ID   NOS2_PIG                Reviewed;        1157 AA.
AC   P79290; A0A287AUH8; A0A287BRU8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2023, sequence version 2.
DT   27-MAR-2024, entry version 133.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc;
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   PubMed=9613441; DOI=10.1016/s0165-2427(97)00139-6;
RA   Pampusch M.S., Bennaars A.M., Harsch S., Murtaugh M.P.;
RT   "Inducible nitric oxide synthase expression in porcine immune cells.";
RL   Vet. Immunol. Immunopathol. 61:279-289(1998).
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:P29477, ECO:0000250|UniProtKB:P35228}.
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: Not stimulated by calcium/calmodulin.
CC       {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   -!- TISSUE SPECIFICITY: Detected in both stimulated and unstimulated immune
CC       cells and macrophages with little or no up-regulation following
CC       cellular stimulation with lipopolysaccharides (LPS) or concanavalin A
CC       (ConA).
CC   -!- INDUCTION: Little by LPS or ConA in spleen cells.
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}.
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DR   EMBL; DQIR01039684; HCZ95159.1; -; Transcribed_RNA.
DR   EMBL; DQIR01166906; HDB22383.1; -; Transcribed_RNA.
DR   EMBL; DQIR01261531; HDC17009.1; -; Transcribed_RNA.
DR   EMBL; U59390; AAB40614.1; -; mRNA.
DR   RefSeq; XP_005669136.1; XM_005669079.2.
DR   RefSeq; XP_013836620.1; XM_013981166.1.
DR   RefSeq; XP_013836621.1; XM_013981167.1.
DR   RefSeq; XP_013836622.1; XM_013981168.1.
DR   AlphaFoldDB; P79290; -.
DR   STRING; 9823.ENSSSCP00000058904; -.
DR   PaxDb; 9823-ENSSSCP00000018812; -.
DR   Ensembl; ENSSSCT00000055475.3; ENSSSCP00000058904.2; ENSSSCG00000017755.5.
DR   GeneID; 396859; -.
DR   CTD; 4843; -.
DR   VGNC; VGNC:99024; NOS2.
DR   eggNOG; KOG1158; Eukaryota.
DR   GeneTree; ENSGT00940000159752; -.
DR   InParanoid; P79290; -.
DR   OMA; CRHIRYA; -.
DR   OrthoDB; 276396at2759; -.
DR   Reactome; R-SSC-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-SSC-392154; Nitric oxide stimulates guanylate cyclase.
DR   Reactome; R-SSC-9033241; Peroxisomal protein import.
DR   Proteomes; UP000008227; Chromosome 12.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000017755; Expressed in caecum and 31 other cell types or tissues.
DR   ExpressionAtlas; P79290; baseline and differential.
DR   GO; GO:0005829; C:cytosol; 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   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   CDD; cd00795; NOS_oxygenase_euk; 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; 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   Calmodulin-binding; Cytoplasm; FAD; Flavoprotein; FMN; Heme; Iron;
KW   Metal-binding; NADP; Oxidoreductase; Reference proteome; Ubl conjugation;
KW   Zinc.
FT   CHAIN           1..1157
FT                   /note="Nitric oxide synthase, inducible"
FT                   /id="PRO_0000170935"
FT   DOMAIN          539..677
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          730..970
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          29..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..535
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   REGION          1138..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           23..27
FT                   /note="DINNN-motif; mediates interaction with SPSB1, SPSB2
FT                   and SPSB4"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   COMPBIAS        29..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110
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         115
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         200
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:P35228"
FT   BINDING         263
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         372
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         373
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         377
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         381
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         462
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         463
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         476
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         491
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         545
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         549
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         550
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         591
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         592
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         628
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         635
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         661
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         665
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         750
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         772
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         908
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         909
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         924
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         926
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         929
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         930
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         943
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         944
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         945
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         984
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1017
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1046
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1047
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1053
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1055
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1057
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1090
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
SQ   SEQUENCE   1157 AA;  131313 MW;  C0A0D67FBA90686B CRC64;
     MACPWKFLFK AKSSRFDLTE EKDINNNLEK LRQASSSPVT QDDPKCPSRS RHRNECSQPL
     AETAKKSPDS LVKLDVLPPA CPRHVRIKNW GSGMTFQDTL HREAKGDLAC KSKSCLGAIM
     NPKSLTIGPR DKPTPPDELL PQAIEFVNLY YSSFKEAKIE EHLARVEAVT KEIETTGTYQ
     LTGDELIFAA KQAWRNAPRC IGRIQWSNLQ VFDARSCSTA QEMFEHICRH LRYATNNGNI
     RSAITVFPQR SDGKHDFRVW NAQLIRYAGY QMPDGTIIGD PASVEFTQLC IDLGWKPKYG
     RFDVVPLVLQ ADGRDPELFE IPPDLVLEVP MEHPKYEWFQ ELELKWYALP AVANMLLEVG
     GLEFPGCPFN GWYMGTEIGV RDFCDVQRYN ILEEVGRRMG LETHKLASLW KDRAVVEINV
     AVLHSFQKQN VTIMDHHSAA ESFMKYMQNE YRSRGGCPAD WIWLVPPISG SITPVFHQEM
     LNYVLSPFYY YQVEAWKTHV WQDEKRRPRR KEIRFKVLVK AVLFAAVLMH KTMAARVRAT
     ILFATETGRS ETLARDLGAL FSCAFNPKVL CMDEYRLSRL EEEQLLLVVT STFGNGGSPG
     NGEKLKKSLF MLKELTNKFR YAVFGLGSSM YPQFCAFAHD VDQKLSHLGA SQLTPTGEGD
     ELSGQEEAFR GWAVQTFKVA CETFDVRGKH HIQIPKLYTS NVTWDPQLYR LVQDSEPLDL
     NKALSSMHAK YVFSMRLKSQ QNLQSPQSSR TTLLVELCCE GSQGPSYLPG EHLGVFPANQ
     PALVQGILER VVDGPAPHQP VRLETLSENG SYWVKDKRLP PCSLSQALTY FLDITTPPTQ
     LLLRKLAQLA TDEAERQRLE TLCQPSDYNK WKFTNSPTFL EVLEEFPSLR VSASFLLSQL
     PILKPRYYSI SSSRDRTPTE IHLTVAVLTY RTRDGQGPLH HGVCSTWLSS LKPQDLVPCF
     VRSASGFQLP EDPSRPCILI GPGTGIAPFR SFWQQRLHEA EHKGLQGGRM TLVFGCRRPD
     EDHLYQEEML EMARKGVLHE VHTAYSRLPG QPKVYVQDLL RQRLAGEVLR VLHEEQGHLY
     VCGDVRMARD VACTLKQLVA TALTLNEEQV EDYFFQLKSQ KRYHEDIFGA VFPYEVKKEG
     AVGPPSDPRA PGAHGKS
//