NOS_LYMST
ID NOS_LYMST Reviewed; 1153 AA.
AC O61309;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Nitric oxide synthase;
DE EC=1.14.13.39;
DE AltName: Full=NOS type I;
DE AltName: Full=Neuronal NOS;
DE Short=N-NOS;
DE Short=nNOS;
GN Name=NOS;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=CNS;
RX PubMed=9552167;
RX DOI=10.1002/(sici)1097-4695(199804)35:1<65::aid-neu6>3.0.co;2-9;
RA Korneev S.A., Piper M.R., Picot J., Phillips R., Korneeva E.I., O'Shea M.;
RT "Molecular characterization of NOS in a mollusc: expression in a giant
RT modulatory neuron.";
RL J. Neurobiol. 35:65-76(1998).
CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC diverse functions throughout the body. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O61309-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O61309-2; Sequence=VSP_003584;
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system, in the
CC serotonergic cerebral giant cells. The isoform Long and isoform Short
CC are expressed equally in the CNS.
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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; AF012531; AAC17487.1; -; mRNA.
DR PIR; T31080; T31080.
DR AlphaFoldDB; O61309; -.
DR SMR; O61309; -.
DR PRIDE; O61309; -.
DR BRENDA; 1.14.13.39; 3112.
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 Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.1230.10; -; 1.
DR Gene3D; 3.90.340.10; -; 1.
DR Gene3D; 3.90.440.10; -; 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 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; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 2.
DR SUPFAM; SSF56512; SSF56512; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS60001; NOS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calmodulin-binding; FAD; Flavoprotein; FMN; Heme;
KW Iron; Metal-binding; NADP; Oxidoreductase; Repeat.
FT CHAIN 1..1153
FT /note="Nitric oxide synthase"
FT /id="PRO_0000170949"
FT DOMAIN 427..610
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 660..903
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REPEAT 934..940
FT /note="1"
FT REPEAT 941..947
FT /note="2"
FT REPEAT 948..954
FT /note="3"
FT REPEAT 955..961
FT /note="4"
FT REPEAT 962..968
FT /note="5"
FT REPEAT 969..975
FT /note="6"
FT REPEAT 976..982
FT /note="7"
FT REPEAT 983..989
FT /note="8"
FT REPEAT 990..996
FT /note="9"
FT REPEAT 997..1003
FT /note="10"
FT REPEAT 1004..1010
FT /note="11"
FT REGION 397..417
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 934..1010
FT /note="11 X 7 AA tandem repeats of E-[NTR]-[ST]-[IM]-[PLQ]-
FT [SP]-[CW]"
FT BINDING 3
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 82
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:0000250|UniProtKB:P29474"
FT BINDING 145
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 254
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 264
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 358
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 556..587
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 697..708
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 836..846
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 911..929
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 1089..1104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT VAR_SEQ 276..309
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9552167"
FT /id="VSP_003584"
SQ SEQUENCE 1153 AA; 129086 MW; 101B77D02B66B109 CRC64;
MGSLSQQAHG PPDAPRSKEE LLIHAKDFIN QYFTSFQMNK TRAHFHRLGE INDLIEKSGT
YDLTMAELTF GAKHAWRNAP GCIGRSQWSK LQVFDAREIG TPREMFEALC SHIRYATNEG
KIRSTITIFP QRKEGRPDFR VWNTQLISYA GYKLGDGKVI GDPANVEFTE MCVEMGWKPK
HGMFDLLPLV LSAAENSPEY FELPTELVLE VTLKHPEYPW FAEMGLKWYA LPTDSGMLLD
CGGLEFPSCP FNGWFMGTMI GSRNLCDPHR YNMLEPIGLK MGLNTETASS LWKDRVLIEV
NVAVLYSFES ANVTIVNHHD ASTDFISHMD KEIKLRGGCP SDWVRMVPPM SGSTLEVFHQ
EMLLYNLHPA FVRQDVKPWK KHVWKSDQSV PINSCNPKRK LGFKALARAV EFSASLMSKA
LSSRVKCSIF YATETGRSER FARRLSEIFK PVFHSRVVCM DDYAVETLEH ESLVMVITST
FGNGEPPENG KQFAQSLLDM KRKYDCDLGF LESCSSISTC IKSSILTEGP LAADVIGDRQ
SLAMGTGPLC NVRFAVFGLG SKAYPYYAAY GKYIYLMLQE LGAERLVNYC AGDALYGQEQ
SFRAWSEEVF KASCEAFCLD NRNDAPGPQT KGDCSKVRIV PVENCQEPDL CQVLRNIHGK
EVMPLILAER IQLQAKDSDQ QTILIKLDAH NATDLKYAPG DHVAIFPANS PEIVDAILVR
LDTSKGPSPD QVVKTEISTQ LGTNDTWRSH LPICTSRTAF SFLLDVTTPP SQEILQVLAT
QASSDMDKHK LEQLASNSEA YEKWRLDLSP NILEILDEFP SLKIPPSLLL TQLPLLQPRY
YSISSSQQKN PNEVHATIAV VRFKTQDGDG PVHEGVCSSW LNRSPIGTVV PCFLRSAPHF
HLPEDPSLPI IMIGPGSGIA PFRSFWQQRL GEIENTMPSC ENTMLSCETT IPSCENSMPS
CENTMPSCEN TMPSCENTIP SCENTIPSCE NTMPSCENTI PSWERTMQPC QIILPSQTKK
HFGEMVLYTG CRTAKHMIYA AELEEMKRLG VLSNYHVALS REAALPKMYV QDIIIKNAAA
VYEIVMKKGG HFYVSGDVSM AHDVTRALEL VLCQQGGREA SQQVMSLRDE NLFHEDIFGS
FVRKAGGQRS EDE
