ID C3YCN5_BRAFL Unreviewed; 1441 AA.
AC C3YCN5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Nitric oxide synthase 1 {ECO:0000256|ARBA:ARBA00035211};
DE EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
DE AltName: Full=Constitutive NOS {ECO:0000256|ARBA:ARBA00029794};
DE AltName: Full=NC-NOS {ECO:0000256|ARBA:ARBA00031302};
DE AltName: Full=NOS type I {ECO:0000256|ARBA:ARBA00029891};
DE AltName: Full=Neuronal NOS {ECO:0000256|ARBA:ARBA00031374};
DE AltName: Full=Nitric oxide synthase, brain {ECO:0000256|ARBA:ARBA00035474};
DE AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1 {ECO:0000256|ARBA:ARBA00032538};
GN Name=NosC {ECO:0000313|EMBL:EEN61836.1};
GN ORFNames=BRAFLDRAFT_290770 {ECO:0000313|EMBL:EEN61836.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|EMBL:EEN61836.1};
RN [1] {ECO:0000313|EMBL:EEN61836.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN61836.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN61836.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004468}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004468}. Cell projection, dendritic spine
CC {ECO:0000256|ARBA:ARBA00004552}.
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267}.
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DR EMBL; GG666502; EEN61836.1; -; Genomic_DNA.
DR RefSeq; XP_002605826.1; XM_002605780.1.
DR STRING; 7739.C3YCN5; -.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; C3YCN5; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006527; P:arginine catabolic process; IBA:GO_Central.
DR GO; GO:0045776; P:negative regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR CDD; cd06202; Nitric_oxide_synthase; 1.
DR CDD; cd00795; NOS_oxygenase_euk; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 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; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
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 Pfam; PF00595; PDZ; 1.
DR PIRSF; PIRSF000333; NOS; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM00228; PDZ; 1.
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; SSF50156; PDZ domain-like; 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.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000333-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000333-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000333-1}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 9..78
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 722..908
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 965..1212
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 156..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378
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 1441 AA; 161189 MW; BE62DA23ED86CE4E CRC64;
MEIRPNVIAV KLMKREGDGL GFLVKQRSCN PPVIVSDVVR GGAADQSGLI QVGDLILSVN
GTSLETVSYS DALQVLRSVE VGKPTEIILR GPEGFATKLE TTFTGTGIPK TVRITTAESP
LRSLALSPAR RLIKRITGNS HVKSIDHINA EALKEKETVS NGPLCTDHTD QKMETPKSCS
SIAVQTSPEE PATKDVNGQC NGNGTVEKLD KTKLTLDTLS IALKRESVNG NELGRPTEDG
PSSRRNSTTL SPSAKPRYAR MKNWLNDKQM TDTLHNKGTP VNPCSGTKCL GSLMRPNAAA
LAKSGRPAGE VRPKEEVLEH AKEFLDEFFA SIKRANTQAH KQRWAEAKAQ IEEKGWYELT
QMELTYGAKL AWRNAPRCVG RIQWSKLQVF DARYVTTARG MYEAICNHIK YTTNKGNLRS
AITIFPARTD GKHDFKVWNS QFVRYAGYKQ PDGSIVGDPA SVEFTEICQS LGWKGKNGPF
DVLPLVLSAN GQDPELFELS KDLVLEVELK HPKYGWFKEL GMKWYALPAV ANMLFDVGGV
EFPAAPFSGW YMCTEIGRDL CDINRYNFTE QIAKRMGLDT GRASSLWRDL ALIEANVAIL
HSFQTCNVTI TDHHTACESF MKHMENEQRL RGGCPADWVW IVPPISGSLT PVFHQEMISY
YLRPSYEYQE DAWMTHVWKK KEDTKKIMPG KAKRKFGFKE VAKAVKFSAK LMGKALAKRV
KATILYATET GKSERYAKTI CEIFKHAFDA KVMCMDDYDI MHLEHETLVI VVTSTFGNGD
PPDNGESFGQ TLLEMRHPPM DNNDNRPPGH TKRLSSISSS ATERRRKFSH QMKERDMESM
DLDGGPLGNV RFSVFGLGSR AYPGFCAFAH AVDTLFGELG GERIYKMGEG DELCGQEESF
RKWAKGVFKA ACDTFCVGDE LNMSEASATL LNSDTTWAAD KFRLIPAEGV KEWDIWEGLS
KVHSRNVVPC RLISRENLQA PDSGRETILV RLDSQGSDDL NYVPGDHLAV YPANEDHLVQ
AVLDRLDNAP DPDCIVNMEV LQEKQTPLGA IRSWMTSERL PPCSLRTALS RYFDITTPPS
PQLLQHLATQ ATDEEEKKEL EVLGKGDSRY EDWKFERTPN LVEVLEDYPS LKVAPTLLLS
QLPFLQQRYY SISSSQLMYP GEIHATVAVV KFATQGGVGP IHNGVCSSWL NRIEKDDIVP
CFVRAAQSFH LPEDPTVPLM MVGPGTGIAP FRSFWQHRQM EVTSGDPHHR PKFGQMTLVF
GCRQSKMDDI YKHETAQAKE DGALTEVYTA LSREPGVPKS YVQNVILDLI PEKVCDLLMN
HNGHFYVCGD VSMAADVCNT LEKVMEKQQG MAPNRAKDFV DKLKDCNRYH EDIFGVTLRT
QEVTDRVRSA ARKNWMRVKR LRPSTVVPPT RGLSPVREVG ENTLIIWLLF STAGLRLLLF
I
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