGGdme:Dmel_CG7641.
NMPDRfig|7227.3.peg.10652.

Organism-specific databases

FlyBaseFBgn0013303. Nca.

Phylogenomic databases

HOGENOMP42325.
OMAP42325. DCPSGNL.

Gene expression databases

GermOnlineCG7641. Drosophila melanogaster.

Family and domain databases

InterProIPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR001125. Recoverin.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PfamPF00036. efhand. 3 hits.
[Graphical view]
PRINTSPR00450. RECOVERIN.
ProDomPD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio817463.

Entry information

Entry nameNCAH_DROME
AccessionPrimary (citable) accession number: P42325
Secondary accession number(s): Q9VW67
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents