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}.
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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
//
