ID NOSL_BOMMO Reviewed; 1097 AA. AC B1B557; B9X250; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 24-JAN-2024, entry version 86. DE RecName: Full=Nitric oxide synthase-like protein; DE EC=1.14.13.39; GN Name=NSL {ECO:0000312|EMBL:BAG12563.1}; OS Bombyx mori (Silk moth). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Bombycidae; Bombycinae; Bombyx. OX NCBI_TaxID=7091; RN [1] {ECO:0000305, ECO:0000312|EMBL:BAG12563.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Wing imaginal disk {ECO:0000312|EMBL:BAG12563.1}; RX PubMed=18505883; DOI=10.1534/genetics.107.082784; RA Sato K., Matsuoka-Matsunaga T., Futahashi R., Kojima T., Mita K., Banno Y., RA Fujiwara H.; RT "Positional cloning of a Bombyx wingless locus flugellos (fl) reveals a RT crucial role for fringe that is specific for wing morphogenesis."; RL Genetics 179:875-885(2008). RN [2] {ECO:0000305, ECO:0000312|EMBL:BAH23564.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Reproductive system {ECO:0000312|EMBL:BAH23564.1}; RA Nagaoka S., Takata Y.; RT "Identification of nitric-oxide synthase from Bombyx mori."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with CC diverse functions throughout the body. {ECO:0000250}. 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 -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000250|UniProtKB:P29475}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P29475}; CC Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29475}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000250|UniProtKB:P29475}; CC Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P29475}; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist. {ECO:0000305}; CC Name=1 {ECO:0000312|EMBL:BAG12563.1}; CC IsoId=B1B557-1; Sequence=Displayed; CC Name=2 {ECO:0000312|EMBL:BAH23564.1}; CC IsoId=B1B557-2; Sequence=VSP_040368; CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB360590; BAG12563.1; -; mRNA. DR EMBL; AB485776; BAH23564.1; -; mRNA. DR RefSeq; NP_001116808.1; NM_001123336.1. [B1B557-1] DR AlphaFoldDB; B1B557; -. DR SMR; B1B557; -. DR STRING; 7091.B1B557; -. DR PaxDb; 7091-BGIBMGA002937-TA; -. DR EnsemblMetazoa; NM_001123336.1; NP_001116808.1; GeneID_100144542. [B1B557-1] DR GeneID; 100144542; -. DR KEGG; bmor:100144542; -. DR CTD; 4843; -. DR eggNOG; KOG1158; Eukaryota. DR HOGENOM; CLU_001570_16_0_1; -. DR InParanoid; B1B557; -. DR OMA; QVFDCRQ; -. DR OrthoDB; 276396at2759; -. DR Proteomes; UP000005204; Unassembled WGS sequence. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. 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; IEA:UniProtKB-EC. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro. DR CDD; cd00795; NOS_oxygenase_euk; 1. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1. DR PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1. 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; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. DR PROSITE; PS60001; NOS; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Calmodulin-binding; FAD; Flavoprotein; FMN; Heme; KW Iron; Metal-binding; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..1097 FT /note="Nitric oxide synthase-like protein" FT /id="PRO_0000403314" FT DOMAIN 420..615 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088" FT DOMAIN 669..914 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 387..410 FT /note="Calmodulin-binding" FT /evidence="ECO:0000250|UniProtKB:P29475" FT BINDING 77 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 140 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 249 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 250 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 254 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 259 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 340 FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin" FT /ligand_id="ChEBI:CHEBI:59560" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 353 FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin" FT /ligand_id="ChEBI:CHEBI:59560" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 368 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P29474" FT BINDING 426..430 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088" FT BINDING 561..592 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088" FT BINDING 704..715 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29475" FT BINDING 847..857 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P29475" FT BINDING 922..940 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29475" FT BINDING 1019..1034 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P29475" FT VAR_SEQ 1..231 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_040368" FT CONFLICT 604 FT /note="D -> G (in Ref. 2; BAH23564)" FT /evidence="ECO:0000305" FT CONFLICT 675 FT /note="T -> A (in Ref. 2; BAH23564)" FT /evidence="ECO:0000305" FT CONFLICT 885 FT /note="Y -> F (in Ref. 2; BAH23564)" FT /evidence="ECO:0000305" FT CONFLICT 998 FT /note="T -> M (in Ref. 2; BAH23564)" FT /evidence="ECO:0000305" SQ SEQUENCE 1097 AA; 124059 MW; BE3639FFEA05DE35 CRC64; MAIPGRGDVP RDPEEVLNDA KDFLGQYFAS IRRANTPAHE ARWKIVQEEV ATTGTYQLTT TELVFGAKLA WRNASRCIGR IQWSKLQVFD CRQVTTTSGM FEALCNHIKY STNKGNIRSA ITLFPQRTDG KHDYRIWNSQ LISYAGYRQP DGTVLGDPMH CEFTDLCLKL GWKPPRTAWD ILPLVLSANG KDPDYFEIPR ELVMEIHMTH PTFEWFKELE LRWYALPAVS SMRFDCGGIE FTANAFNGWY MSTEIGCRNF CDTNRLNVLE KIAQNMGLDT RTPVNLWKDK ALVEVNVAVL HSFQQHNATI VDHHTASESF IKHLDNENRL RSGCPADWIW IVPPMSSSIT PVFHQEMALY YLKPSYEYQE PAWKTHQWQK SKPITGKRPI NRKFHFKQIA RAVKFTSKLF GRALSKRIKA TVLYATETGK SEQYAKELGV IFGHAFNAQV HCMADYDITS IEHEALLLVV TSTFGNGDPP ENGVAFGEHL CEILYADQVG EDSTGNQMLT PKSFIKANSD IQRYTAGNPK KLNRLESLKG STTDATSIDS FGPLSNVRFA VFALGSSAYP NFCNFGKYVD KLLVDLGGER IHDLATGDEM CGQDQAFRKW ASSVFNVACE TFCLDDDETL QEAKRALGTV ALSEETVQFA RAGCRPATLH AALQKSLNKQ FVSCTVKANK DLGDASAERS TIFIDLEPKE EIKYNPGDHV GIIACNRKEL VESLLSRIKD VDDYDEPLQL QLLKETHTSS GLVKSWEPHE KLPIMSVREL FTRFLDITTP PTTILLQYLA TTCEDEEEKK QLNVLATDPG AYEDWRHFHF PTLPEVLDQF PSARPNASLL AALLSPLQPR FYSISSSPLA HAKRLHLTVA VVTYRTQDGE GPVHYGVCSN YLMERKPGDE VYLFIRSAPN FHLPQDLSVP LILIGPGTGI APFRGFWHHR RALQNSCSRT TTGPVWLFFG CRTKTMDLYR EEKEQALKEG VLSKVFLALS REKEVPKTYV QEVAENVGAE IHDLLINKGA HFYVCGDCKM AEDVHQKLKG IVKKHGNMTD EQVQNFMFML KEENRYHEDI FGITLRTAEV HSASRESARR NRVASQP //