ID C4TP54_9EUPU Unreviewed; 1616 AA.
AC C4TP54;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 71.
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=limNOS2 {ECO:0000313|EMBL:BAH70357.1};
OS Ambigolimax valentianus.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC Helicina; Limacoidea; Limacidae; Ambigolimax.
OX NCBI_TaxID=1338344 {ECO:0000313|EMBL:BAH70357.1};
RN [1] {ECO:0000313|EMBL:BAH70357.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19560441; DOI=10.1016/j.bbrc.2009.06.112;
RA Matsuo R., Ito E.;
RT "A novel nitric oxide synthase expressed specifically in the olfactory
RT center.";
RL Biochem. Biophys. Res. Commun. 386:724-728(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB506804; BAH70357.1; -; mRNA.
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:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 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 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 2: Evidence at transcript level;
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}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 16..98
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 919..1101
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1157..1404
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 158..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1616 AA; 178612 MW; 6D1868F26AB0EC92 CRC64;
MPSTTSSSEL PPNTIRVKLI KQKHAGLGFL VKQRTLKPFV LVASIVKGGV AEESGLVQIG
DIILRINDVD LTDMSYPSAI EVLKAVPIDT PVVLLLRGPE GYTTYLQTTF MENGVPRTVR
VTKVLHDSIM GRIKKTFSGS SGQISPVKGL KRLCNGELDG RNKKGEDDIT DKDADSTGGG
DDNTNVVSVE ELADPPSRQP IRPESGGQDK KPALNGEAVT GVASPLSGEA SKFLFRNEGR
VDSEEETVLD NGTVGSPKIV LTSPKSKDGS KPGPMPRAQT FDSGVGDSCR SPCQKKSIEI
IQTDDVITVV VKGDLTVHSE DTSSTDPNTP KKFIISSTKH SQPPLSSSTN LRHEPIDFPA
HAETAFNPPN SSLSRNSSRK KSGRASPNTC GRVSPGGGRG GRSPATSPTK HPKSSDTNDE
DNGRVGRGSE KRRATSPALG RRKSTDRRGS VASTGMTSPK RFVRVKNMLD DKTYRTLYTR
RSSRQFLVTQ TGAWVPSCPC SSSAPGNTRT TEDLLIHAKD FIDQYYTSIK RNNTQSHHNR
WTEIQESVDQ HGTYDLTSAE LNFGAKQAWR NAPRCIGRIQ WSKLQVFDAR HILTARSMFE
ALCNHIKYGT NKGSLRSAIT IFPHRKANRR DFGVWNAQLI RYAGYRAEDG AVTGDPANVE
FTEQCVKLGW KPRYGQFDIL PLVLSAAGSD PEWFDIPHDL VLEVNIKHPK YPWFADLGLK
WYALPAVSGM LFDCGGLEFP ACPFNGWYMG TEIGARNFCD TSRYNMLETI ATNMGLDIMK
NASLWKDRAM VECNVAVLHS YQANGVTITD HHSASESFIK HMENEQKLRG GCPGDWVWVV
PPLGGSLLEV FHQELLLYKL KPSYEYQDEA WKTHVWKKDR EKLATVAKTK RKIGFKELAR
AVKFSAKLMG KASARRVKCV ILYATETGKS EKFANTLTAI FKHAFDAKVM CMPDYDIISL
EHESLVLVVA STFGNGDPPE NGDAFAINLF DMKSADLPPN GDHSGSRTHS SYVRLSISSD
KGEKNDANNG DSLVSIKGPL GNVRFSVFAL GSKAYPHFAA FGHYIHDVLH DLGAECIFPI
GTGDELCAQE QSFRLWAEGV FTAACETFCL GDDVNIYEAT GALNSDHSWT PNKFRLTLVD
NAKDLNICDA LTSFHGKTVV PCILSERIQL QEESSDRQTI LIKLNTQGSS ELLYVPGDHV
GVFLANPKEL VDGVLARLHN SPPPDQIVKA EYLSEVSTPL GTKKTWTQIE KMPTCSMRLA
FTQFLDLTTP PSQSLLSLLA TQATRDSDRE KLELLATDAT AYEKWRYELS PNMLEVLDQF
SSLKVLPTLL MTQLPHLLQR YYSISSSPLM FPGEVHATID VVKFRTQDGA GPIHEGVCSG
WLNRCDVGTV VPCLVRTAQS FHMPEDKSLP IIMVGPGTGI APFRSFWQER CIDLEMYRDQ
KNWGEMVLYF GCRTSTQDNI YKQELDEYSA NHVLTKFYVA LSREPNTPKV YVQDILYSRA
PEVYDAIVKK GGHFYVCGDV AMAHDVTRTL ETLLKEQGDI PLDSATIIVD GLRDANRFHE
DIFGVNVRKP GDLAELSKDR SVRALQYLNA ISKPDKPDAL KEIAVCIKST EETGDE
//
