NOS_DROME
ID NOS_DROME Reviewed; 1349 AA.
AC Q27571; A4V0K9; A4V0L0; Q4ABG3; Q4ABG4; Q4ABG5; Q4ABG6; Q4ABG7; Q7YU33;
AC Q9U096; Q9VKP8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Nitric oxide synthase {ECO:0000303|PubMed:7568075};
DE Short=dNOS {ECO:0000303|PubMed:7568075};
DE EC=1.14.13.39 {ECO:0000269|PubMed:7568075, ECO:0000305|PubMed:12804606};
GN Name=Nos; ORFNames=CG6713;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, AND ACTIVITY REGULATION.
RC TISSUE=Head;
RX PubMed=7568075; DOI=10.1073/pnas.92.20.9072;
RA Regulski M., Tully T.;
RT "Molecular and biochemical characterization of dNOS: a Drosophila
RT Ca2+/calmodulin-dependent nitric oxide synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9072-9076(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE SPLICING, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo, and Larva;
RX PubMed=11526108; DOI=10.1074/jbc.m105066200;
RA Stasiv Y., Regulski M., Kuzin B., Tully T., Enikolopov G.;
RT "The Drosophila nitric-oxide synthase gene (dNOS) encodes a family of
RT proteins that can modulate NOS activity by acting as dominant negative
RT regulators.";
RL J. Biol. Chem. 276:42241-42251(2001).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=12804606; DOI=10.1016/s0006-291x(03)01003-9;
RA Sengupta R., Sahoo R., Mukherjee S., Regulski M., Tully T., Stuehr D.J.,
RA Ghosh S.;
RT "Characterization of Drosophila nitric oxide synthase: a biochemical
RT study.";
RL Biochem. Biophys. Res. Commun. 306:590-597(2003).
CC -!- FUNCTION: Catalyzes the conversion of L-arginine to L-citrulline
CC producing nitric oxide (NO) which is a messenger molecule with diverse
CC functions throughout the body (PubMed:7568075, PubMed:12804606).
CC Truncated isoforms (isoform 3-isoform 6) are able to form intracellular
CC complexes with the full-length protein and serve as dominant negative
CC inhibitors of the enzyme activity. {ECO:0000269|PubMed:11526108,
CC ECO:0000269|PubMed:12804606, ECO:0000269|PubMed:7568075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC Evidence={ECO:0000269|PubMed:7568075, ECO:0000305|PubMed:12804606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC Evidence={ECO:0000269|PubMed:7568075, ECO:0000305|PubMed:12804606};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin.
CC {ECO:0000269|PubMed:12804606, ECO:0000269|PubMed:7568075}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1 {ECO:0000305}; Synonyms=A {ECO:0000312|FlyBase:FBgn0011676},
CC dNOS-1;
CC IsoId=Q27571-1; Sequence=Displayed;
CC Name=2 {ECO:0000305}; Synonyms=dNOS-2 {ECO:0000303|PubMed:11526108};
CC IsoId=Q27571-2; Sequence=VSP_003587;
CC Name=3 {ECO:0000305}; Synonyms=dNOS-3 {ECO:0000303|PubMed:11526108};
CC IsoId=Q27571-3; Sequence=VSP_003585, VSP_003586;
CC Name=4 {ECO:0000305}; Synonyms=B, dNOS-4 {ECO:0000303|PubMed:11526108},
CC F {ECO:0000312|FlyBase:FBgn0011676};
CC IsoId=Q27571-4; Sequence=VSP_003592, VSP_003593;
CC Name=5 {ECO:0000305}; Synonyms=dNOS-5 {ECO:0000303|PubMed:11526108};
CC IsoId=Q27571-5; Sequence=VSP_003588, VSP_003589;
CC Name=6 {ECO:0000305}; Synonyms=dNOS-6 {ECO:0000303|PubMed:11526108};
CC IsoId=Q27571-6; Sequence=VSP_003590, VSP_003591;
CC Name=10 {ECO:0000305}; Synonyms=dNOS-10 {ECO:0000303|PubMed:11526108};
CC IsoId=Q27571-7; Sequence=VSP_003594;
CC -!- DEVELOPMENTAL STAGE: Isoform 3 is expressed in larvae only. Isoform 4,
CC isoform 5, isoform 6 and isoform 10 are expressed throughout
CC development from embryos to adults. {ECO:0000269|PubMed:11526108}.
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ66452.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U25117; AAC46882.1; -; mRNA.
DR EMBL; AF215700; AAF25682.1; -; Genomic_DNA.
DR EMBL; AF215691; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AF215692; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AF215693; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AF215694; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AF215695; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AF215696; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AF215697; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AF215698; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AF215699; AAF25682.1; JOINED; Genomic_DNA.
DR EMBL; AE014134; AAF53014.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66450.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66451.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66452.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014134; AAZ66453.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66454.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66455.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66456.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66457.1; -; Genomic_DNA.
DR EMBL; BT010016; AAQ22485.1; -; mRNA.
DR PIR; T13254; T13254.
DR RefSeq; NP_001027240.1; NM_001032069.2. [Q27571-4]
DR RefSeq; NP_001027243.2; NM_001032072.2.
DR RefSeq; NP_523541.2; NM_078817.4. [Q27571-1]
DR AlphaFoldDB; Q27571; -.
DR SMR; Q27571; -.
DR BioGRID; 60568; 5.
DR IntAct; Q27571; 2.
DR STRING; 7227.FBpp0099922; -.
DR PaxDb; Q27571; -.
DR PRIDE; Q27571; -.
DR EnsemblMetazoa; FBtr0080188; FBpp0079777; FBgn0011676. [Q27571-1]
DR EnsemblMetazoa; FBtr0100489; FBpp0099926; FBgn0011676. [Q27571-4]
DR GeneID; 34495; -.
DR KEGG; dme:Dmel_CG6713; -.
DR CTD; 34495; -.
DR FlyBase; FBgn0011676; Nos.
DR VEuPathDB; VectorBase:FBgn0011676; -.
DR eggNOG; KOG1158; Eukaryota.
DR GeneTree; ENSGT00940000168337; -.
DR InParanoid; Q27571; -.
DR PhylomeDB; Q27571; -.
DR Reactome; R-DME-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DME-203615; eNOS activation.
DR Reactome; R-DME-203754; NOSIP mediated eNOS trafficking.
DR Reactome; R-DME-392154; Nitric oxide stimulates guanylate cyclase.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-9033241; Peroxisomal protein import.
DR GenomeRNAi; 34495; -.
DR PRO; PR:Q27571; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011676; Expressed in neuropil and 10 other tissues.
DR Genevisible; Q27571; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0012506; C:vesicle membrane; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; NAS:FlyBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; NAS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004517; F:nitric-oxide synthase activity; IDA:FlyBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006527; P:arginine catabolic process; IBA:GO_Central.
DR GO; GO:0007444; P:imaginal disc development; TAS:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:FlyBase.
DR GO; GO:0008156; P:negative regulation of DNA replication; TAS:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0002027; P:regulation of heart rate; IMP:FlyBase.
DR GO; GO:0046620; P:regulation of organ growth; TAS:FlyBase.
DR GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0007416; P:synapse assembly; TAS:FlyBase.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.1230.10; -; 1.
DR Gene3D; 3.90.340.10; -; 1.
DR Gene3D; 3.90.440.10; -; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR044943; NOS_dom_1.
DR InterPro; IPR044940; NOS_dom_2.
DR InterPro; IPR044944; NOS_dom_3.
DR InterPro; IPR012144; NOS_euk.
DR InterPro; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_sf.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF02898; NO_synthase; 1.
DR PIRSF; PIRSF000333; NOS; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF56512; SSF56512; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS60001; NOS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; FAD; Flavoprotein; FMN; Heme;
KW Iron; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..1349
FT /note="Nitric oxide synthase"
FT /id="PRO_0000170951"
FT DOMAIN 671..868
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 928..1167
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 23..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..661
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 23..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 328
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 391
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 500
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 501
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 505
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 510
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 591
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 604
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 619
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 814..845
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 957..968
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1100..1110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1175..1193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 1273..1287
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT VAR_SEQ 201..214
FT /note="FMHLDDEGRSLLMR -> RFFPARRPPVRAAL (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003585"
FT VAR_SEQ 215..1349
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003586"
FT VAR_SEQ 417..521
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7568075"
FT /id="VSP_003587"
FT VAR_SEQ 701..746
FT /note="IYCMSDYDISSIEHEALLIVVASTFGNGDPPENGELFSQELYAMRV -> CP
FT VGSVSSDPQDPVQLGLVVVLVSSTCVCKKHLPAAWQNKISCKHL (in isoform
FT 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003590"
FT VAR_SEQ 701..704
FT /note="IYCM -> VSLT (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003588"
FT VAR_SEQ 705..1349
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003589"
FT VAR_SEQ 736..756
FT /note="LFSQELYAMRVQESSEHGLQD -> VSTPPRKDHTELINGLGPAAF (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003592"
FT VAR_SEQ 747..1349
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003591"
FT VAR_SEQ 757..1349
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003593"
FT VAR_SEQ 758..1291
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_003594"
FT CONFLICT 20
FT /note="S -> A (in Ref. 1; AAC46882)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="Q -> QQ (in Ref. 1; AAC46882)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="S -> L (in Ref. 1; AAC46882)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> C (in Ref. 1; AAC46882)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="T -> S (in Ref. 2; AAF25682)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197
FT /note="S -> R (in Ref. 1; AAC46882 and 2; AAF25682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1349 AA; 151715 MW; E19D8CBAEFAF76FC CRC64;
MSQHFTSIFE NLRFVTIKRS TNAQQQQQQQ QQQLQQQQQQ LQQQKAQTQQ QNSRKIKTQA
TPTLNGNGLL SGNPNGGGGD SSPSHEVDHP GGAQGAQAAG GLPSSSGTPL RHHKRASIST
ASPPIRERRG TNTSIVVELD GSGSGSGSGG GGVGVGQGAG CPPSGSCTAS GKSSRELSPS
PKNQQQPRKM SQDYRSRAGS FMHLDDEGRS LLMRKPMRLK NIEGRPEVYD TLHCKGREIL
SCSKATCTSS IMNIGNAAVE ARKSDLILEH AKDFLEQYFT SIKRTSSTAH ETRWKQVRQS
IETTGHYQLT ETELIYGAKL AWRNSSRCIG RIQWSKLQVF DCRYVTTTSG MFEAICNHIK
YATNKGNLRS AITIFPQRTD AKHDYRIWNN QLISYAGYKQ ADGKIIGDPM NVEFTEVCTK
LGWKSKGSEW DILPLVVSAN GHDPDYFDYP PELILEVPLT HPKFEWFSDL GLRWYALPAV
SSMLFDVGGI QFTATTFSGW YMSTEIGSRN LCDTNRRNML ETVALKMQLD TRTPTSLWKD
KAVVEMNIAV LHSYQSRNVT IVDHHTASES FMKHFENESK LRNGCPADWI WIVPPLSGSI
TPVFHQEMAL YYLKPSFEYQ DPAWRTHVWK KGRGESKGKK PRRKFNFKQI ARAVKFTSKL
FGRALSKRIK ATVLYATETG KSEQYAKQLC ELLGHAFNAQ IYCMSDYDIS SIEHEALLIV
VASTFGNGDP PENGELFSQE LYAMRVQESS EHGLQDSSIG SSKSFMKASS RQEFMKLPLQ
QVKRIDRWDS LRGSTSDTFT EETFGPLSNV RFAVFALGSS AYPNFCAFGQ YVDNILGELG
GERLLRVAYG DEMCGQEQSF RKWAPEVFKL ACETFCLDPE ESLSDASLAL QNDSLTVNTV
RLVPSANKGS LDSSLSKYHN KKVHCCKAKA KPHNLTRLSE GAKTTMLLEI CAPGLEYEPG
DHVGIFPANR TELVDGLLNR LVGVDNPDEV LQLQLLKEKQ TSNGIFKCWE PHDKIPPDTL
RNLLARFFDL TTPPSRQLLT LLAGFCEDTA DKERLELLVN DSSAYEDWRH WRLPHLLDVL
EEFPSCRPPA PLLLAQLTPL QPRFYSISSS PRRVSDEIHL TVAIVKYRCE DGQGDERYGV
CSNYLSGLRA DDELFMFVRS ALGFHLPSDR SRPIILIGPG TGIAPFRSFW QEFQVLSDLD
PTAKLPKMWL FFGCRNRDVD LYAEEKAELQ KDQILDRVFL ALSREQAIPK TYVQDLIEQE
FDSLYQLIVQ ERGHIYVCGD VTMAEHVYQT IRKCIAGKEQ KSEAEVETFL LTLRDESRYH
EDIFGITLRT AEIHTKSRAT ARIRMASQP
