HAOX2_HUMAN
ID HAOX2_HUMAN Reviewed; 351 AA.
AC Q9NYQ3; Q2TU86; Q5QP00; Q9UJS6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=2-Hydroxyacid oxidase 2 {ECO:0000303|PubMed:10777549};
DE Short=HAOX2 {ECO:0000303|PubMed:10777549};
DE EC=1.1.3.15 {ECO:0000305|PubMed:10777549};
DE AltName: Full=(S)-2-hydroxy-acid oxidase, peroxisomal;
DE AltName: Full=Cell growth-inhibiting gene 16 protein;
DE AltName: Full=Long chain alpha-hydroxy acid oxidase;
DE AltName: Full=Long-chain L-2-hydroxy acid oxidase;
GN Name=HAO2; Synonyms=HAOX2; ORFNames=GIG16;
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), FUNCTION, TISSUE SPECIFICITY,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP PATHWAY.
RX PubMed=10777549; DOI=10.1074/jbc.275.17.12590;
RA Jones J.M., Morrell J.C., Gould S.J.;
RT "Identification and characterization of HAOX1, HAOX2, and HAOX3, three
RT human peroxisomal 2-hydroxy acid oxidases.";
RL J. Biol. Chem. 275:12590-12597(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Spielbauer B., Conzelmann E.;
RT "Human long-chain L-2-hydroxy acid oxidase.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human cell growth inhibiting gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Oxidase that catalyzes the oxidation of medium and long chain
CC hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, to
CC the correspondong 2-oxoacids (PubMed:10777549). Its role in the
CC oxidation of 2-hydroxy fatty acids may contribute to the general
CC pathway of fatty acid alpha-oxidation (Probable). Active in vitro with
CC the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP),
CC but O2 is believed to be the physiological electron acceptor, leading
CC to the production of H2O2. Is not active on glycolate, glyoxylate, L-
CC lactate and 2-hydroxybutanoate (PubMed:10777549).
CC {ECO:0000269|PubMed:10777549, ECO:0000305|PubMed:10777549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2;
CC Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15;
CC Evidence={ECO:0000305|PubMed:10777549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790;
CC Evidence={ECO:0000305|PubMed:10777549};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyhexadecanoate + O2 = 2-oxohexadecanoate + H2O2;
CC Xref=Rhea:RHEA:67944, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:65097, ChEBI:CHEBI:176593;
CC Evidence={ECO:0000305|PubMed:10777549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67945;
CC Evidence={ECO:0000305|PubMed:10777549};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctanoate + O2 = 2-oxooctanoate + H2O2;
CC Xref=Rhea:RHEA:67940, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:133514, ChEBI:CHEBI:176689;
CC Evidence={ECO:0000305|PubMed:10777549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67941;
CC Evidence={ECO:0000305|PubMed:10777549};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9UJM8};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:10777549}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9UJM8}.
CC -!- INTERACTION:
CC Q9NYQ3; Q9UDX3: SEC14L4; NbExp=3; IntAct=EBI-8803200, EBI-10320311;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10777549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYQ3-2; Sequence=VSP_055095;
CC -!- TISSUE SPECIFICITY: Expressed in the liver and kidney.
CC {ECO:0000269|PubMed:10777549}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF231917; AAF40200.1; -; mRNA.
DR EMBL; AF203975; AAF14000.1; -; mRNA.
DR EMBL; AY513277; AAT08030.1; -; mRNA.
DR EMBL; AK298289; BAG60549.1; -; mRNA.
DR EMBL; AL139346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56698.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56699.1; -; Genomic_DNA.
DR EMBL; BC020863; AAH20863.1; -; mRNA.
DR CCDS; CCDS76196.1; -. [Q9NYQ3-2]
DR CCDS; CCDS901.1; -. [Q9NYQ3-1]
DR RefSeq; NP_001005783.2; NM_001005783.2. [Q9NYQ3-2]
DR RefSeq; NP_057611.1; NM_016527.3. [Q9NYQ3-1]
DR AlphaFoldDB; Q9NYQ3; -.
DR SMR; Q9NYQ3; -.
DR BioGRID; 119356; 28.
DR IntAct; Q9NYQ3; 26.
DR STRING; 9606.ENSP00000483507; -.
DR BindingDB; Q9NYQ3; -.
DR ChEMBL; CHEMBL2169732; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR iPTMnet; Q9NYQ3; -.
DR PhosphoSitePlus; Q9NYQ3; -.
DR BioMuta; HAO2; -.
DR DMDM; 13124287; -.
DR MassIVE; Q9NYQ3; -.
DR PaxDb; Q9NYQ3; -.
DR PeptideAtlas; Q9NYQ3; -.
DR PRIDE; Q9NYQ3; -.
DR ProteomicsDB; 83262; -. [Q9NYQ3-1]
DR Antibodypedia; 33905; 119 antibodies from 22 providers.
DR DNASU; 51179; -.
DR Ensembl; ENST00000325945.4; ENSP00000316339.3; ENSG00000116882.15. [Q9NYQ3-1]
DR Ensembl; ENST00000361035.8; ENSP00000354314.4; ENSG00000116882.15. [Q9NYQ3-2]
DR Ensembl; ENST00000622548.4; ENSP00000483507.1; ENSG00000116882.15. [Q9NYQ3-1]
DR GeneID; 51179; -.
DR KEGG; hsa:51179; -.
DR MANE-Select; ENST00000325945.4; ENSP00000316339.3; NM_016527.4; NP_057611.1.
DR UCSC; uc001ehq.1; human. [Q9NYQ3-1]
DR CTD; 51179; -.
DR DisGeNET; 51179; -.
DR GeneCards; HAO2; -.
DR HGNC; HGNC:4810; HAO2.
DR HPA; ENSG00000116882; Group enriched (kidney, liver).
DR MIM; 605176; gene.
DR neXtProt; NX_Q9NYQ3; -.
DR OpenTargets; ENSG00000116882; -.
DR PharmGKB; PA29186; -.
DR VEuPathDB; HostDB:ENSG00000116882; -.
DR eggNOG; KOG0538; Eukaryota.
DR GeneTree; ENSGT00390000018717; -.
DR HOGENOM; CLU_020639_0_0_1; -.
DR InParanoid; Q9NYQ3; -.
DR OMA; FQYEIYL; -.
DR PhylomeDB; Q9NYQ3; -.
DR TreeFam; TF313363; -.
DR BRENDA; 1.1.3.15; 2681.
DR PathwayCommons; Q9NYQ3; -.
DR Reactome; R-HSA-390918; Peroxisomal lipid metabolism.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; Q9NYQ3; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 51179; 30 hits in 1070 CRISPR screens.
DR ChiTaRS; HAO2; human.
DR GenomeRNAi; 51179; -.
DR Pharos; Q9NYQ3; Tchem.
DR PRO; PR:Q9NYQ3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NYQ3; protein.
DR Bgee; ENSG00000116882; Expressed in right lobe of liver and 108 other tissues.
DR ExpressionAtlas; Q9NYQ3; baseline and differential.
DR Genevisible; Q9NYQ3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0019395; P:fatty acid oxidation; IDA:UniProtKB.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Fatty acid metabolism; Flavoprotein; FMN;
KW Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..351
FT /note="2-Hydroxyacid oxidase 2"
FT /id="PRO_0000206320"
FT DOMAIN 2..351
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT MOTIF 349..351
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 77..79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 130
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 165
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 222
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 249
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 277..281
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 300..301
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MEDKMWSECEGPEM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055095"
FT VARIANT 15
FT /note="E -> K (in dbSNP:rs34638261)"
FT /id="VAR_049087"
FT VARIANT 221
FT /note="L -> M (in dbSNP:rs6661625)"
FT /id="VAR_049088"
FT CONFLICT 80
FT /note="F -> Y (in Ref. 2; AAF14000)"
FT /evidence="ECO:0000305"
FT CONFLICT 292..294
FT /note="LGA -> HED (in Ref. 2; AAF14000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 38839 MW; 7330DE44E282947D CRC64;
MSLVCLTDFQ AHAREQLSKS TRDFIEGGAD DSITRDDNIA AFKRIRLRPR YLRDVSEVDT
RTTIQGEEIS APICIAPTGF HCLVWPDGEM STARAAQAAG ICYITSTFAS CSLEDIVIAA
PEGLRWFQLY VHPDLQLNKQ LIQRVESLGF KALVITLDTP VCGNRRHDIR NQLRRNLTLT
DLQSPKKGNA IPYFQMTPIS TSLCWNDLSW FQSITRLPII LKGILTKEDA ELAVKHNVQG
IIVSNHGGRQ LDEVLASIDA LTEVVAAVKG KIEVYLDGGV RTGNDVLKAL ALGAKCIFLG
RPILWGLACK GEHGVKEVLN ILTNEFHTSM ALTGCRSVAE INRNLVQFSR L
