ID   NOSIP_DROME             Reviewed;         307 AA.
AC   Q9VWV8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Nitric oxide synthase-interacting protein homolog;
GN   ORFNames=CG6179;
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).
CC   -!- FUNCTION: Negatively regulates nitric oxide production by inducing
CC       nitric oxide synthase translocation to actin cytoskeleton and
CC       inhibiting its enzymatic activity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NOSIP family. {ECO:0000305}.
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DR   EMBL; AE014298; AAF48829.1; -; Genomic_DNA.
DR   RefSeq; NP_573288.1; NM_133060.3.
DR   AlphaFoldDB; Q9VWV8; -.
DR   BioGRID; 59136; 1.
DR   STRING; 7227.FBpp0074330; -.
DR   PaxDb; Q9VWV8; -.
DR   DNASU; 32819; -.
DR   EnsemblMetazoa; FBtr0074558; FBpp0074330; FBgn0030915.
DR   GeneID; 32819; -.
DR   KEGG; dme:Dmel_CG6179; -.
DR   UCSC; CG6179-RA; d. melanogaster.
DR   FlyBase; FBgn0030915; CG6179.
DR   VEuPathDB; VectorBase:FBgn0030915; -.
DR   eggNOG; KOG3039; Eukaryota.
DR   GeneTree; ENSGT00390000015505; -.
DR   HOGENOM; CLU_053742_0_0_1; -.
DR   InParanoid; Q9VWV8; -.
DR   OMA; AKEKRPM; -.
DR   OrthoDB; 1567031at2759; -.
DR   PhylomeDB; Q9VWV8; -.
DR   Reactome; R-DME-203754; NOSIP mediated eNOS trafficking.
DR   BioGRID-ORCS; 32819; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 32819; -.
DR   PRO; PR:Q9VWV8; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0030915; Expressed in cleaving embryo and 21 other tissues.
DR   ExpressionAtlas; Q9VWV8; baseline and differential.
DR   Genevisible; Q9VWV8; DM.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:FlyBase.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
DR   GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR016818; NOSIP.
DR   InterPro; IPR031790; Znf-NOSIP.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13063; PTHR13063; 1.
DR   Pfam; PF15906; zf-NOSIP; 1.
DR   PIRSF; PIRSF023577; ENOS_interacting; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..307
FT                   /note="Nitric oxide synthase-interacting protein homolog"
FT                   /id="PRO_0000280592"
FT   REGION          120..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   307 AA;  34158 MW;  32DE54BF6DD3330D CRC64;
     MTRHARNCTA GAVYTYNEKK RDAAESGYGT NAQRLGKDSV KSFDCCSLTL QPCRRPVITK
     DGYLFDKEAI LQYIVTKKNE YSRRLKEYER LRRAEEDKLS QEANSKQQAR MERFVNAEKP
     AMTPAHSSAA ASEKPSTSSA AAAASSESSS ASSISNMTNG HEKKLPSFWL PSECPNAGLA
     KAQKPDATIY CPVSQKPLRV KDLIDVKFTL LKDGDTKRSL IAKEARYMCP ITHDVLSNAV
     PCAVLRPTGD VVTMECVERL IRKDMIHPLT DRKLKEKDII PLQRGGTGYA TTNDHLQAKE
     KRPMLQA