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Database: UniProt
Entry: A0A452QRU4_URSAM
LinkDB: A0A452QRU4_URSAM
Original site: A0A452QRU4_URSAM 
ID   A0A452QRU4_URSAM        Unreviewed;      1064 AA.
AC   A0A452QRU4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Nitric oxide synthase {ECO:0000256|PIRNR:PIRNR000333};
DE            EC=1.14.13.39 {ECO:0000256|PIRNR:PIRNR000333};
GN   Name=NOS2 {ECO:0000313|Ensembl:ENSUAMP00000008286.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000008286.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000008286.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC       diverse functions. {ECO:0000256|PIRNR:PIRNR000333}.
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:0000256|ARBA:ARBA00035595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC         Evidence={ECO:0000256|ARBA:ARBA00035595};
CC   -!- COFACTOR:
CC       Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC         Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000333};
CC       Note=Binds 1 FAD. {ECO:0000256|PIRNR:PIRNR000333};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000333};
CC       Note=Binds 1 FMN. {ECO:0000256|PIRNR:PIRNR000333};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970,
CC         ECO:0000256|PIRNR:PIRNR000333};
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267,
CC       ECO:0000256|PIRNR:PIRNR000333}.
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DR   AlphaFoldDB; A0A452QRU4; -.
DR   STRING; 9643.ENSUAMP00000008286; -.
DR   Ensembl; ENSUAMT00000009348.1; ENSUAMP00000008286.1; ENSUAMG00000007029.1.
DR   GeneTree; ENSGT00940000159752; -.
DR   OMA; WFMDAEI; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
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:0006527; P:arginine catabolic process; IEA:Ensembl.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR   GO; GO:0051712; P:positive regulation of killing of cells of another organism; IEA:Ensembl.
DR   GO; GO:0032310; P:prostaglandin secretion; IEA:Ensembl.
DR   GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR   CDD; cd00795; NOS_oxygenase_euk; 1.
DR   Gene3D; 3.40.50.360; -; 2.
DR   Gene3D; 6.10.250.410; -; 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; 2.
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   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860,
KW   ECO:0000256|PIRNR:PIRNR000333};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000333};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000333};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000333};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000333};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000333};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000333};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000333};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022}.
FT   DOMAIN          446..584
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          637..877
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         107
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:0000256|PIRSR:PIRSR000333-1"
SQ   SEQUENCE   1064 AA;  121521 MW;  24BB0CEF7A67DAA4 CRC64;
     MTFQDTLHHK AKGDIACKSK SCLGAIMNPK SLTRGPRNKP TPPDELLPQA IEFVNQYYGS
     FKEAKIEEHL ARVEAVTKEI ETTGTYQLTG DELIFATKQA WRNAPRCIGR IQWSNLQVFD
     ARSCSTAKEM FEHICRHLRY ATNNGNIRSA ITVFPQRSDG KHDFRVWNAQ LIRYAGYQMP
     DGTILGDPAS VEFTQLCIDL GWKPKYSRFD VVPLVLQADG QDPEFFEIPP DLVLEVPMEH
     PKYEWFRELQ LKWYALPAVA NMLLEVGGLE FPGCPFNGWY MGTEIGVRDF CDVQRYNILE
     EVGRRMGLET HKLASLWKDR AVVEINVAVL HSFQKRNVSI MDHHSAAESF MKYMQNEYRS
     RGGCPADWIW LVPPISGSIT PVFHQEMLNY VLSPFYYYQV EAWKTHTWQD EKRRPRRRKI
     PFKVLVKAVL FSAMLMRKTM ASRVRATILF ATETGKSETL ARDLGALFSC AFNPKVLCMD
     EYRLRHLEDE QLLLVVTSTF GNGDSPGNGE KLKKSLFLLK ELTNKFRYAV FGLGSSMYPQ
     FCAFAHDIDQ KLSHLGASQL APTGEGDELS GQEEAFRSWA VQTFKAACET FEVQGKHRIQ
     IPRLYTCNVT WDPQHYRLVQ DSQPLDLERA LSSMHAKKVF TLRLKSQRNL QSPQSSRTTL
     LVELSCEDSR GLSYLPGEHL GVCPSNQLAL VQGILERVVD GPSPHQPVHL EILSENGSYW
     VRDKRLPPCS LSQALTHFLD ITTPPTPLLL RKLAQLATEE AERQRLETLC QPSEYNKWKF
     INSPTFLEVL EEFPSLRVSA GFLLSQLPIL KPRYYSISSS RDRTPTEVHL TVAVLTYRTR
     DGQGPLHHGV CSTWLSSLKP QDPVPCFVRS ASNFQLPEDP SHPCILIGPG TGIAPFRGFW
     QQRLHDTKYK GLQAGRMTLV FGCRRPDEDH LYREEMLEMA QNGVLHEVHT AYSRLPCQPK
     VYVQDILRQR LASEVLRVLH EEHGHLYVCG DVRMARDVAH TLKLLVAAKL RLSEEQVEDY
     FFQLKSQKRY HEDIFGAVFP YEVKKDGAAK QPSDPKVTTA YGRS
//
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