NOS_BOMMO
ID NOS_BOMMO Reviewed; 1209 AA.
AC Q8T8C0; Q9BLL0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Nitric oxide synthase {ECO:0000312|EMBL:BAB85836.1};
DE EC=1.14.13.39;
DE AltName: Full=Inducible nitric oxide synthase-like protein;
GN Name=NOS {ECO:0000312|EMBL:BAB85836.1};
GN Synonyms=iNOS-LP {ECO:0000312|EMBL:BAB33296.1};
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:BAB85836.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=Tokai X Asahi {ECO:0000269|PubMed:12000645};
RC TISSUE=Larva {ECO:0000269|PubMed:12000645};
RX PubMed=12000645; DOI=10.1046/j.1365-2583.2002.00333.x;
RA Imamura M., Yang J., Yamakawa M.;
RT "cDNA cloning, characterization and gene expression of nitric oxide
RT synthase from the silkworm, Bombyx mori.";
RL Insect Mol. Biol. 11:257-265(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAH23563.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Reproductive system {ECO:0000312|EMBL:BAH23563.1};
RA Nagaoka S., Takata Y.;
RT "Identification of nitric-oxide synthase from Bombyx mori.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAH23563.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-354.
RA Yang J., Taniai K., Yamakawa M.;
RT "Inducible nitric oxide synthase-like protein(iNOS-LP) cDNA.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC diverse functions throughout the body. Involved in the induction of
CC immune gene expression. {ECO:0000269|PubMed:12000645, ECO:0000305}.
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 -!- ACTIVITY REGULATION: Expression is dependent on and stimulated by
CC NADPH, calcium, BH4 and calmodulin. The activity is not dependent on
CC FAD and is not stimulated by its presence.
CC {ECO:0000269|PubMed:12000645}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed at a low level in the
CC larval fat body, hemocyte, Malpighian tubule, midgut, silk gland and
CC adult antenna. {ECO:0000269|PubMed:12000645}.
CC -!- INDUCTION: Induced strongly in the fat body by lipopolysaccharide
CC (LPS). {ECO:0000269|PubMed:12000645}.
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; AB071182; BAB85836.1; -; mRNA.
DR EMBL; AB485775; BAH23563.1; -; mRNA.
DR EMBL; AB017521; BAB33296.1; -; mRNA.
DR RefSeq; NP_001036963.1; NM_001043498.1.
DR AlphaFoldDB; Q8T8C0; -.
DR SMR; Q8T8C0; -.
DR STRING; 7091.BGIBMGA002938-TA; -.
DR PRIDE; Q8T8C0; -.
DR GeneID; 692510; -.
DR KEGG; bmor:692510; -.
DR CTD; 4842; -.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; Q8T8C0; -.
DR OrthoDB; 90349at2759; -.
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 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 2: Evidence at transcript level;
KW Calmodulin-binding; FAD; Flavoprotein; FMN; Heme; Iron; Metal-binding;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..1209
FT /note="Nitric oxide synthase"
FT /id="PRO_0000403313"
FT DOMAIN 521..723
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 776..1021
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 491..511
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:P29475, ECO:0000255"
FT REGION 603..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 181
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 244
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 353
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 354
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 358
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 363
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 444
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 457
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 472
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 527..531
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 669..700
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 811..822
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 954..964
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 1028..1147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 1128..1143
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT CONFLICT 157
FT /note="R -> K (in Ref. 3; BAB33296)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="F -> L (in Ref. 3; BAB33296)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="T -> I (in Ref. 3; BAB33296)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="A -> P (in Ref. 3; BAB33296)"
FT /evidence="ECO:0000305"
FT CONFLICT 340..341
FT /note="CG -> KK (in Ref. 3; BAB33296)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..352
FT /note="NG -> KN (in Ref. 3; BAB33296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1209 AA; 137507 MW; 92A73F04B12C2E2C CRC64;
MSNFFKICCV KDPGGSAKEN LRKMDQVNGH FVSATCPFSG ESVELKVDSN QKQVKPNLRI
KVPQPIRLKN HVAHDENFDT LHSRINEVTH FNTKCSEKVC QTSIMDIPGR GDTPRTAEEV
FKDAQAFLTQ YYASIKRENS EAHKARLDEV KRELKERGTY QLKTSELVFG AKLAWRNATR
CIGRIQWKKL QIFDCREVTT ASGMFEALCN HIKYATNKGN IRSAITIFPQ RTDGKHDYRI
WNPQLINYAG YQEPDGSITG DPARVEFTEI CMKLGWKAPR TPWDILPLVL SADGKDPEFF
ELPKEIVMEV QFEHPEYDWF KDMGWKWYAL PAVSNMRLAC GGLEFTANSF NGWYMGTEIG
CRNLCDESRL NIVEAVAKKM GLDTNSFVSL WKDKALVEVN IAVLHSFHRD NVSIVDHHSA
SEQFQKHLEN ENKSRGGCPA DWIWIVPPMS SSLTTVFHQE MALYYIRPSY DYQEPPWKTH
QWTKSDGTKT VHRKFHFKQI ARAVKFTSKL FGRALSKRIK ATILYATETG KSEHYAKELG
TIFGHAFNAQ VHCMSEYDMF SIEHETLVLI VASTFGNGEP PANGVDFAEH LFQMLYNETN
NNRGDGTSDL GSGTFKTPTP KSLMRSNSMM TPSFEYKRQL TRLESNKSSV AGASSIEQIG
PLSNVCFAVF GLGSSAYPKF CHFGKTVDKI LGDLGGERIL ELACGDELYG QEQQFRAWSS
KIFQVACETF CLDENGMVKD AKKALGDVPL TEETVRFGKY QGDTKLKAAL EASFRKQLIT
CKVKENKNLG DFSADRATVF VDMQPETEFK YDPGDHVGVL ACNRKEIVDA VLERMKDVDD
YDKTVQLQVM KETLTPTGAI KTWEQHERLP AVTIRQIFTR FLDITTPPST TVLKYLSKAC
TDQNDAAQLK ELAIDSNKYD DWRHLHYPHL AEVLAQFPSC RPQASLLAAL LPSLQPRFYS
ISSSPLAHPH RIHITCAVVV YRTQNGQGPM HYGVCSTYLQ NLKPEDEALV FIRRAPSFHM
PKDLSAPLIL VGPGSGIAPF RGFWHHRKHQ IKNLIPNKQK PGPVWLFFGC RNRGMDLYKE
EKEKALADGV LSKVFLALSR EDSVEKKHIQ TLLEDEGAEI SRMLLDENGH FYVCGDCKMA
EEVQQKLKEI MKKHAKMTEQ EYEEFILNLM DENRYHEDIF GITLRTAEVQ SASREFAKRT
RQESQKSQT
