NINAG_DROME
ID NINAG_DROME Reviewed; 581 AA.
AC Q9VGP2; Q8MSH3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Neither inactivation nor afterpotential protein G;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=ninaG; ORFNames=CG6728;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [4]
RP FUNCTION.
RX PubMed=15640158; DOI=10.1074/jbc.m412236200;
RA Sarfare S., Ahmad S.T., Joyce M.V., Boggess B., O'Tousa J.E.;
RT "The Drosophila ninaG oxidoreductase acts in visual pigment chromophore
RT production.";
RL J. Biol. Chem. 280:11895-11901(2005).
RN [5]
RP FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=16464863; DOI=10.1074/jbc.m510293200;
RA Ahmad S.T., Joyce M.V., Boggess B., O'tousa J.E.;
RT "The role of Drosophila ninaG oxidoreductase in visual pigment chromophore
RT biogenesis.";
RL J. Biol. Chem. 281:9205-9209(2006).
CC -!- FUNCTION: Oxidoreductase involved in biosynthesis of 3-hydroxyretinal,
CC a chromophore for rhodopsin Rh1. Not responsible for the initial
CC hydroxylation of the retinal ring but rather acts in a subsequent step
CC in chromophore production. May catalyze the conversion of (3R)-3-
CC hydroxyretinol to the 3S enantiomer. {ECO:0000269|PubMed:15640158,
CC ECO:0000269|PubMed:16464863}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF54634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF54634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY118818; AAM50678.1; -; mRNA.
DR RefSeq; NP_001247047.1; NM_001260118.1.
DR RefSeq; NP_650070.1; NM_141813.2.
DR AlphaFoldDB; Q9VGP2; -.
DR SMR; Q9VGP2; -.
DR IntAct; Q9VGP2; 1.
DR STRING; 7227.FBpp0081880; -.
DR GlyGen; Q9VGP2; 4 sites.
DR PaxDb; Q9VGP2; -.
DR PRIDE; Q9VGP2; -.
DR EnsemblMetazoa; FBtr0301146; FBpp0290369; FBgn0037896.
DR GeneID; 41369; -.
DR KEGG; dme:Dmel_CG6728; -.
DR UCSC; CG6728-RA; d. melanogaster.
DR CTD; 41369; -.
DR FlyBase; FBgn0037896; ninaG.
DR VEuPathDB; VectorBase:FBgn0037896; -.
DR eggNOG; KOG1238; Eukaryota.
DR GeneTree; ENSGT00530000063260; -.
DR InParanoid; Q9VGP2; -.
DR PhylomeDB; Q9VGP2; -.
DR BioCyc; MetaCyc:MON-17371; -.
DR BioGRID-ORCS; 41369; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41369; -.
DR PRO; PR:Q9VGP2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037896; Expressed in head capsule and 2 other tissues.
DR ExpressionAtlas; Q9VGP2; baseline and differential.
DR Genevisible; Q9VGP2; DM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IMP:UniProtKB.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:1990146; P:protein localization to rhabdomere; IMP:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0001523; P:retinoid metabolic process; IMP:UniProtKB.
DR GO; GO:0061541; P:rhabdomere morphogenesis; IMP:UniProtKB.
DR GO; GO:0046154; P:rhodopsin metabolic process; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 2.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Secreted; Sensory transduction; Signal; Vision.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..581
FT /note="Neither inactivation nor afterpotential protein G"
FT /id="PRO_0000235295"
FT ACT_SITE 516
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 48..77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 581 AA; 63475 MW; A2F13BEBC25E496D CRC64;
MGMKFQKILV LAGIVIGFLS IIVVLAGTLL KNSVPNVLAP VERHFAFDYV IVGGGTGGST
LTSLLAKNSN GSVLLIEAGG QFGLLSRIPL LTTFQQKGIN DWSFLSVPQK HSSRGLIERR
QCLPRGKGLG GSANLNYMLH FDGHGPDFDS WRDHHNLSDW SWAQMRSFMA AAKPKNPDML
EIPRRYSKLT EALEEAQAQF AYKDWIFRRS LYNIRNGLRH SVVQQFLNPV IHHSNLRLLP
DALVKRIQLA PSPFLQATSI LVGIKDEENR EKEFSIELLM ASGIGDVSAL KKLGIPAQHS
LPLVGHNLHD HFNLPLFVSM GVTGPTLNQN TLLNPMTLIN YLSSGSGPLG NFGVLGNVVS
YGGLGAPPYG ITFFGAGAID ESALMSISNF KGPAFRALFP RYYNSSQEGF VVISSCLQPK
SRGSVGLLNR HMRRNPLIDP NYLSSEEDVA CTISAIRSAV ELVNSTAFAA LHPRIHWPRV
QECSNFGPFE RDFFDNRPSD QYLECLMRHV GLGSHHPGGT CALGSVVDSQ LRLKGVSNVR
VVDASVLPRP ISGNPNSVVV AIALRAASWI LKSELQAGDS K
