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Protein

Neither inactivation nor afterpotential protein G

Gene

ninaG

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Oxidoreductase involved in biosynthesis of 3-hydroxyretinal, a chromophore for rhodopsin Rh1. Not responsible for the initial hydroxylation of the retinal ring but rather acts in a subsequent step in chromophore production. May catalyze the conversion of (3R)-3-hydroxyretinol to the 3S enantiomer.2 Publications

Cofactori

FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei516 – 5161Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 7730FADBy similarityAdd
BLAST

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • oxidoreductase activity Source: UniProtKB
  • oxidoreductase activity, acting on CH-OH group of donors Source: InterPro

GO - Biological processi

  • response to stimulus Source: UniProtKB-KW
  • retinoid metabolic process Source: UniProtKB
  • rhodopsin metabolic process Source: UniProtKB
  • transport Source: UniProtKB
  • visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17371.

Names & Taxonomyi

Protein namesi
Recommended name:
Neither inactivation nor afterpotential protein G (EC:1.-.-.-)
Gene namesi
Name:ninaG
ORF Names:CG6728
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0037896. ninaG.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 581555Neither inactivation nor afterpotential protein GPRO_0000235295Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence analysis
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence analysis
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence analysis
Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9VGP2.

Expressioni

Gene expression databases

BgeeiQ9VGP2.
GenevisibleiQ9VGP2. DM.

Interactioni

Protein-protein interaction databases

IntActiQ9VGP2. 1 interaction.
STRINGi7227.FBpp0081880.

Structurei

3D structure databases

ProteinModelPortaliQ9VGP2.
SMRiQ9VGP2. Positions 44-577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1238. Eukaryota.
COG2303. LUCA.
GeneTreeiENSGT00530000063260.
InParanoidiQ9VGP2.
OrthoDBiEOG70GMFH.
PhylomeDBiQ9VGP2.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 2 hits.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9VGP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGMKFQKILV LAGIVIGFLS IIVVLAGTLL KNSVPNVLAP VERHFAFDYV
60 70 80 90 100
IVGGGTGGST LTSLLAKNSN GSVLLIEAGG QFGLLSRIPL LTTFQQKGIN
110 120 130 140 150
DWSFLSVPQK HSSRGLIERR QCLPRGKGLG GSANLNYMLH FDGHGPDFDS
160 170 180 190 200
WRDHHNLSDW SWAQMRSFMA AAKPKNPDML EIPRRYSKLT EALEEAQAQF
210 220 230 240 250
AYKDWIFRRS LYNIRNGLRH SVVQQFLNPV IHHSNLRLLP DALVKRIQLA
260 270 280 290 300
PSPFLQATSI LVGIKDEENR EKEFSIELLM ASGIGDVSAL KKLGIPAQHS
310 320 330 340 350
LPLVGHNLHD HFNLPLFVSM GVTGPTLNQN TLLNPMTLIN YLSSGSGPLG
360 370 380 390 400
NFGVLGNVVS YGGLGAPPYG ITFFGAGAID ESALMSISNF KGPAFRALFP
410 420 430 440 450
RYYNSSQEGF VVISSCLQPK SRGSVGLLNR HMRRNPLIDP NYLSSEEDVA
460 470 480 490 500
CTISAIRSAV ELVNSTAFAA LHPRIHWPRV QECSNFGPFE RDFFDNRPSD
510 520 530 540 550
QYLECLMRHV GLGSHHPGGT CALGSVVDSQ LRLKGVSNVR VVDASVLPRP
560 570 580
ISGNPNSVVV AIALRAASWI LKSELQAGDS K
Length:581
Mass (Da):63,475
Last modified:May 16, 2006 - v2
Checksum:iA2F13BEBC25E496D
GO

Sequence cautioni

The sequence AAF54634.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54634.1. Sequence problems.
AY118818 mRNA. Translation: AAM50678.1.
RefSeqiNP_001247047.1. NM_001260118.1.
NP_650070.1. NM_141813.2.
UniGeneiDm.13684.

Genome annotation databases

EnsemblMetazoaiFBtr0301146; FBpp0290369; FBgn0037896.
GeneIDi41369.
KEGGidme:Dmel_CG6728.
UCSCiCG6728-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54634.1. Sequence problems.
AY118818 mRNA. Translation: AAM50678.1.
RefSeqiNP_001247047.1. NM_001260118.1.
NP_650070.1. NM_141813.2.
UniGeneiDm.13684.

3D structure databases

ProteinModelPortaliQ9VGP2.
SMRiQ9VGP2. Positions 44-577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9VGP2. 1 interaction.
STRINGi7227.FBpp0081880.

Proteomic databases

PaxDbiQ9VGP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0301146; FBpp0290369; FBgn0037896.
GeneIDi41369.
KEGGidme:Dmel_CG6728.
UCSCiCG6728-RA. d. melanogaster.

Organism-specific databases

CTDi41369.
FlyBaseiFBgn0037896. ninaG.

Phylogenomic databases

eggNOGiKOG1238. Eukaryota.
COG2303. LUCA.
GeneTreeiENSGT00530000063260.
InParanoidiQ9VGP2.
OrthoDBiEOG70GMFH.
PhylomeDBiQ9VGP2.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17371.

Miscellaneous databases

GenomeRNAii41369.
NextBioi823513.
PROiQ9VGP2.

Gene expression databases

BgeeiQ9VGP2.
GenevisibleiQ9VGP2. DM.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 2 hits.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  4. "The Drosophila ninaG oxidoreductase acts in visual pigment chromophore production."
    Sarfare S., Ahmad S.T., Joyce M.V., Boggess B., O'Tousa J.E.
    J. Biol. Chem. 280:11895-11901(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The role of Drosophila ninaG oxidoreductase in visual pigment chromophore biogenesis."
    Ahmad S.T., Joyce M.V., Boggess B., O'tousa J.E.
    J. Biol. Chem. 281:9205-9209(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY.

Entry informationi

Entry nameiNINAG_DROME
AccessioniPrimary (citable) accession number: Q9VGP2
Secondary accession number(s): Q8MSH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: January 20, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.