Nitric oxide synthase - Bombyx mori (Silk moth)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Nitric oxide synthase
EC=1.14.13.39

Alternative name(s):
Inducible nitric oxide synthase-like protein

Gene names

Name:	NOS
Synonyms:	iNOS-LP

Organism

Bombyx mori (Silk moth) [Reference proteome]

Taxonomic identifier

7091 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length	1209 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. Involved in the induction of immune gene expression. Ref.1
Catalytic activity	2 L-arginine + 3 NADPH + 4 O₂ = 2 L-citrulline + 2 nitric oxide + 3 NADP⁺ + 4 H₂O.
Cofactor	Heme group By similarity. UniProtKB P29475 Binds 1 FAD By similarity. UniProtKB P29475 Binds 1 FMN By similarity. UniProtKB P29475
Enzyme regulation	Expression is dependent on and stimulated by NADPH, calcium, BH4 and calmodulin. The activity is not dependent on FAD and is not stimulated by its presence. Ref.1
Tissue specificity	Constitutively expressed at a low level in the larval fat body, hemocyte, Malpighian tubule, midgut, silk gland and adult antenna. Ref.1
Induction	Induced strongly in the fat body by lipopolysaccharide (LPS). Ref.1
Sequence similarities	Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Ligand	Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nitric oxide biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1209

1209

Nitric oxide synthase

PRO_0000403313

Regions

Domain

521 – 723

203

Flavodoxin-like

Domain

776 – 1021

246

FAD-binding FR-type

Nucleotide binding

527 – 531

5

FMN By similarity

Nucleotide binding

669 – 700

32

FMN By similarity

Nucleotide binding

811 – 822

12

FAD By similarity UniProtKB P29475

Nucleotide binding

954 – 964

11

FAD By similarity UniProtKB P29475

Nucleotide binding

1028 – 1147

120

NADP By similarity UniProtKB P29475

Nucleotide binding

1128 – 1143

16

NADP By similarity UniProtKB P29475

Region

491 – 511

21

Calmodulin-binding Potential UniProtKB P29475

Region

516 – 535

20

Tetrahydrobiopterin-binding By similarity UniProtKB P29475

Sites

Metal binding

181

1

Iron (heme axial ligand) By similarity UniProtKB P29475

Experimental info

Sequence conflict

157

1

R → K in BAB33296. Ref.3

Sequence conflict

205

1

F → L in BAB33296. Ref.3

Sequence conflict

259

1

T → I in BAB33296. Ref.3

Sequence conflict

332

1

A → P in BAB33296. Ref.3

Sequence conflict

340 – 341

2

CG → KK in BAB33296. Ref.3

Sequence conflict

351 – 352

2

NG → KN in BAB33296. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q8T8C0 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 92A73F04B12C2E2C
Show »

FASTA

1,209

137,507

        10         20         30         40         50         60 
MSNFFKICCV KDPGGSAKEN LRKMDQVNGH FVSATCPFSG ESVELKVDSN QKQVKPNLRI 

        70         80         90        100        110        120 
KVPQPIRLKN HVAHDENFDT LHSRINEVTH FNTKCSEKVC QTSIMDIPGR GDTPRTAEEV 

       130        140        150        160        170        180 
FKDAQAFLTQ YYASIKRENS EAHKARLDEV KRELKERGTY QLKTSELVFG AKLAWRNATR 

       190        200        210        220        230        240 
CIGRIQWKKL QIFDCREVTT ASGMFEALCN HIKYATNKGN IRSAITIFPQ RTDGKHDYRI 

       250        260        270        280        290        300 
WNPQLINYAG YQEPDGSITG DPARVEFTEI CMKLGWKAPR TPWDILPLVL SADGKDPEFF 

       310        320        330        340        350        360 
ELPKEIVMEV QFEHPEYDWF KDMGWKWYAL PAVSNMRLAC GGLEFTANSF NGWYMGTEIG 

       370        380        390        400        410        420 
CRNLCDESRL NIVEAVAKKM GLDTNSFVSL WKDKALVEVN IAVLHSFHRD NVSIVDHHSA 

       430        440        450        460        470        480 
SEQFQKHLEN ENKSRGGCPA DWIWIVPPMS SSLTTVFHQE MALYYIRPSY DYQEPPWKTH 

       490        500        510        520        530        540 
QWTKSDGTKT VHRKFHFKQI ARAVKFTSKL FGRALSKRIK ATILYATETG KSEHYAKELG 

       550        560        570        580        590        600 
TIFGHAFNAQ VHCMSEYDMF SIEHETLVLI VASTFGNGEP PANGVDFAEH LFQMLYNETN 

       610        620        630        640        650        660 
NNRGDGTSDL GSGTFKTPTP KSLMRSNSMM TPSFEYKRQL TRLESNKSSV AGASSIEQIG 

       670        680        690        700        710        720 
PLSNVCFAVF GLGSSAYPKF CHFGKTVDKI LGDLGGERIL ELACGDELYG QEQQFRAWSS 

       730        740        750        760        770        780 
KIFQVACETF CLDENGMVKD AKKALGDVPL TEETVRFGKY QGDTKLKAAL EASFRKQLIT 

       790        800        810        820        830        840 
CKVKENKNLG DFSADRATVF VDMQPETEFK YDPGDHVGVL ACNRKEIVDA VLERMKDVDD 

       850        860        870        880        890        900 
YDKTVQLQVM KETLTPTGAI KTWEQHERLP AVTIRQIFTR FLDITTPPST TVLKYLSKAC 

       910        920        930        940        950        960 
TDQNDAAQLK ELAIDSNKYD DWRHLHYPHL AEVLAQFPSC RPQASLLAAL LPSLQPRFYS 

       970        980        990       1000       1010       1020 
ISSSPLAHPH RIHITCAVVV YRTQNGQGPM HYGVCSTYLQ NLKPEDEALV FIRRAPSFHM 

      1030       1040       1050       1060       1070       1080 
PKDLSAPLIL VGPGSGIAPF RGFWHHRKHQ IKNLIPNKQK PGPVWLFFGC RNRGMDLYKE 

      1090       1100       1110       1120       1130       1140 
EKEKALADGV LSKVFLALSR EDSVEKKHIQ TLLEDEGAEI SRMLLDENGH FYVCGDCKMA 

      1150       1160       1170       1180       1190       1200 
EEVQQKLKEI MKKHAKMTEQ EYEEFILNLM DENRYHEDIF GITLRTAEVQ SASREFAKRT 


RQESQKSQT

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References

[1]	"cDNA cloning, characterization and gene expression of nitric oxide synthase from the silkworm, Bombyx mori." Imamura M., Yang J., Yamakawa M. Insect Mol. Biol. 11:257-265(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION. Strain: Tokai X Asahi. Tissue: Larva.
[2]	"Identification of nitric-oxide synthase from Bombyx mori." Nagaoka S., Takata Y. Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Reproductive system.
[3]	"Inducible nitric oxide synthase-like protein(iNOS-LP) cDNA." Yang J., Taniai K., Yamakawa M. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-354.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB071182 mRNA. Translation: BAB85836.1. AB485775 mRNA. Translation: BAH23563.1. AB017521 mRNA. Translation: BAB33296.1.
RefSeq	NP_001036963.1. NM_001043498.1.
UniGene	Bmo.133.
3D structure databases
ProteinModelPortal	Q8T8C0.
SMR	Q8T8C0. Positions 63-482, 518-594.
ModBase	Search...
Proteomic databases
PRIDE	Q8T8C0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	692510.
Organism-specific databases
CTD	4842.
Family and domain databases
Gene3D	1.20.990.10. 1 hit. 3.90.340.10. 1 hit.
InterPro	IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR004030. NO_synthase_oxygenase_dom. IPR026009. NOS. IPR012144. NOS_met. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
PANTHER	PTHR19384:SF5. PTHR19384:SF5. 1 hit.
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. PF02898. NO_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF000333. NOS. 1 hit.
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
SUPFAM	SSF56512. NO_synthase_oxygenase_reg. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. PS60001. NOS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NOS_BOMMO

Accession

Primary (citable) accession number: Q8T8C0
Secondary accession number(s): Q9BLL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2011
Last sequence update:	June 1, 2002
Last modified:	April 3, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Family and domain databases

Entry information

Relevant documents