OXDD_HUMAN
ID OXDD_HUMAN Reviewed; 341 AA.
AC Q99489; A8KAG4; Q5JXM4; Q5JXM5; Q5JXM6; Q8N552;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=D-aspartate oxidase;
DE Short=DASOX;
DE Short=DDO;
DE EC=1.4.3.1 {ECO:0000269|PubMed:9163533};
GN Name=DDO;
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] (ISOFORMS DDO-1 AND DDO-2), FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Brain;
RX PubMed=9163533; DOI=10.1093/oxfordjournals.jbchem.a021655;
RA Setoyama C., Miura R.;
RT "Structural and functional characterization of the human brain D-aspartate
RT oxidase.";
RL J. Biochem. 121:798-803(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ISOFORM 4).
RA Birkett C., Cho J., Gau Y., Hamer R., Kelly S., Kovacs K., Liu L., Liu X.,
RA Porter J., Sachs A., Shu Y., Sun Z., Wong J., Wu M., Zhang X., Jay G.,
RA He W.;
RT "High-throughput cloning of full-length human cDNAs directly from cDNA
RT libraries optimized for large and rare transcripts.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-136.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Selectively catalyzes the oxidative deamination of D-
CC aspartate and its N-methylated derivative, N-methyl D-aspartate.
CC {ECO:0000269|PubMed:9163533}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate;
CC Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29990; EC=1.4.3.1; Evidence={ECO:0000269|PubMed:9163533};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 mM for D-aspartate (at pH 8.3) {ECO:0000269|PubMed:9163533};
CC KM=6.8 mM for N-methyl D-aspartate (at pH 8.3)
CC {ECO:0000269|PubMed:9163533};
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=DDO-1; Synonyms=A;
CC IsoId=Q99489-1; Sequence=Displayed;
CC Name=DDO-2;
CC IsoId=Q99489-2; Sequence=VSP_001269;
CC Name=3;
CC IsoId=Q99489-3; Sequence=VSP_037664;
CC Name=4;
CC IsoId=Q99489-4; Sequence=VSP_037664, VSP_001269;
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR EMBL; D89858; BAA14031.1; -; mRNA.
DR EMBL; AK293029; BAF85718.1; -; mRNA.
DR EMBL; AL050350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48316.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48317.1; -; Genomic_DNA.
DR EMBL; BC032786; AAH32786.3; -; mRNA.
DR EMBL; DN990727; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS5082.1; -. [Q99489-1]
DR CCDS; CCDS5083.1; -. [Q99489-2]
DR PIR; JC5438; JC5438.
DR PIR; JC5439; JC5439.
DR RefSeq; NP_003640.2; NM_003649.2.
DR RefSeq; NP_004023.2; NM_004032.2. [Q99489-2]
DR PDB; 6RKF; X-ray; 3.22 A; A/B/C/D/E/F=1-341.
DR PDBsum; 6RKF; -.
DR AlphaFoldDB; Q99489; -.
DR SMR; Q99489; -.
DR BioGRID; 114098; 3.
DR IntAct; Q99489; 2.
DR STRING; 9606.ENSP00000357920; -.
DR BindingDB; Q99489; -.
DR ChEMBL; CHEMBL5887; -.
DR iPTMnet; Q99489; -.
DR PhosphoSitePlus; Q99489; -.
DR BioMuta; DDO; -.
DR DMDM; 2494037; -.
DR MassIVE; Q99489; -.
DR MaxQB; Q99489; -.
DR PaxDb; Q99489; -.
DR PeptideAtlas; Q99489; -.
DR PRIDE; Q99489; -.
DR ProteomicsDB; 78291; -. [Q99489-1]
DR ProteomicsDB; 78292; -. [Q99489-2]
DR ProteomicsDB; 78293; -. [Q99489-3]
DR ProteomicsDB; 78294; -. [Q99489-4]
DR Antibodypedia; 32325; 226 antibodies from 24 providers.
DR DNASU; 8528; -.
DR Ensembl; ENST00000368923.8; ENSP00000357919.4; ENSG00000203797.12. [Q99489-2]
DR Ensembl; ENST00000368924.9; ENSP00000357920.4; ENSG00000203797.12. [Q99489-1]
DR GeneID; 8528; -.
DR KEGG; hsa:8528; -.
DR MANE-Select; ENST00000368924.9; ENSP00000357920.4; NM_001372108.2; NP_001359037.1.
DR UCSC; uc003puc.4; human. [Q99489-1]
DR CTD; 8528; -.
DR DisGeNET; 8528; -.
DR GeneCards; DDO; -.
DR HGNC; HGNC:2727; DDO.
DR HPA; ENSG00000203797; Tissue enhanced (heart).
DR MIM; 124450; gene.
DR neXtProt; NX_Q99489; -.
DR OpenTargets; ENSG00000203797; -.
DR PharmGKB; PA27194; -.
DR VEuPathDB; HostDB:ENSG00000203797; -.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR HOGENOM; CLU_034311_0_2_1; -.
DR InParanoid; Q99489; -.
DR OMA; MAIRERC; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; Q99489; -.
DR TreeFam; TF313887; -.
DR BRENDA; 1.4.3.1; 2681.
DR PathwayCommons; Q99489; -.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; Q99489; -.
DR SignaLink; Q99489; -.
DR BioGRID-ORCS; 8528; 8 hits in 1064 CRISPR screens.
DR ChiTaRS; DDO; human.
DR GeneWiki; DDO_(gene); -.
DR GenomeRNAi; 8528; -.
DR Pharos; Q99489; Tchem.
DR PRO; PR:Q99489; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q99489; protein.
DR Bgee; ENSG00000203797; Expressed in heart left ventricle and 136 other tissues.
DR ExpressionAtlas; Q99489; baseline and differential.
DR Genevisible; Q99489; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; NAS:UniProtKB.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
DR GO; GO:0008445; F:D-aspartate oxidase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0006533; P:aspartate catabolic process; IDA:UniProtKB.
DR GO; GO:0019478; P:D-amino acid catabolic process; IDA:UniProtKB.
DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
DR GO; GO:0007320; P:insemination; IEA:Ensembl.
DR InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; PTHR11530; 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR PROSITE; PS00677; DAO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; FAD; Flavoprotein; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..341
FT /note="D-aspartate oxidase"
FT /id="PRO_0000162770"
FT MOTIF 339..341
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 6..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 43..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 48..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307..311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MRPARHWETRFGARDFGGFQDCFFRDRLM (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_037664"
FT VAR_SEQ 95..153
FT /note="Missing (in isoform DDO-2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9163533, ECO:0000303|Ref.6"
FT /id="VSP_001269"
FT VARIANT 136
FT /note="F -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036244"
FT VARIANT 189
FT /note="Q -> E (in dbSNP:rs17622)"
FT /id="VAR_014939"
FT VARIANT 230
FT /note="H -> Y (in dbSNP:rs17621)"
FT /id="VAR_014940"
FT VARIANT 255
FT /note="L -> R (in dbSNP:rs17623)"
FT /id="VAR_014941"
FT CONFLICT 278
FT /note="R -> S (in Ref. 2; BAF85718)"
FT /evidence="ECO:0000305"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6RKF"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 61..79
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:6RKF"
FT TURN 108..112
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:6RKF"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 197..207
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 269..280
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6RKF"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6RKF"
FT HELIX 314..333
FT /evidence="ECO:0007829|PDB:6RKF"
FT CONFLICT Q99489-4:9
FT /note="T -> N (in Ref. 6; DN990727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 37535 MW; 8CAE7501FB7F215C CRC64;
MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP
IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGWQIFQS TPTEEVPFWA DVVLGFRKMT
EAELKKFPQY VFGQAFTTLK CECPAYLPWL EKRIKGSGGW TLTRRIEDLW ELHPSFDIVV
NCSGLGSRQL AGDSKIFPVR GQVLQVQAPW VEHFIRDGSG LTYIYPGTSH VTLGGTRQKG
DWNLSPDAEN SREILSRCCA LEPSLHGACN IREKVGLRPY RPGVRLQTEL LARDGQRLPV
VHHYGHGSGG ISVHWGTALE AARLVSECVH ALRTPIPKSN L
