ID   NOS2_CANLF              Reviewed;        1154 AA.
AC   O62699; O97604;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Nitric oxide synthase, inducible;
DE            EC=1.14.13.39 {ECO:0000250|UniProtKB:P35228};
DE   AltName: Full=Inducible NO synthase;
DE            Short=Inducible NOS;
DE            Short=iNOS;
DE   AltName: Full=NOS type II;
DE   AltName: Full=Peptidyl-cysteine S-nitrosylase NOS2;
GN   Name=NOS2;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aorta;
RX   PubMed=9746458; DOI=10.1152/ajpheart.1998.275.4.h1122;
RA   Wang X., McGregor C.G.A., Miller V.M.;
RT   "Induction and cDNA sequence of inducible nitric oxide synthase from canine
RT   aortic smooth muscle cells.";
RL   Am. J. Physiol. 275:H1122-H1129(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-632.
RC   TISSUE=Alveolar macrophage;
RA   Haerter L., Straubinger R.K., Appel M.J.G.;
RT   "The canine inducible NO synthase.";
RL   Submitted (NOV-1997) 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 macrophages, NO mediates
CC       tumoricidal and bactericidal actions. Also has nitrosylase activity and
CC       mediates cysteine S-nitrosylation of cytoplasmic target proteins such
CC       PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex
CC       involved in the selective inflammatory stimulus-dependent S-
CC       nitrosylation of GAPDH implicated in regulation of the GAIT complex
CC       activity and probably multiple targets including ANXA5, EZR, MSN and
CC       VIM. Involved in inflammation, enhances the synthesis of pro-
CC       inflammatory mediators such as IL6 and IL8.
CC       {ECO:0000250|UniProtKB:P35228, ECO:0000250|UniProtKB:P79290}.
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:P35228};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC         Evidence={ECO:0000250|UniProtKB:P35228};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P35228};
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:P35228};
CC       Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P35228};
CC   -!- COFACTOR:
CC       Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC         Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:P35228};
CC       Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC       enzyme. {ECO:0000250|UniProtKB:P35228};
CC   -!- ACTIVITY REGULATION: Regulated by calcium/calmodulin. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with NHERF1. Interacts with GAPDH;
CC       induced by oxidatively-modified low-densitity lipoprotein (LDL(ox)).
CC       Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9
CC       transnitrosylase complex. Interacts with SPSB1, SPSB2 and SPSB4.
CC       Interacts with ELOC and CUL5 in the presence of SPSB1 or SPSB2 or
CC       SPSB4. Forms a complex with ASL, ASS1 and HSP90AA1; the complex
CC       regulates cell-autonomous L-arginine synthesis and citrulline recycling
CC       while channeling extracellular L-arginine to nitric oxide synthesis
CC       pathway. {ECO:0000250|UniProtKB:P29477}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P35228}. Note=Localizes as discrete foci
CC       scattered throughout the cytosol and in the presence of SPSB1 and
CC       SPSB4, exhibits a more diffuse cytosolic localization.
CC       {ECO:0000250|UniProtKB:P35228}.
CC   -!- PTM: Polyubiquitinated; mediated by SPSB1, SPSB2 and SPSB4, leading to
CC       proteasomal degradation. {ECO:0000250|UniProtKB:P35228}.
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; AF077821; AAC78630.1; -; mRNA.
DR   EMBL; AF032909; AAC15587.1; -; mRNA.
DR   RefSeq; NP_001300777.1; NM_001313848.1.
DR   AlphaFoldDB; O62699; -.
DR   SMR; O62699; -.
DR   STRING; 9615.ENSCAFP00000027512; -.
DR   PaxDb; 9612-ENSCAFP00000027512; -.
DR   GeneID; 403822; -.
DR   KEGG; cfa:403822; -.
DR   CTD; 4843; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   InParanoid; O62699; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; ISS:UniProtKB.
DR   GO; GO:0006527; P:arginine catabolic process; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; 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:0018119; P:peptidyl-cysteine S-nitrosylation; ISS:UniProtKB.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR   GO; GO:0032310; P:prostaglandin secretion; ISS:UniProtKB.
DR   GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR   GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR   GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR   CDD; cd00795; NOS_oxygenase_euk; 1.
DR   Gene3D; 3.40.50.360; -; 2.
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; 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   PIRSF; PIRSF000333; NOS; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
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; SSF63380; Riboflavin synthase domain-like; 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   Calcium; Calmodulin-binding; Cytoplasm; FAD; Flavoprotein; FMN; Heme; Iron;
KW   Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Ubl conjugation; Zinc.
FT   CHAIN           1..1154
FT                   /note="Nitric oxide synthase, inducible"
FT                   /id="PRO_0000170927"
FT   DOMAIN          536..674
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          727..967
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          22..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..532
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   MOTIF           23..27
FT                   /note="DINNN-motif; mediates interaction with SPSB1, SPSB2
FT                   and SPSB4"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         197
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         260
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         369
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         370
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         374
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         378
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         459
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         460
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         473
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         488
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         542
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         543
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         544
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         546
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         547
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         588
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         589
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         625
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         632
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         658
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         747
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         769
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         903
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         905
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         906
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         921
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         923
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         927
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         940
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         941
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         942
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         981
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1014
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1043
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
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         1050
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1052
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1054
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1087
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   MOD_RES         572
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06518"
FT   CONFLICT        42..52
FT                   /note="DDLKNHKHHND -> KCHSLSKHRDE (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="P -> S (in Ref. 2; AAC15587)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59..64
FT                   /note="ETVQKL -> GTVKTS (in Ref. 2; AAC15587)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68..80
FT                   /note="LDKLHATPLSRPQ -> TIKPAAPPLACPR (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91..92
FT                   /note="MT -> RS (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102..104
FT                   /note="KGD -> MGV (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="K -> T (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111..115
FT                   /note="SCLGA -> LCMGS (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="P -> T (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125..127
FT                   /note="EPR -> GPS (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133..134
FT                   /note="PD -> TE (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="S -> G (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="E -> D (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        394..395
FT                   /note="RR -> SK (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497..499
FT                   /note="VWQ -> LWL (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        506..508
FT                   /note="QRR -> HRK (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        615
FT                   /note="K -> N (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624..626
FT                   /note="GSS -> RSN (in Ref. 1; AAC78630)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1154 AA;  131847 MW;  D6AD3A88AE89E995 CRC64;
     MACPWKFLFR AKFHQYGMKE EKDINNNVEK PPGATPSPST QDDLKNHKHH NDSPQPLTET
     VQKLPESLDK LHATPLSRPQ HVRIKNWGNG MTFQDTLHHK AKGDLACKSK SCLGAIMNPK
     SLTREPRDKP TPPDELLPQA IEFVNQYYSS FKEAKIEEHL ARVEAVTKEI ETTGTYQLTG
     DELIFATKQA WRNAPRCIGR IQWSNLQVFD ARSCSTAKEM FEHICRHLRY ASNNGNIRSA
     ITVFPQRTDG KHDFRVWNAQ LIRYAGYQMP DGTILGDPAS VEFTQLCIDL GWKPKYGRFD
     VVPLVLQADG QDPEFFEIPP DLVLEVPMEH PKYEWFRELE LKWYALPAVA NMLLEVGGLE
     FPGCPFNGWY MGTEIGVRDF CDVQRYNILE EVGRRMGLET HKLASLWKDR AVIEINVAVL
     HSFQKQNVTI MDHHSAAESF MKYMQSEYRS RGGCPADWIW LVPPISGSIT PVFHQEMLNY
     VLSPFYYYQV EAWKTHVWQD EKRRPQRRKI QLKVLVKAVL FASMLMRKTM ASRVRVTILF
     ATETGKSETL ARDLGALFSC AFHPKVLCMD EYKLSHLEEE QLLLVVTSTF GNGDSPGNGE
     KLKKSLFMLK ELTNKFRYAV FGLGSSMYPQ FCAFAHDIDH KLSHLGASQL TPGGEGDELN
     GKEEAFRCWA VQTFKAACDT SDVRGKHCIQ IPRLYTSNVT WDPHHYRLLQ DSQPLDLNKA
     LSKMHAKNVF TLRLKSQRNL QSPISNRTTL QVELSCEDSQ ELSYLPGEHL GVFPGNQLAL
     VQGILERVVY SPAPLQPVHL ETLSERGSYW VRNNRLPPCS LSQALTYFLD ITTPPTHLLL
     RKLAQLAHQY AERHRLEILC HPSEYNKWKL TNSPTFLEVL EEFPSLRVSA GFLLSQLPIL
     KPRYYSISSS RDCTPMEVHL TVAVLVYPTR DGQGPLHHGV CSTWLSNLKP QDPVPCFVRS
     AGNFKLPEDP SRPCILIGPG TGIAPFRSFW QQRLHDIKHK GLRGSRMTLV FGCRRPDEDH
     LYREEMLEMA QSGVLHEVHT AYSRLPGQPK VYVQDILRQQ LASQVLRMLH EEQGHLYVCG
     DVRMARDVAH TLKHLVAAKL SLSEEQVEDY FFQLKSQKRY HEDIFGAVFP YEVKKDGAAK
     QPSDPRVPAA HGRS
//