NOSL_BOMMO
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 03-AUG-2022, entry version 80.
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}.
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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.BGIBMGA002937-TA; -.
DR PRIDE; B1B557; -.
DR EnsemblMetazoa; BGIBMGA002937-RA; BGIBMGA002937-TA; BGIBMGA002937.
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; CAFGKYV; -.
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 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
