ID   NOS3_CANLF              Reviewed;        1205 AA.
AC   Q9TUX8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Nitric oxide synthase 3 {ECO:0000305};
DE            EC=1.14.13.39 {ECO:0000250|UniProtKB:P29474};
DE   AltName: Full=Constitutive NOS;
DE            Short=cNOS;
DE   AltName: Full=EC-NOS;
DE   AltName: Full=NOS type III;
DE            Short=NOSIII;
DE   AltName: Full=Nitric oxide synthase, endothelial {ECO:0000305};
DE            Short=Endothelial NOS {ECO:0000305};
DE            Short=eNOS {ECO:0000305};
GN   Name=NOS3; Synonyms=NOS;
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=Heart;
RX   PubMed=10442857; DOI=10.1006/niox.1999.0234;
RA   Schwemmer M., Bassenge E.;
RT   "Assembly and characterization of canine heart endothelial nitric oxide
RT   synthase cDNA and 5'-flanking sequence by homology (RT-)PCR cloning.";
RL   Nitric Oxide 3:254-264(1999).
CC   -!- FUNCTION: Produces nitric oxide (NO) which is implicated in vascular
CC       smooth muscle relaxation through a cGMP-mediated signal transduction
CC       pathway. NO mediates vascular endothelial growth factor (VEGF)-induced
CC       angiogenesis in coronary vessels and promotes blood clotting through
CC       the activation of platelets (By similarity).
CC       {ECO:0000250|UniProtKB:P29474}.
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:P29474};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC         Evidence={ECO:0000250|UniProtKB:P29474};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P29474};
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: Stimulated by calcium/calmodulin. Inhibited by
CC       NOSIP and NOSTRIN (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By similarity).
CC       Interacts with HSP90AB1 (By similarity). Forms a complex with ASL, ASS1
CC       and SLC7A1; the complex regulates cell-autonomous L-arginine synthesis
CC       and citrulline recycling while channeling extracellular L-arginine to
CC       nitric oxide synthesis pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P29474, ECO:0000250|UniProtKB:P70313}.
CC   -!- SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell
CC       membrane {ECO:0000250}. Note=Specifically associates with actin
CC       cytoskeleton in the G2 phase of the cell cycle, which is favored by
CC       interaction with NOSIP and results in a reduced enzymatic activity.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation by AMPK at Ser-1179 in the presence of Ca(2+)-
CC       calmodulin (CaM) activates activity. In absence of Ca(2+)-calmodulin,
CC       AMPK also phosphorylates Thr-497, resulting in inhibition of activity.
CC       Phosphorylation of Ser-116 by CDK5 reduces activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR   EMBL; AF143503; AAD52161.1; -; mRNA.
DR   AlphaFoldDB; Q9TUX8; -.
DR   BMRB; Q9TUX8; -.
DR   SMR; Q9TUX8; -.
DR   STRING; 9615.ENSCAFP00000061234; -.
DR   PaxDb; 9612-ENSCAFP00000006985; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   InParanoid; Q9TUX8; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR   GO; GO:0006527; P:arginine catabolic process; 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: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; -; 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; Cell membrane; Cytoplasm; Cytoskeleton; FAD;
KW   Flavoprotein; FMN; Golgi apparatus; Heme; Iron; Lipoprotein; Membrane;
KW   Metal-binding; Myristate; NADP; Oxidoreductase; Palmitate; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P29473"
FT   CHAIN           2..1205
FT                   /note="Nitric oxide synthase 3"
FT                   /id="PRO_0000289580"
FT   DOMAIN          522..705
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          758..1004
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..488
FT                   /note="Interaction with NOSIP"
FT                   /evidence="ECO:0000250"
FT   REGION          492..512
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          819..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..67
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96
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         101
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         104
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         186
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         249
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         358
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         359
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         363
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         368
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         448
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         449
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
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         477
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   BINDING         528
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         529
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         530
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         532
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         574
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         575
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         656
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         663
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         689
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         693
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P35228"
FT   BINDING         778
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         800
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         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         958
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         960
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         964
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         977
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         978
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         979
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1018
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1051
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1080
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1081
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   BINDING         1089
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1091
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   MOD_RES         116
FT                   /note="Phosphoserine; by CDK5"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   MOD_RES         497
FT                   /note="Phosphothreonine; by AMPK"
FT                   /evidence="ECO:0000250|UniProtKB:P29473"
FT   MOD_RES         617
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70313"
FT   MOD_RES         635
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29473"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   MOD_RES         838
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29474"
FT   MOD_RES         1177
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P70313"
FT   MOD_RES         1179
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000250|UniProtKB:P29473"
FT   MOD_RES         1181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70313"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   LIPID           15
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           26
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1205 AA;  133046 MW;  C150CDEB01685BA5 CRC64;
     MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPTSEPSR APALAPPPSP PPAPDHSSPP
     LTRPPDGPKF PRVKNWEVGS ITYDTLSAQS QQDGPCTPRR CLGSLVFPRK LQSRPSQNPA
     PPEQLLSQAR DFISQYYSSI KRSGSQAHEQ RLQEVEAEVA ATGTYQLRES ELVFGAKQAW
     RNAPRCVGRI QWGKLQVFDA RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRASGR
     GDFRIWNSQL VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE
     PPELFALPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF PAAPFSGWYM
     STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA AVEINLAVLH SYQLAKVTIV
     DHHAATASFM KHLENEQKAR GGCPADWAWI VPPISGSLTP VFHQEMVNYV LSPAFRYQTD
     PWKGSASKGA GVTRKKTFKE VANAVKISAS LMGTVMAKRV KATILYGSET GRAQSYAQQL
     GRLFRKAFDP RVLCMDEYDV VSLEHETLVL VVTSTFGNGD PPENGESFAA ALMEMSGSYN
     SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESRNTDS AGALGTLRFC VFGLGSRAYP
     HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFGGW AQAAFQASWE TFCVGEDAKA
     AARDIFSPKR TWKRQRYRLS AQAEGLQLLP GLIHVHRRKM VQATVLAVEN LQSSKSTRAT
     ILVRLDTGSQ EALQYQPGDH IGICPPNRPG LVEALLSRVE DPPPPGEPVA VEQLEKGSPG
     GPPPSWVRDP RLPPCTLRQA LTFFLDITSP PSPQLLRLLS TLAEESSEQQ ELESLSQDPR
     RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPSA HPGEIHLTVA
     VLAYRTQDGL GPLHYGVCST WLSQLKAGDP VPCFIRGAPS FRLPPDPSLP CILVGPGTGI
     APFRGFWQGR LHDIYSKGLQ PAPMTLVFGC RCSQLDHLYR DEVQDAQQRG VFGRVLTAFS
     REPDSPKTYV QDILRTELAA EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME
     LDEAGDVIGV LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWALDPPGP
     DTVGP
//