ID   NOS1_SHEEP              Reviewed;        1463 AA.
AC   Q29498; P79210; W5P268;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2023, sequence version 3.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Nitric oxide synthase 1 {ECO:0000305};
DE            EC=1.14.13.39 {ECO:0000250|UniProtKB:P29476};
DE   AltName: Full=Constitutive NOS;
DE   AltName: Full=NC-NOS;
DE   AltName: Full=NOS type I;
DE   AltName: Full=Neuronal NOS;
DE            Short=N-NOS;
DE            Short=NNOS;
DE   AltName: Full=Nitric oxide synthase, brain {ECO:0000305};
DE            Short=bNOS {ECO:0000305};
DE   AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1;
GN   Name=NOS1;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel;
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-121.
RA   Mimmack M.L.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1020-1132.
RC   TISSUE=Neuron;
RA   Aguan K., Weiner C.P.;
RT   "Effect of hypoxia on the expression pattern of neuronal nitric oxide
RT   synthase gene in the sheep fetal brain microvasculature.";
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC       diverse functions throughout the body. In the brain and peripheral
CC       nervous system, NO displays many properties of a neurotransmitter.
CC       Probably has nitrosylase activity and mediates cysteine S-nitrosylation
CC       of cytoplasmic target proteins such SRR (By similarity).
CC       {ECO:0000250|UniProtKB:P29476}.
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:0000250|UniProtKB:P29476};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC         Evidence={ECO:0000250|UniProtKB:P29476};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P29475};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P29476};
CC       Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P29476};
CC       Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P29476};
CC   -!- COFACTOR:
CC       Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC         Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:P29475};
CC       Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC       enzyme. {ECO:0000250|UniProtKB:P29475};
CC   -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin. Inhibited by
CC       DYNLL1 that prevents the dimerization of the protein. Inhibited by
CC       NOSIP. {ECO:0000250|UniProtKB:P29476}.
CC   -!- SUBUNIT: Homodimer. Interacts with DLG4; the interaction possibly being
CC       prevented by the association between NOS1 and CAPON. Forms a ternary
CC       complex with CAPON and RASD1. Forms a ternary complex with CAPON and
CC       SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair
CC       its synaptic location (By similarity). Interacts with HTR4 (By
CC       similarity). Interacts with SLC6A4. Interacts with VAC14 (By
CC       similarity). Interacts (via N-terminal domain) with DLG4 (via N-
CC       terminal tandem pair of PDZ domains). Interacts with SLC6A4. Forms a
CC       complex with ASL, ASS1 and SLC7A1; the complex regulates cell-
CC       autonomous L-arginine synthesis and citrulline recycling while
CC       channeling extracellular L-arginine to nitric oxide synthesis pathway
CC       (By similarity). Interacts with DMD; localizes NOS1 to sarcolemma in
CC       muscle cells (By similarity). Interacts with DYNLL1; inhibits the
CC       nitric oxide synthase activity (By similarity).
CC       {ECO:0000250|UniProtKB:P29476, ECO:0000250|UniProtKB:Q9Z0J4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000250|UniProtKB:Q9Z0J4}; Peripheral membrane protein
CC       {ECO:0000255}. Cell projection, dendritic spine
CC       {ECO:0000250|UniProtKB:P29476}. Note=In skeletal muscle, it is
CC       localized beneath the sarcolemma of fast-twitch muscle fiber by
CC       associating with the dystrophin glycoprotein complex (By similarity).
CC       In neurons, enriched in dendritic spines (By similarity).
CC       {ECO:0000250|UniProtKB:P29476, ECO:0000250|UniProtKB:Q9Z0J4}.
CC   -!- DOMAIN: The PDZ domain participates in protein-protein interaction, and
CC       is responsible for targeting nNos to synaptic membranes. Mediates
CC       interaction with VAC14. {ECO:0000250|UniProtKB:P29476}.
CC   -!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and
CC       Hsp40 (in vitro). {ECO:0000250|UniProtKB:P29476}.
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR   EMBL; AMGL01039383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01039384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X99042; CAA67503.1; -; Genomic_DNA.
DR   EMBL; U76739; AAB40706.1; -; mRNA.
DR   AlphaFoldDB; Q29498; -.
DR   SMR; Q29498; -.
DR   STRING; 9940.ENSOARP00000004517; -.
DR   PaxDb; 9940-ENSOARP00000004517; -.
DR   Ensembl; ENSOART00000004598.1; ENSOARP00000004517.1; ENSOARG00000004210.1.
DR   eggNOG; KOG1158; Eukaryota.
DR   OMA; KCPEPLR; -.
DR   Proteomes; UP000002356; Chromosome 17.
DR   Bgee; ENSOARG00000004210; Expressed in major salivary gland and 26 other cell types or tissues.
DR   ExpressionAtlas; Q29498; baseline.
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; ISS:UniProtKB.
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; 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   2: Evidence at transcript level;
KW   Calmodulin-binding; Cell membrane; Cell projection; FAD; Flavoprotein; FMN;
KW   Heme; Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Synapse; Ubl conjugation.
FT   CHAIN           1..1463
FT                   /note="Nitric oxide synthase 1"
FT                   /id="PRO_0000170925"
FT   DOMAIN          17..99
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          755..969
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          1024..1271
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          1..200
FT                   /note="Interaction with NOSIP"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   REGION          110..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..240
FT                   /note="DYNLL1/PIN/nNOS-inhibiting protein-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   REGION          215..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..745
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   COMPBIAS        229..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         334
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         415
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:P29475"
FT   BINDING         478
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         587
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         588
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         592
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         677
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         678
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         691
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         706
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         761
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         762
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         763
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         765
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         766
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         807
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         808
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         812
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         920
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         925
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         927
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         953
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         957
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1044
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1066
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1207
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1208
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1209
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1210
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1227
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1230
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1231
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1244
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1245
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1246
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1285
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1318
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1347
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1348
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1354
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1356
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1358
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1391
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1432
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1434
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   MOD_RES         881
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   MOD_RES         891
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z0J4"
FT   MOD_RES         892
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   CONFLICT        84
FT                   /note="L -> F (in Ref. 2; CAA67503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="R -> H (in Ref. 2; CAA67503)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1463 AA;  164011 MW;  D781502A207161A1 CRC64;
     MESHMFSVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA
     GDIILAVNGQ PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI
     RVTRPGRVTP PPDAPAGREQ PRAVDGAPGP GNGPQHAPDP GQEASSLAQA NGLAARPPGQ
     DPAKKSTGVA LQGSGENNKL LKEIEPVLNL LTSGGKAING GGPAKTETKD VEVQVDRDPD
     SKSHKPLPLG VENDRVFNDL WGKGNMPVVL NNPYSEKEQP SASGKQSPTK NGSPSKCPRF
     LKVKNWETDV VLSDTLHLKS TLGTGCTEHI CMGSVMLPSQ QIRKPEDVRT KEQLFPLAKE
     FIDQYYSSIK RFGSKAHMER LEEVNKEIET TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ
     WSKLQVFDAR DCTTAHGMFN YICNHIKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI
     RYAGYKQPDG SILGDPANVE FTEICIQQGW KPPRSRFDVL PLLLQANGND PELFQIPPEL
     VLEVPIRHPK FEWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD
     SSRYNILEDV AKKMNLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK
     HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN
     GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA
     FDAKVMSMEE YDIVHLEHET LVLVVTSTFG NGDPPENGEK FGCALMEMRN PNSVHEERKY
     PEPLRFFPRK GPPLSRGDTE VHGLAAVRDS QLRSYKVRFN SVSSYSDSRK SSGDGPDLRD
     NFESTGPLAN VRFSVFGLGS RAYPHFCAFG HAVDTLLEEL GGERILKMRE GDELCGQEEA
     FRTWAKKVFK AACDVFCVGD DVNIEKANNS LISNDRSWKR NKFRLTYVAE APELTQGLSN
     VHKKRVSAAR LLSRQNLQSP KSSRSTIFVR LHTNGNQELQ YQPGDHLGVF PGNHEDLVNA
     LIERLEDAPP ANQLVKVELL EERNTALGVI SNWTDEHRLP PCTIFQAFKY YLDITTPPTP
     LQLQQFASLA TSEKERQRLL VLSKGLQEYE EWKWGKNPTI VEVLEEFPSI QMPSTLLLTQ
     LSLLQPRYYS ISSSPDMYPD EVHLTVAIVS YRTRDGEGPI HHGVCSSWLN RIQADEVVPC
     FVRGAPSFHL PQNPQVPCIL VGPGTGIAPF RSFWQQRQFD IQHKGMSPCP MVLVFGCRQS
     KIDHIYREEA LQAKSKGVFR ELYTAYSREP DKPKKYVQDI LQEQLAEPVY RALKEQGGHI
     YVCGDVTMAA DVLKAIQRIM TQKGKLSVED AGVFISRLRD DNRYHEDIFG VTLRTYEVTN
     RLRSESIAFI EESKKDTDEV FSS
//