ID NOS2_BOVIN Reviewed; 1156 AA.
AC Q27995; Q06Q84; Q27985;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 08-NOV-2023, entry version 159.
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 Short=NOSII;
DE AltName: Full=Peptidyl-cysteine S-nitrosylase NOS2;
GN Name=NOS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Widdison S., Ashley G.R., Howard C.J., Coffey T.J.;
RT "Cloning and characterization of bovine inducible nitric oxide synthase.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-275.
RC TISSUE=Bone marrow macrophage;
RX PubMed=7536776;
RA Adler H., Frech B., Thoeny M., Pfister H., Peterhans E., Jungi T.W.;
RT "Inducible nitric oxide synthase in cattle. Differential cytokine
RT regulation of nitric oxide synthase in bovine and murine macrophages.";
RL J. Immunol. 154:4710-4718(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 987-1122.
RC TISSUE=Pulmonary artery;
RX PubMed=7558036; DOI=10.1006/geno.1995.1086;
RA Bloch K.D., Wolfram J.R., Brown D.M., Roberts J.D. Jr., Zapol D.G.,
RA Lepore J.J., Filippov G., Thomas J.E., Jacob H.J., Bloch D.B.;
RT "Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B,
RT and NOS2C) colocalize to human chromosome 17.";
RL Genomics 27:526-530(1995).
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; DQ676956; ABG74910.1; -; mRNA.
DR EMBL; U14640; AAC48470.2; -; mRNA.
DR EMBL; U18331; AAC48479.1; -; mRNA.
DR PIR; I46074; I46074.
DR RefSeq; NP_001070267.1; NM_001076799.1.
DR AlphaFoldDB; Q27995; -.
DR SMR; Q27995; -.
DR STRING; 9913.ENSBTAP00000009062; -.
DR PaxDb; 9913-ENSBTAP00000009062; -.
DR GeneID; 282876; -.
DR KEGG; bta:282876; -.
DR CTD; 4843; -.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; Q27995; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000009136; 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; IBA:GO_Central.
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 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..1156
FT /note="Nitric oxide synthase, inducible"
FT /id="PRO_0000170926"
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 27..84
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 MOTIF 23..27
FT /note="DINNN-motif; mediates interaction with SPSB1, SPSB2
FT and SPSB4"
FT /evidence="ECO:0000250|UniProtKB:P35228"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Polar 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 118
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
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:P29474"
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:P29474"
FT BINDING 476
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 491
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P29474"
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"
FT MOD_RES 575
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q06518"
FT CONFLICT 236
FT /note="N -> S (in Ref. 2; AAC48470)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068..1069
FT /note="VL -> AF (in Ref. 3; AAC48479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1156 AA; 131208 MW; 52A52C984462F692 CRC64;
MACPWQFLFK IKSQKVDLAT ELDINNNVGK FYQPPSSPVT QDDPKRHSPG KHGNESPQPL
TGTVKTSPES LSKLDAPPSA CPRHVRIKNW GSGVTFQDTL HQKAKGDLSC KSKSCLASIM
NPKSLTIGPR DKPTPPDELL PQAIEFVNQY YGSFKEAKIE EHLARVEAVT KEIETTGTYQ
LTGDELIFAT KQAWRNAPRC IGRIQWSNLQ VFDARSCSTA QEMFEHICRH VRYATNNGNI
RSAITVFPQR SDGKHDFRVW NAQLIRYAGY QMPDGSIRGD PANVEFTQLC IDLGWKPKYG
RFDVLPLVLQ ADGRDPELFE IPPDLVLEVP MEHPRYEWFR ELELKWYALP AVANMLLEVG
GLEFPGCPFN GWYMGTEVGV RDFCDAQRYN ILEEVGRRMG LETHKVASLW KDRAVVEINV
AVLHSFQKQN VTIMDHHSAA ESFMKYMQNE YRSRGGCPAD WIWLVPPISG SITPVFHQEM
LNYVLSPFYY YQVEPWKTHV WQDERRRPQR REIRFKVLVK AVFFASVLMH KAMASRVRAT
ILFATETGRS ETLAQDLGAL FSCAFNPKVL CMDQYQLSHL EEEQLLLVVT STFGNGDSPG
NGEKLKKSLL MLKELTNTFR YAVFGLGSSM YPQFCAFAHD IDQKLSQLGA SQLAPTGEGD
ELSGQEEAFR SWAVQTFKAA CETFDVSGKH HIEIPKLYTS NVTWDPQHYR LVQDSEPLDL
NKALSSMHAK HVFTMRLKSQ QNLQSPKSSR TTLLVELSCE GSQAPSYLPG EHLGVFPCNQ
PALVQGILER VVDGPAPHQP VRLETLCENG SYWVKDKRLP PCSLSQALTY FLDITTPPTQ
LLLRKLAQLA TEEAEKQRLE TLCQPSDYNK WKFTNSPTFL EVLEEFPSLR VSASFLLSQL
PILKPRYYSI SSSRDLTPTE IHLTVAVLTY RTRDGQGPLH HGVCSTWLSS LKPQDPVPCF
VRSASGFQLP EDRSRPCILI GPGTGIAPFR SFWQQRLHEA EHKGLQGGRM TLVFGCRRPE
EDHLYWEEML EMARKGVLHE VHTAYSRLPD QPKVYVQDIL RQRLAGEVLR VLHEEQGHLY
VCGDVRMARD VARTLKQLMA TALSLNEEQV EDYFFQLKNQ KRYHEDIFGA VFPYEVKKDG
AAGLPSNPRA PGAHRS
//
