AOC2_HUMAN
ID AOC2_HUMAN Reviewed; 756 AA.
AC O75106; A5PKW2; O00120; O75105; Q4TTW5; Q9UNY0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Retina-specific copper amine oxidase;
DE Short=RAO;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P19801};
DE AltName: Full=Amine oxidase [copper-containing];
DE AltName: Full=Semicarbazide-sensitive amine oxidase;
DE Short=SSAO;
DE Flags: Precursor;
GN Name=AOC2;
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 2).
RC TISSUE=Retina;
RX PubMed=9119395; DOI=10.1006/geno.1996.4570;
RA Imamura Y., Kubota R., Wang Y., Asakawa S., Kudoh J., Mashima Y.,
RA Oguchi Y., Shimizu N.;
RT "Human retina-specific amine oxidase (RAO): cDNA cloning, tissue
RT expression, and chromosomal mapping.";
RL Genomics 40:277-283(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=9722954; DOI=10.1006/geno.1998.5357;
RA Imamura Y., Noda S., Mashima Y., Kudoh J., Oguchi Y., Shimizu N.;
RT "Human retina-specific amine oxidase: genomic structure of the gene (AOC2),
RT alternatively spliced variant, and mRNA expression in retina.";
RL Genomics 51:293-298(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RA Zhang X., McIntire W.S.;
RT "Human copper-containing amine oxidases.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-5; CYS-22; LEU-141;
RP GLN-273 AND ASP-427.
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(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).
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 TISSUE SPECIFICITY.
RX PubMed=12755418; DOI=10.1007/s000110300061;
RA Heniquez A., Meissonnier G., Visentin V., Prevot D., Carpene C.;
RT "High expression of semicarbazide-sensitive amine oxidase genes AOC2 and
RT AOC3, but not the diamine oxidase gene AOC1 in human adipocytes.";
RL Inflamm. Res. 52:S74-S75(2003).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17400359; DOI=10.1016/j.biochi.2007.02.013;
RA Bour S., Daviaud D., Gres S., Lefort C., Prevot D., Zorzano A.,
RA Wabitsch M., Saulnier-Blache J.-S., Valet P., Carpene C.;
RT "Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and
RT monoamine oxidase in human adipocytes.";
RL Biochimie 89:916-925(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19588076; DOI=10.1007/s00018-009-0076-5;
RA Kaitaniemi S., Elovaara H., Groen K., Kidron H., Liukkonen J., Salminen T.,
RA Salmi M., Jalkanen S., Elima K.;
RT "The unique substrate specificity of human AOC2, a semicarbazide-sensitive
RT amine oxidase.";
RL Cell. Mol. Life Sci. 66:2743-2757(2009).
CC -!- FUNCTION: Has a monoamine oxidase activity with substrate specificity
CC for 2-phenylethylamine and tryptamine. May play a role in adipogenesis.
CC May be a critical modulator of signal transmission in retina.
CC {ECO:0000269|PubMed:17400359, ECO:0000269|PubMed:19588076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P19801};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P19801};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P19801};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.056 mM for tryptamine {ECO:0000269|PubMed:19588076};
CC KM=0.077 mM for 2-phenylethylamine {ECO:0000269|PubMed:19588076};
CC KM=0.167 mM for benzylamine {ECO:0000269|PubMed:19588076};
CC KM=0.178 mM for p-tyramine {ECO:0000269|PubMed:19588076};
CC KM=1.7 mM for methylamine {ECO:0000269|PubMed:19588076};
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a
CC heterodimer with AOC3, in vitro. {ECO:0000250|UniProtKB:P19801,
CC ECO:0000269|PubMed:19588076}.
CC -!- INTERACTION:
CC O75106; Q13520: AQP6; NbExp=3; IntAct=EBI-17685278, EBI-13059134;
CC O75106; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-17685278, EBI-781551;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:19588076}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19588076}. Note=Present on the surface of the
CC cells. {ECO:0000269|PubMed:19588076}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:19588076}. Note=Either not translocated to the
CC plasma membrane or below detection level.
CC {ECO:0000269|PubMed:19588076}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Long;
CC IsoId=O75106-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=O75106-2; Sequence=VSP_006549;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues with much higher
CC expression in retina. Isoform 1 and isoform 2 are expressed in adipose
CC tissue, whereas isoform 1 only seems to be present in thymus, and
CC isoform 2 only in testis. {ECO:0000269|PubMed:12755418,
CC ECO:0000269|PubMed:17400359, ECO:0000269|PubMed:19588076}.
CC -!- INDUCTION: Up-regulated during in vitro adipocyte differentiation.
CC {ECO:0000269|PubMed:17400359}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/aoc2/";
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DR EMBL; D88213; BAA19001.1; -; mRNA.
DR EMBL; AB012943; BAA32590.1; -; Genomic_DNA.
DR EMBL; AB012943; BAA32589.1; -; Genomic_DNA.
DR EMBL; AF081363; AAD39345.1; -; mRNA.
DR EMBL; DQ060035; AAY43129.1; -; Genomic_DNA.
DR EMBL; AC016889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60895.1; -; Genomic_DNA.
DR EMBL; BC142641; AAI42642.1; -; mRNA.
DR CCDS; CCDS11443.1; -. [O75106-1]
DR CCDS; CCDS45690.1; -. [O75106-2]
DR RefSeq; NP_001149.2; NM_001158.4. [O75106-2]
DR RefSeq; NP_033720.2; NM_009590.3. [O75106-1]
DR AlphaFoldDB; O75106; -.
DR SMR; O75106; -.
DR BioGRID; 106811; 22.
DR IntAct; O75106; 5.
DR STRING; 9606.ENSP00000253799; -.
DR BindingDB; O75106; -.
DR ChEMBL; CHEMBL4112; -.
DR GlyConnect; 1714; 2 N-Linked glycans (1 site).
DR GlyGen; O75106; 5 sites, 2 N-linked glycans (1 site).
DR iPTMnet; O75106; -.
DR PhosphoSitePlus; O75106; -.
DR BioMuta; AOC2; -.
DR jPOST; O75106; -.
DR MassIVE; O75106; -.
DR PaxDb; O75106; -.
DR PeptideAtlas; O75106; -.
DR PRIDE; O75106; -.
DR ProteomicsDB; 49761; -. [O75106-1]
DR ProteomicsDB; 49762; -. [O75106-2]
DR Antibodypedia; 17156; 81 antibodies from 17 providers.
DR DNASU; 314; -.
DR Ensembl; ENST00000253799.8; ENSP00000253799.2; ENSG00000131480.9. [O75106-1]
DR Ensembl; ENST00000452774.2; ENSP00000406134.1; ENSG00000131480.9. [O75106-2]
DR GeneID; 314; -.
DR KEGG; hsa:314; -.
DR MANE-Select; ENST00000253799.8; ENSP00000253799.2; NM_009590.4; NP_033720.2.
DR UCSC; uc002ibt.5; human. [O75106-1]
DR CTD; 314; -.
DR DisGeNET; 314; -.
DR GeneCards; AOC2; -.
DR HGNC; HGNC:549; AOC2.
DR HPA; ENSG00000131480; Low tissue specificity.
DR MIM; 602268; gene.
DR neXtProt; NX_O75106; -.
DR OpenTargets; ENSG00000131480; -.
DR PharmGKB; PA24839; -.
DR VEuPathDB; HostDB:ENSG00000131480; -.
DR eggNOG; KOG1186; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR HOGENOM; CLU_015739_1_0_1; -.
DR InParanoid; O75106; -.
DR OMA; QDFSKFF; -.
DR OrthoDB; 1320015at2759; -.
DR PhylomeDB; O75106; -.
DR TreeFam; TF314750; -.
DR BRENDA; 1.4.3.21; 2681.
DR PathwayCommons; O75106; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; O75106; -.
DR SignaLink; O75106; -.
DR BioGRID-ORCS; 314; 13 hits in 1065 CRISPR screens.
DR GenomeRNAi; 314; -.
DR Pharos; O75106; Tchem.
DR PRO; PR:O75106; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75106; protein.
DR Bgee; ENSG00000131480; Expressed in sperm and 103 other tissues.
DR Genevisible; O75106; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR032952; AOC2.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR PANTHER; PTHR10638:SF4; PTHR10638:SF4; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Catecholamine metabolism; Cell membrane;
KW Copper; Cytoplasm; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Signal; TPQ.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..756
FT /note="Retina-specific copper amine oxidase"
FT /id="PRO_0000035671"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT ACT_SITE 465
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 378..388
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 462..467
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 516
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 518
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 525
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 526
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 527
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 568
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 574..581
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 659
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 661
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 663
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 669
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 680
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT MOD_RES 465
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 398..424
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 730..737
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 744
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT VAR_SEQ 599..625
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9119395"
FT /id="VSP_006549"
FT VARIANT 5
FT /note="I -> V (in dbSNP:rs34230945)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025022"
FT VARIANT 22
FT /note="Y -> C (in dbSNP:rs34435306)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025023"
FT VARIANT 141
FT /note="P -> L (in dbSNP:rs35833794)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025024"
FT VARIANT 273
FT /note="R -> Q (in dbSNP:rs35508987)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025025"
FT VARIANT 427
FT /note="E -> D (in dbSNP:rs34351794)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025026"
FT CONFLICT 181
FT /note="E -> D (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..218
FT /note="GDRA -> RERT (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..222
FT /note="MA -> IG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="H -> Q (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 83673 MW; 10263D8D56D3BD25 CRC64;
MHLKIVLAFL ALSLITIFAL AYVLLTSPGG SSQPPHCPSV SHRAQPWPHP GQSQLFADLS
REELTAVMRF LTQRLGPGLV DAAQAQPSDN CIFSVELQLP PKAAALAHLD RGSPPPAREA
LAIVLFGGQP QPNVSELVVG PLPHPSYMRD VTVERHGGPL PYHRRPVLRA EFTQMWRHLK
EVELPKAPIF LSSTFNYNGS TLAAVHATPR GLRSGDRATW MALYHNISGV GLFLHPVGLE
LLLDHRALDP AHWTVQQVFY LGHYYADLGQ LEREFKSGRL EVVRVPLPPP NGASSLRSRN
SPGPLPPLQF SPQGSQYSVQ GNLVVSSLWS FTFGHGVFSG LRIFDVRFQG ERIAYEVSVQ
ECVSIYGADS PKTMLTRYLD SSFGLGRNSR GLVRGVDCPY QATMVDIHIL VGKGAVQLLP
GAVCVFEEAQ GLPLRRHHNY LQNHFYGGLA SSALVVRSVS SVGNYDYIWD FVLYPNGALE
GRVHATGYIN TAFLKGGEEG LLFGNRVGER VLGTVHTHAF HFKLDLDVAG LKNWVVAEDV
VFKPVAAPWN PEHWLQRPQL TRQVLGKEDL TAFSLGSPLP RYLYLASNQT NAWGHQRGYR
IQIHSPLGIH IPLESDMERA LSWGRYQLVV TQRKEEESQS SSIYHQNDIW TPTVTFADFI
NNETLLGEDL VAWVTASFLH IPHAEDIPNT VTLGNRVGFL LRPYNFFDED PSIFSPGSVY
FEKGQDAGLC SINPVACLPD LAACVPDLPP FSYHGF
