ID   AEDO_HUMAN              Reviewed;         270 AA.
AC   Q96SZ5; B1AL29;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=2-aminoethanethiol dioxygenase;
DE            EC=1.13.11.19 {ECO:0000269|PubMed:17581819, ECO:0000269|PubMed:29752763, ECO:0000269|PubMed:32601061};
DE   AltName: Full=Cysteamine dioxygenase;
GN   Name=ADO; Synonyms=C10orf22;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TRP-25 AND ALA-39.
RC   TISSUE=Brain, and Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-270, AND VARIANT ALA-39.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17581819; DOI=10.1074/jbc.m703089200;
RA   Dominy J.E. Jr., Simmons C.R., Hirschberger L.L., Hwang J., Coloso R.M.,
RA   Stipanuk M.H.;
RT   "Discovery and characterization of a second mammalian thiol dioxygenase,
RT   cysteamine dioxygenase.";
RL   J. Biol. Chem. 282:25189-25198(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CROSS-LINK,
RP   AND MUTAGENESIS OF TYR-87; TYR-222 AND TYR-223.
RX   PubMed=29752763; DOI=10.1002/anie.201803907;
RA   Wang Y., Griffith W.P., Li J., Koto T., Wherritt D.J., Fritz E., Liu A.;
RT   "Cofactor Biogenesis in Cysteamine Dioxygenase: C-F Bond Cleavage with
RT   Genetically Incorporated Unnatural Tyrosine.";
RL   Angew. Chem. Int. Ed. 57:8149-8153(2018).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=31273118; DOI=10.1126/science.aaw0112;
RA   Masson N., Keeley T.P., Giuntoli B., White M.D., Puerta M.L., Perata P.,
RA   Hopkinson R.J., Flashman E., Licausi F., Ratcliffe P.J.;
RT   "Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia
RT   in animals and plants.";
RL   Science 365:65-69(2019).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=32601061; DOI=10.1074/jbc.ra120.013915;
RA   Wang Y., Davis I., Chan Y., Naik S.G., Griffith W.P., Liu A.;
RT   "Characterization of the nonheme iron center of cysteamine dioxygenase and
RT   its interaction with substrates.";
RL   J. Biol. Chem. 295:11789-11802(2020).
RN   [10] {ECO:0007744|PDB:7REI}
RP   X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF MUTANTS SER-18/SER-239 IN COMPLEX
RP   WITH NICKEL, SUBUNIT, COFACTOR, AND IRON-BINDING SITES.
RX   PubMed=34508780; DOI=10.1016/j.jbc.2021.101176;
RA   Wang Y., Shin I., Li J., Liu A.;
RT   "Crystal structure of human cysteamine dioxygenase provides a structural
RT   rationale for its function as an oxygen sensor.";
RL   J. Biol. Chem. 297:101176-101176(2021).
CC   -!- FUNCTION: Plays a vital role in regulating thiol metabolism and
CC       preserving oxygen homeostasis by oxidizing the sulfur of cysteamine and
CC       N-terminal cysteine-containing proteins to their corresponding sulfinic
CC       acids using O2 as a cosubstrate (PubMed:17581819, PubMed:29752763,
CC       PubMed:31273118, PubMed:32601061). Catalyzes the oxidation of
CC       cysteamine (2-aminoethanethiol) to hypotaurine (PubMed:17581819,
CC       PubMed:29752763, PubMed:32601061). Catalyzes the oxidation of
CC       regulators of G-protein signaling 4 (RGS4) and 5 (RGS5) and
CC       interleukin-32 (IL32) (PubMed:31273118, PubMed:32601061).
CC       {ECO:0000269|PubMed:17581819, ECO:0000269|PubMed:29752763,
CC       ECO:0000269|PubMed:31273118, ECO:0000269|PubMed:32601061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cysteamine + O2 = H(+) + hypotaurine; Xref=Rhea:RHEA:14409,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57853,
CC         ChEBI:CHEBI:58029; EC=1.13.11.19;
CC         Evidence={ECO:0000269|PubMed:17581819, ECO:0000269|PubMed:29752763,
CC         ECO:0000269|PubMed:32601061};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14410;
CC         Evidence={ECO:0000305|PubMed:17581819};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-cysteinyl-[protein] + O2 = H(+) + N-terminal S-
CC         hydroxy-S-oxy-L-cysteinyl-[protein]; Xref=Rhea:RHEA:70895, Rhea:RHEA-
CC         COMP:12707, Rhea:RHEA-COMP:17973, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:65250, ChEBI:CHEBI:156254;
CC         Evidence={ECO:0000269|PubMed:31273118, ECO:0000269|PubMed:32601061};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70896;
CC         Evidence={ECO:0000305|PubMed:31273118};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:34508780};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.4 mM for cysteamine {ECO:0000269|PubMed:29752763};
CC         KM=123 uM for RGS4 {ECO:0000269|PubMed:31273118};
CC         KM=71.51 uM for RGS5 {ECO:0000269|PubMed:31273118};
CC         KM=33.6 uM for IL32 {ECO:0000269|PubMed:31273118};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:34508780}.
CC   -!- INTERACTION:
CC       Q96SZ5; P40123: CAP2; NbExp=3; IntAct=EBI-11102284, EBI-1051165;
CC       Q96SZ5; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-11102284, EBI-11988027;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB55123.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL133417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471083; EAW54235.1; -; Genomic_DNA.
DR   EMBL; BC018660; AAH18660.3; -; mRNA.
DR   EMBL; BC028589; AAH28589.2; -; mRNA.
DR   EMBL; BC067740; AAH67740.2; -; mRNA.
DR   EMBL; AK027453; BAB55123.1; ALT_INIT; mRNA.
DR   CCDS; CCDS7266.2; -.
DR   RefSeq; NP_116193.2; NM_032804.5.
DR   PDB; 7REI; X-ray; 1.78 A; A=1-270.
DR   PDBsum; 7REI; -.
DR   AlphaFoldDB; Q96SZ5; -.
DR   SMR; Q96SZ5; -.
DR   BioGRID; 124330; 21.
DR   IntAct; Q96SZ5; 10.
DR   STRING; 9606.ENSP00000362888; -.
DR   GlyGen; Q96SZ5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96SZ5; -.
DR   MetOSite; Q96SZ5; -.
DR   PhosphoSitePlus; Q96SZ5; -.
DR   BioMuta; ADO; -.
DR   DMDM; 88984104; -.
DR   EPD; Q96SZ5; -.
DR   jPOST; Q96SZ5; -.
DR   MassIVE; Q96SZ5; -.
DR   MaxQB; Q96SZ5; -.
DR   PaxDb; 9606-ENSP00000362888; -.
DR   PeptideAtlas; Q96SZ5; -.
DR   ProteomicsDB; 78164; -.
DR   Pumba; Q96SZ5; -.
DR   Antibodypedia; 45164; 219 antibodies from 25 providers.
DR   DNASU; 84890; -.
DR   Ensembl; ENST00000373783.3; ENSP00000362888.1; ENSG00000181915.6.
DR   GeneID; 84890; -.
DR   KEGG; hsa:84890; -.
DR   MANE-Select; ENST00000373783.3; ENSP00000362888.1; NM_032804.6; NP_116193.2.
DR   UCSC; uc001jmg.4; human.
DR   AGR; HGNC:23506; -.
DR   CTD; 84890; -.
DR   DisGeNET; 84890; -.
DR   GeneCards; ADO; -.
DR   HGNC; HGNC:23506; ADO.
DR   HPA; ENSG00000181915; Low tissue specificity.
DR   MIM; 611392; gene.
DR   neXtProt; NX_Q96SZ5; -.
DR   OpenTargets; ENSG00000181915; -.
DR   PharmGKB; PA162375713; -.
DR   VEuPathDB; HostDB:ENSG00000181915; -.
DR   eggNOG; KOG4281; Eukaryota.
DR   GeneTree; ENSGT00390000014082; -.
DR   HOGENOM; CLU_061320_2_1_1; -.
DR   InParanoid; Q96SZ5; -.
DR   OMA; PQGFPEN; -.
DR   OrthoDB; 2914618at2759; -.
DR   PhylomeDB; Q96SZ5; -.
DR   TreeFam; TF314673; -.
DR   BioCyc; MetaCyc:HS17749-MONOMER; -.
DR   BRENDA; 1.13.11.19; 2681.
DR   PathwayCommons; Q96SZ5; -.
DR   Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine.
DR   SignaLink; Q96SZ5; -.
DR   BioGRID-ORCS; 84890; 50 hits in 1156 CRISPR screens.
DR   ChiTaRS; ADO; human.
DR   GenomeRNAi; 84890; -.
DR   Pharos; Q96SZ5; Tbio.
DR   PRO; PR:Q96SZ5; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q96SZ5; Protein.
DR   Bgee; ENSG00000181915; Expressed in sperm and 210 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0047800; F:cysteamine dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR   GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR   CDD; cd20289; cupin_ADO; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR012864; PCO/ADO.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR22966:SF61; 2-AMINOETHANETHIOL DIOXYGENASE; 1.
DR   PANTHER; PTHR22966; UNCHARACTERIZED; 1.
DR   Pfam; PF07847; PCO_ADO; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   Genevisible; Q96SZ5; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome; Thioether bond.
FT   CHAIN           1..270
FT                   /note="2-aminoethanethiol dioxygenase"
FT                   /id="PRO_0000089784"
FT   REGION          21..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         112
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:34508780,
FT                   ECO:0007744|PDB:7REI"
FT   BINDING         114
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:34508780,
FT                   ECO:0007744|PDB:7REI"
FT   BINDING         193
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:34508780,
FT                   ECO:0007744|PDB:7REI"
FT   CROSSLNK        220..223
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000269|PubMed:29752763"
FT   VARIANT         25
FT                   /note="G -> W (in dbSNP:rs2236295)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_025333"
FT   VARIANT         39
FT                   /note="P -> A (in dbSNP:rs10995311)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_025334"
FT   VARIANT         266
FT                   /note="P -> S (in dbSNP:rs569705)"
FT                   /id="VAR_033691"
FT   MUTAGEN         87
FT                   /note="Y->A: Moderate reduction in enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:29752763"
FT   MUTAGEN         222
FT                   /note="Y->A,F: Significant reduction in enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:29752763"
FT   MUTAGEN         223
FT                   /note="Y->A: No significant reduction in enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:29752763"
FT   HELIX           9..21
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   HELIX           47..60
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          84..92
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          118..135
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   HELIX           159..164
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          166..176
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          192..210
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          222..225
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          241..250
FT                   /evidence="ECO:0007829|PDB:7REI"
FT   STRAND          258..260
FT                   /evidence="ECO:0007829|PDB:7REI"
SQ   SEQUENCE   270 AA;  29751 MW;  6B496CCF16E92C9D CRC64;
     MPRDNMASLI QRIARQACLT FRGSGGGRGA SDRDAASGPE APMQPGFPEN LSKLKSLLTQ
     LRAEDLNIAP RKATLQPLPP NLPPVTYMHI YETDGFSLGV FLLKSGTSIP LHDHPGMHGM
     LKVLYGTVRI SCMDKLDAGG GQRPRALPPE QQFEPPLQPR EREAVRPGVL RSRAEYTEAS
     GPCILTPHRD NLHQIDAVEG PAAFLDILAP PYDPDDGRDC HYYRVLEPVR PKEASSSACD
     LPREVWLLET PQADDFWCEG EPYPGPKVFP
//