ID M7ANS9_CHEMY Unreviewed; 1443 AA.
AC M7ANS9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 ORFNames=UY3_18643 {ECO:0000313|EMBL:EMP24405.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP24405.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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|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; KB601989; EMP24405.1; -; Genomic_DNA.
DR STRING; 8469.M7ANS9; -.
DR eggNOG; KOG1158; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
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; 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 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 17..99
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 773..953
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1008..1255
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 141..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 433
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 1443 AA; 162643 MW; 6E42CE7D08131FC2 CRC64;
MEENVFSVQQ IQPNVISVRL FKRKVGGLGF LVKERVNKPP VIISDLIRGG AAEQSGLIQA
GDIILAVNGR PLVDMSYESA LEILRSIASE TYVVLILRGP EGFTTHLETT FAGDGLPKTV
RVTRPLCPTA KAVDLSNPSI HSRDLQQGAD HTMGSASSAW ARENRKEAES LVHVNGVVTS
TKGEDGKGRD NAGANPCLNG GVENNELLKE IEPVLKLLKS GSKELNGDAP TKVETRDIEV
QVDWEVDKSQ KPAPAGMEND RVFNDLWGKS DTPIVLNNPY LEKEQPPPSG RQSPTKNLVN
GSPSKCPRFA KVKNWETGSV LHDTLQLKTA MASACTEQIC MGSIMTPTQH VRKPEDTRTK
EQLLPLAKDF IDQYYSSIKR QVFWHSRVVF GSKAHMERLE EVTKEIETTD TYQLRDTELI
YGAKHGWRNA SRCVGRIQWS KLQVFDARDC TTAHGMFNYI CNHIKYATNK GNLRSAITIF
PQRMDGKHDF RVWNAQLIRY AGYKQPDGTI LGDPANVELT EICIQQGWKA PKGRFDVLPL
LLQANGNDPE LFEIPPELVL EVPIRHPKFA WFKDLGLKWY GLPAVSNMLL EIGGLEFTAC
PFSGWYMGTE IGVRDYCDNS RYNMLEEVAK KMNLDMRKTS SLWKDQALVE INIAVLYSFQ
SDKVTIVDHH SATESFIKHM ENEYRCRGGC PADWVWIVPP MSSSITPVFH QEMLNYRLTP
SFEYQPDPWN THIWKGVNGT PTKKRAIGFK KLAKAVKFSA KLMGQAMAKR VKATILYATE
TGKSQVYAKT LCEIFKHAFD AKVMSMDEYD IVHLEHETLV LVVTSTFGNG DPPENGEKFG
CAMMEMRNPN SHLEERKSYK VRFNSVSSYS DARKSSSDGP EARDNFESTG PLANVRFSVF
GLGSRAYPHF CAFARAVDTL LEELGGERIL RMGEGDELCG QEESFRTWAK KVFKAACDVF
CVGDDVNIEK ANNSLISNDR SWKRSKFRLT YVAEAPELTQ GLYSIHKKRV YAARLLTRQN
LQSPKSSRST IFLRLHTNGQ QELRYQPGDH LGVFPGNHED LVSALMERLE DAPPANQLVK
VELLEERSTA LGVISNWTDE NRIPPCTIFQ AFKCYLDITT PPTPLLLQQF ALLATSDKEK
KRLQVLSKGL QEYEEWKWSK NPTVVEVLEE FPSVQMPSTL LLTQLPVLQP RYYSISSSPD
MSPDEVHLTV AVLSYRTRDG EGPIHHGVCS SWFNRIQADE VVPCFVRGAP GFHMPQDPQV
PCILIGPGTG IAPFRSFWQQ RLFEIEHKAL KPCPMILVFG CRQSKIDHIY KEETLLAKNK
GIFKELYTAY SREPDKPKKY VQDVLQEQLA QSVYKALKEQ GGHIYVCGDV TMAGDVFKAV
QRIVKQQGQL SVEQAGAFIS KLRDDNRYHE DIFGVTLRTY EVTNRLRSES IAFIEESKKD
TDE
//
