ID   TPH1_HUMAN              Reviewed;         444 AA.
AC   P17752; D3DQX6; O95188; O95189; Q16736; Q3KPG8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 4.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=Tryptophan 5-hydroxylase 1;
DE            EC=1.14.16.4 {ECO:0000250|UniProtKB:P17532};
DE   AltName: Full=Tryptophan 5-monooxygenase 1;
GN   Name=TPH1; Synonyms=TPH, TPRH, TRPH;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Carcinoma;
RX   PubMed=2377472; DOI=10.1093/nar/18.14.4257;
RA   Boulalard S., Darmon M.C., Ganem Y., Launay J.-M., Mallet J.;
RT   "Complete coding sequence of human tryptophan hydroxylase.";
RL   Nucleic Acids Res. 18:4257-4257(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=7986090; DOI=10.1006/abbi.1994.1523;
RA   Tipper J.P., Citron B.A., Ribeiro P., Kaufman S.;
RT   "Cloning and expression of rabbit and human brain tryptophan hydroxylase
RT   cDNA in Escherichia coli.";
RL   Arch. Biochem. Biophys. 315:445-453(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-444 (ISOFORMS 1 AND 2), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9751214; DOI=10.1046/j.1471-4159.1998.71041769.x;
RA   Wang G.A., Coon S.L., Kaufman S.;
RT   "Alternative splicing at the 3'-cDNA of human tryptophan hydroxylase.";
RL   J. Neurochem. 71:1769-1772(1998).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 102-402 IN COMPLEX WITH IRON, AND
RP   COFACTOR.
RX   PubMed=12379098; DOI=10.1021/bi026561f;
RA   Wang L., Erlandsen H., Haavik J., Knappskog P.M., Stevens R.C.;
RT   "Three-dimensional structure of human tryptophan hydroxylase and its
RT   implications for the biosynthesis of the neurotransmitters serotonin and
RT   melatonin.";
RL   Biochemistry 41:12569-12574(2002).
CC   -!- FUNCTION: Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-
CC       determining step of serotonin biosynthesis.
CC       {ECO:0000250|UniProtKB:P17532}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2
CC         = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-
CC         hydroxy-L-tryptophan; Xref=Rhea:RHEA:16709, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15642, ChEBI:CHEBI:57912, ChEBI:CHEBI:58266,
CC         ChEBI:CHEBI:59560; EC=1.14.16.4;
CC         Evidence={ECO:0000250|UniProtKB:P17532};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:12379098};
CC   -!- PATHWAY: Aromatic compound metabolism; serotonin biosynthesis;
CC       serotonin from L-tryptophan: step 1/2. {ECO:0000250|UniProtKB:P17532}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P70080}.
CC   -!- INTERACTION:
CC       P17752; Q14457: BECN1; NbExp=3; IntAct=EBI-3956833, EBI-949378;
CC       P17752; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-3956833, EBI-18924329;
CC       P17752; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-3956833, EBI-739467;
CC       P17752; O43586: PSTPIP1; NbExp=3; IntAct=EBI-3956833, EBI-1050964;
CC       P17752; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-3956833, EBI-12949277;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P17752-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P17752-2; Sequence=VSP_000546;
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Seems to be less widely expressed than
CC       isoform 1. {ECO:0000269|PubMed:9751214}.
CC   -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC       Ubiquitinated is triggered by phosphorylation.
CC       {ECO:0000250|UniProtKB:P09810}.
CC   -!- PTM: Phosphorylated; triggering degradation by the proteasome.
CC       {ECO:0000250|UniProtKB:P09810}.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000305}.
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DR   EMBL; X52836; CAA37018.1; -; mRNA.
DR   EMBL; L29306; AAA67050.1; -; mRNA.
DR   EMBL; CH471064; EAW68421.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68422.1; -; Genomic_DNA.
DR   EMBL; BC106739; AAI06740.1; -; mRNA.
DR   EMBL; AF057280; AAC69458.1; -; Genomic_DNA.
DR   EMBL; AF057280; AAC69459.1; -; Genomic_DNA.
DR   CCDS; CCDS7829.1; -. [P17752-1]
DR   PIR; S10489; S10489.
DR   RefSeq; NP_004170.1; NM_004179.2. [P17752-1]
DR   PDB; 1MLW; X-ray; 1.71 A; A=102-402.
DR   PDB; 3HF6; X-ray; 1.80 A; A=105-393.
DR   PDB; 3HF8; X-ray; 1.85 A; A=105-393.
DR   PDB; 3HFB; X-ray; 1.92 A; A=104-393.
DR   PDB; 5J6D; X-ray; 1.90 A; A/B=102-402.
DR   PDB; 5L01; X-ray; 1.90 A; A=1-444.
DR   PDB; 5TPG; X-ray; 1.50 A; A=104-402.
DR   PDB; 7ZIF; X-ray; 1.87 A; A=105-401.
DR   PDB; 7ZIG; X-ray; 1.81 A; A=105-401.
DR   PDB; 7ZIH; X-ray; 1.47 A; A=105-401.
DR   PDB; 7ZII; X-ray; 1.63 A; A=105-401.
DR   PDB; 7ZIJ; X-ray; 1.95 A; A=105-401.
DR   PDB; 7ZIK; X-ray; 2.59 A; A/B=105-401.
DR   PDBsum; 1MLW; -.
DR   PDBsum; 3HF6; -.
DR   PDBsum; 3HF8; -.
DR   PDBsum; 3HFB; -.
DR   PDBsum; 5J6D; -.
DR   PDBsum; 5L01; -.
DR   PDBsum; 5TPG; -.
DR   PDBsum; 7ZIF; -.
DR   PDBsum; 7ZIG; -.
DR   PDBsum; 7ZIH; -.
DR   PDBsum; 7ZII; -.
DR   PDBsum; 7ZIJ; -.
DR   PDBsum; 7ZIK; -.
DR   AlphaFoldDB; P17752; -.
DR   SMR; P17752; -.
DR   BioGRID; 113019; 12.
DR   IntAct; P17752; 12.
DR   STRING; 9606.ENSP00000250018; -.
DR   BindingDB; P17752; -.
DR   ChEMBL; CHEMBL5689; -.
DR   DrugBank; DB05199; LX1031.
DR   DrugBank; DB00360; Sapropterin.
DR   DrugBank; DB12095; Telotristat ethyl.
DR   DrugBank; DB00150; Tryptophan.
DR   DrugCentral; P17752; -.
DR   GuidetoPHARMACOLOGY; 1241; -.
DR   GlyGen; P17752; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P17752; -.
DR   PhosphoSitePlus; P17752; -.
DR   BioMuta; TPH1; -.
DR   DMDM; 116242823; -.
DR   jPOST; P17752; -.
DR   MassIVE; P17752; -.
DR   PaxDb; 9606-ENSP00000250018; -.
DR   PeptideAtlas; P17752; -.
DR   ProteomicsDB; 53513; -. [P17752-1]
DR   ProteomicsDB; 53514; -. [P17752-2]
DR   Antibodypedia; 4386; 671 antibodies from 43 providers.
DR   DNASU; 7166; -.
DR   Ensembl; ENST00000250018.6; ENSP00000250018.2; ENSG00000129167.10. [P17752-1]
DR   Ensembl; ENST00000682019.1; ENSP00000508368.1; ENSG00000129167.10. [P17752-1]
DR   GeneID; 7166; -.
DR   KEGG; hsa:7166; -.
DR   MANE-Select; ENST00000682019.1; ENSP00000508368.1; NM_004179.3; NP_004170.1.
DR   UCSC; uc001mnp.3; human. [P17752-1]
DR   AGR; HGNC:12008; -.
DR   CTD; 7166; -.
DR   DisGeNET; 7166; -.
DR   GeneCards; TPH1; -.
DR   HGNC; HGNC:12008; TPH1.
DR   HPA; ENSG00000129167; Group enriched (choroid plexus, intestine, stomach).
DR   MIM; 191060; gene.
DR   neXtProt; NX_P17752; -.
DR   OpenTargets; ENSG00000129167; -.
DR   PharmGKB; PA355; -.
DR   VEuPathDB; HostDB:ENSG00000129167; -.
DR   eggNOG; KOG3820; Eukaryota.
DR   GeneTree; ENSGT00950000182885; -.
DR   HOGENOM; CLU_023198_0_0_1; -.
DR   InParanoid; P17752; -.
DR   OMA; SEVDMPW; -.
DR   OrthoDB; 275463at2759; -.
DR   PhylomeDB; P17752; -.
DR   TreeFam; TF313327; -.
DR   BioCyc; MetaCyc:HS05250-MONOMER; -.
DR   BRENDA; 1.14.16.4; 2681.
DR   PathwayCommons; P17752; -.
DR   Reactome; R-HSA-209931; Serotonin and melatonin biosynthesis.
DR   Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR   SABIO-RK; P17752; -.
DR   SignaLink; P17752; -.
DR   SIGNOR; P17752; -.
DR   UniPathway; UPA00846; UER00799.
DR   BioGRID-ORCS; 7166; 20 hits in 1158 CRISPR screens.
DR   ChiTaRS; TPH1; human.
DR   EvolutionaryTrace; P17752; -.
DR   GeneWiki; TPH1; -.
DR   GenomeRNAi; 7166; -.
DR   Pharos; P17752; Tclin.
DR   PRO; PR:P17752; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P17752; Protein.
DR   Bgee; ENSG00000129167; Expressed in buccal mucosa cell and 103 other cell types or tissues.
DR   ExpressionAtlas; P17752; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004510; F:tryptophan 5-monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0060749; P:mammary gland alveolus development; IEA:Ensembl.
DR   GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
DR   GO; GO:0002576; P:platelet degranulation; ISS:UniProtKB.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:1900046; P:regulation of hemostasis; ISS:UniProtKB.
DR   GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR   GO; GO:0042427; P:serotonin biosynthetic process; ISS:UniProtKB.
DR   CDD; cd04929; ACT_TPH; 1.
DR   CDD; cd03346; eu_TrpOH; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR036951; ArAA_hydroxylase_sf.
DR   InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR005963; Trp_5_mOase.
DR   InterPro; IPR041904; TrpOH_cat.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   NCBIfam; TIGR01270; Trp_5_monoox; 1.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF23; TRYPTOPHAN 5-HYDROXYLASE 1; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
DR   Genevisible; P17752; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Iron; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Serotonin biosynthesis;
KW   Ubl conjugation.
FT   CHAIN           1..444
FT                   /note="Tryptophan 5-hydroxylase 1"
FT                   /id="PRO_0000205568"
FT   DOMAIN          19..94
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   BINDING         235
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P70080"
FT   BINDING         257
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P70080"
FT   BINDING         265
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P70080"
FT   BINDING         272
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:12379098,
FT                   ECO:0007744|PDB:1MLW"
FT   BINDING         277
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:12379098,
FT                   ECO:0007744|PDB:1MLW"
FT   BINDING         317
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:12379098,
FT                   ECO:0007744|PDB:1MLW"
FT   BINDING         336
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P70080"
FT   BINDING         366
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P70080"
FT   MOD_RES         58
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         438..444
FT                   /note="VSRKPSI -> SLNEDVLQVSVFALLLFLPSLHGECHPDT (in isoform
FT                   2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000546"
FT   CONFLICT        19
FT                   /note="S -> T (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="I -> T (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90..91
FT                   /note="NL -> TP (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="L -> M (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="D -> E (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="T -> S (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="L -> S (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="N -> S (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="H -> Y (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="Q -> R (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="R -> Q (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="V -> I (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="A -> V (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        414
FT                   /note="T -> A (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419
FT                   /note="S -> N (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="Q -> R (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        436
FT                   /note="A -> G (in Ref. 2; AAA67050)"
FT                   /evidence="ECO:0000305"
FT   HELIX           112..117
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   TURN            126..128
FT                   /evidence="ECO:0007829|PDB:5J6D"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:7ZIJ"
FT   TURN            134..137
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           139..154
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           168..188
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           191..203
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           214..225
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   STRAND          228..231
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:1MLW"
FT   HELIX           238..245
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   STRAND          249..252
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           270..276
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           278..281
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           284..297
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           302..313
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   TURN            314..318
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   STRAND          320..323
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   STRAND          326..329
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           332..335
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           338..344
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   TURN            345..347
FT                   /evidence="ECO:0007829|PDB:3HF6"
FT   STRAND          351..353
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           356..359
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   STRAND          373..377
FT                   /evidence="ECO:0007829|PDB:7ZIH"
FT   HELIX           379..393
FT                   /evidence="ECO:0007829|PDB:7ZIH"
SQ   SEQUENCE   444 AA;  50985 MW;  DFAD501446953A91 CRC64;
     MIEDNKENKD HSLERGRASL IFSLKNEVGG LIKALKIFQE KHVNLLHIES RKSKRRNSEF
     EIFVDCDINR EQLNDIFHLL KSHTNVLSVN LPDNFTLKED GMETVPWFPK KISDLDHCAN
     RVLMYGSELD ADHPGFKDNV YRKRRKYFAD LAMNYKHGDP IPKVEFTEEE IKTWGTVFQE
     LNKLYPTHAC REYLKNLPLL SKYCGYREDN IPQLEDVSNF LKERTGFSIR PVAGYLSPRD
     FLSGLAFRVF HCTQYVRHSS DPFYTPEPDT CHELLGHVPL LAEPSFAQFS QEIGLASLGA
     SEEAVQKLAT CYFFTVEFGL CKQDGQLRVF GAGLLSSISE LKHALSGHAK VKPFDPKITC
     KQECLITTFQ DVYFVSESFE DAKEKMREFT KTIKRPFGVK YNPYTRSIQI LKDTKSITSA
     MNELQHDLDV VSDALAKVSR KPSI
//