ID   NOS2_CAVPO              Reviewed;        1149 AA.
AC   O54705;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 162.
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; Synonyms=NOS;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hartley; TISSUE=Lung;
RX   PubMed=9677342; DOI=10.1042/bj3330795;
RA   Shirato M., Sakamoto T., Uchida Y., Nomura A., Ishii Y., Iijima H.,
RA   Goto Y., Hasegawa S.;
RT   "Molecular cloning and characterization of Ca2+-dependent inducible nitric
RT   oxide synthase from guinea-pig lung.";
RL   Biochem. J. 333:795-799(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: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.
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: Expressed in the lung and colon. Not detected in
CC       the heart, aorta, liver, kidney, and spleen.
CC   -!- INDUCTION: By lipopolysaccharide (LPS); in kidney, spleen, and colon.
CC       Expression is reduced in the presence of LPS in lung.
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; AF027180; AAC33177.1; -; mRNA.
DR   RefSeq; NP_001166455.1; NM_001172984.1.
DR   AlphaFoldDB; O54705; -.
DR   SMR; O54705; -.
DR   STRING; 10141.ENSCPOP00000016760; -.
DR   GeneID; 100135576; -.
DR   KEGG; cpoc:100135576; -.
DR   CTD; 4843; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   InParanoid; O54705; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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:0042742; P:defense response to bacterium; 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   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..1149
FT                   /note="Nitric oxide synthase, inducible"
FT                   /id="PRO_0000170929"
FT   DOMAIN          538..676
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          729..969
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          22..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..534
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        49..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         109
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         114
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         117
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         199
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         262
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         371
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         376
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         380
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         461
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:P29474"
FT   BINDING         475
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         490
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         544
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
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         548
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         590
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         627
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         634
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         660
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         664
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         749
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         771
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         907
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         923
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         925
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         928
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         929
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         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         983
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1016
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1045
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         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         1056
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1089
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   MOD_RES         574
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06518"
SQ   SEQUENCE   1149 AA;  130632 MW;  66D595A2486DB50E CRC64;
     MACPWNFLWK LKSSRYDLTE EKDINNNVGK ASHLYSPEIQ DDPKYCSPGK HQNGSSQSLT
     GTAKKVPESQ SKPHKPSPTC SQHMKIKNWG NGMILQDTLH TKAKTNFTCK PKSCLGSVMN
     PRSMTRGPRD TPIPPDELLP QAIEFVNQYY DSFKEAKIEE YLARVETVTK EIETTGTYQL
     TGDELIFATK LAWRNAPRCI GRIQWSNLQV FDARSCHTAQ EMFEHICRHV RYSTNNGNIR
     SAITVFPQRT DGKHDFRVWN AQLIRYAGYQ MPDGTIQGDP ANLEFTQLCI DLGWKPRYGR
     FDVLPLILQA DGRDPELFEI PPDLVLEVPM EHPKYEWFQD LGLKWYALPA VANMLLEVGG
     LEFPACPFNG WYMGTEIGVR DFCDAQRYNI LEEVGRRMGL ETHTLASLWK DRAVTEINVA
     VLHSFQKQNV TIMDHHSAAE SFMKHMQNEY RARGGCPADW IWLVPPISGS ITPVFHQEML
     NYILSPFYYY QVEAWKTHVW QDETRRPKRR EIPFRVLAKA TLFASLLMRK MMASRVRATI
     LFATETGKSE ALAQDLGALF SCAFNPKVLC MDQYQLSSLE EEKLLLVVTS TFGNGDCPGN
     GETLKKSLFV LKKLTNTFRY AVFGLGSSMY PRFCAFAHDI DIKLSQLGAS QLTPVGEGDE
     LSGQEDAFCT WAVQTFQAAC AAFDVRGRHH ITIPKRYTSS VTWEPYHYRL VQDSQPLDLN
     KALSRMHATD VFTMRLKSQK NLQSPKSSRT TLLMELSCDD SRSLAYLPGE HLGVFPCNQP
     ALVQGILECV VDNPGPHHTV CLEVLDDSGS YWAKDKRLPP CSLSQALTYF LDITTPPTQL
     QLQKLARLAT EQAERLRLES LSQPSEYNKW KFTNSPTFLE VLEEFPSLRV PAAFLLSQLP
     ILKPRYYSIS SSLDHTPAEV HLTVAVVTYR TRDGRGPLHH GVCSTWFSGL KPQDPVPCLV
     RSVNSFQLPK DPSQPCILIG PGTGIAPFRS FWQQRLHNLK HTGLQGGRMT LLFGCRHPEE
     DHIYKEEMQE MVQKGVLHEV HTAYSRLPGK PKAYVQDILR QQLAREVLRV LHEEPGHLYV
     CGNVLMAQDV ACTLKQLLAA KLNLNEEQVE DYFFQLKSQK RYHEDIFGAV FPHGVKKDRA
     ERPPGDDKL
//