QSOX2_HUMAN
ID QSOX2_HUMAN Reviewed; 698 AA.
AC Q6ZRP7; A2CEE0; A6NLB0; Q5TB37; Q7Z7B6; Q86VV7; Q8N3G2;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Sulfhydryl oxidase 2;
DE EC=1.8.3.2;
DE AltName: Full=Neuroblastoma-derived sulfhydryl oxidase;
DE AltName: Full=Quiescin Q6-like protein 1;
DE Flags: Precursor;
GN Name=QSOX2; Synonyms=QSCN6L1, SOXN;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14633699;
RA Wittke I., Wiedemeyer R., Pillmann A., Savelyeva L., Westermann F.,
RA Schwab M.;
RT "Neuroblastoma-derived sulfhydryl oxidase, a new member of the sulfhydryl
RT oxidase/quiescin 6 family, regulates sensitization to interferon gamma-
RT induced cell death in human neuroblastoma cells.";
RL Cancer Res. 63:7742-7752(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-698.
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-698.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP IDENTIFICATION BY 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: Catalyzes the oxidation of sulfhydryl groups in peptide and
CC protein thiols to disulfides with the reduction of oxygen to hydrogen
CC peroxide. May contribute to disulfide bond formation in a variety of
CC secreted proteins. Also seems to play a role in regulating the
CC sensitization of neuroblastoma cells for interferon-gamma-induced
CC apoptosis. {ECO:0000269|PubMed:14633699}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O00391};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O00391};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14633699}; Single-
CC pass membrane protein {ECO:0000269|PubMed:14633699}. Secreted
CC {ECO:0000269|PubMed:14633699}. Cell membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}. Note=Seems to be predominantly
CC targeted to the nuclear and outer plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, brain, placenta, kidney,
CC heart and fetal tissues. Weakly expressed in lung, liver and skeletal
CC muscles. {ECO:0000269|PubMed:14633699}.
CC -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC87262.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC85331.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ318051; CAC85331.1; ALT_FRAME; mRNA.
DR EMBL; AL138781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR392000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK128077; BAC87262.1; ALT_INIT; mRNA.
DR EMBL; AL834369; CAD39032.1; -; mRNA.
DR CCDS; CCDS35178.1; -.
DR RefSeq; NP_859052.3; NM_181701.3.
DR AlphaFoldDB; Q6ZRP7; -.
DR SMR; Q6ZRP7; -.
DR BioGRID; 127987; 87.
DR IntAct; Q6ZRP7; 25.
DR STRING; 9606.ENSP00000351536; -.
DR GlyGen; Q6ZRP7; 7 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q6ZRP7; -.
DR PhosphoSitePlus; Q6ZRP7; -.
DR BioMuta; QSOX2; -.
DR DMDM; 158958335; -.
DR EPD; Q6ZRP7; -.
DR jPOST; Q6ZRP7; -.
DR MassIVE; Q6ZRP7; -.
DR MaxQB; Q6ZRP7; -.
DR PaxDb; Q6ZRP7; -.
DR PeptideAtlas; Q6ZRP7; -.
DR PRIDE; Q6ZRP7; -.
DR ProteomicsDB; 68152; -.
DR Antibodypedia; 2576; 113 antibodies from 19 providers.
DR DNASU; 169714; -.
DR Ensembl; ENST00000358701.10; ENSP00000351536.5; ENSG00000165661.17.
DR GeneID; 169714; -.
DR KEGG; hsa:169714; -.
DR MANE-Select; ENST00000358701.10; ENSP00000351536.5; NM_181701.4; NP_859052.3.
DR UCSC; uc010nbi.4; human.
DR CTD; 169714; -.
DR DisGeNET; 169714; -.
DR GeneCards; QSOX2; -.
DR HGNC; HGNC:30249; QSOX2.
DR HPA; ENSG00000165661; Low tissue specificity.
DR MIM; 612860; gene.
DR neXtProt; NX_Q6ZRP7; -.
DR OpenTargets; ENSG00000165661; -.
DR PharmGKB; PA162400588; -.
DR VEuPathDB; HostDB:ENSG00000165661; -.
DR eggNOG; KOG1731; Eukaryota.
DR GeneTree; ENSGT00940000159734; -.
DR HOGENOM; CLU_020182_1_0_1; -.
DR InParanoid; Q6ZRP7; -.
DR OMA; RHLNPKF; -.
DR OrthoDB; 498515at2759; -.
DR PhylomeDB; Q6ZRP7; -.
DR TreeFam; TF316749; -.
DR BRENDA; 1.8.3.2; 2681.
DR PathwayCommons; Q6ZRP7; -.
DR SignaLink; Q6ZRP7; -.
DR SIGNOR; Q6ZRP7; -.
DR BioGRID-ORCS; 169714; 10 hits in 1089 CRISPR screens.
DR ChiTaRS; QSOX2; human.
DR GenomeRNAi; 169714; -.
DR Pharos; Q6ZRP7; Tbio.
DR PRO; PR:Q6ZRP7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q6ZRP7; protein.
DR Bgee; ENSG00000165661; Expressed in secondary oocyte and 142 other tissues.
DR ExpressionAtlas; Q6ZRP7; baseline and differential.
DR Genevisible; Q6ZRP7; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.20.120.1960; -; 1.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR InterPro; IPR040986; QSOX_FAD-bd_dom.
DR InterPro; IPR042568; QSOX_FAD-bd_sf.
DR InterPro; IPR041269; QSOX_Trx1.
DR InterPro; IPR039798; Sulfhydryl_oxidase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR22897; PTHR22897; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR Pfam; PF18371; FAD_SOX; 1.
DR Pfam; PF18108; QSOX_Trx1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; FAD; Flavoprotein; Glycoprotein; Membrane;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..698
FT /note="Sulfhydryl oxidase 2"
FT /id="PRO_0000249538"
FT TRANSMEM 662..682
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 34..178
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 421..530
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT REGION 570..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 94
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 433
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 437
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 478
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 482
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 505..512
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 527
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 530
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..94
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 122..131
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT DISULFID 418..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 476..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 536..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT VARIANT 126
FT /note="K -> E (in dbSNP:rs12380852)"
FT /id="VAR_027435"
FT CONFLICT 96
FT /note="G -> A (in Ref. 1; CAC85331)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="N -> K (in Ref. 3; BAC87262)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="R -> W (in Ref. 1; CAC85331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 77529 MW; 7F2B3F890AE657CF CRC64;
MAAAGAAVAR SPGIGAGPAL RARRSPPPRA ARLPRLLVLL AAAAVGPGAG GAARLYRAGE
DAVWVLDSGS VRGATANSSA AWLVQFYSSW CGHCIGYAPT WRALAGDVRD WASAIRVAAL
DCMEEKNQAV CHDYDIHFYP TFRYFKAFTK EFTTGENFKG PDRELRTVRQ TMIDFLQNHT
EGSRPPACPR LDPIQPSDVL SLLDNRGSHY VAIVFESNSS YLGREVILDL IPYESIVVTR
ALDGDKAFLE KLGVSSVPSC YLIYPNGSHG LINVVKPLRA FFSSYLKSLP DVRKKSLPLP
EKPHKEENSE IVVWREFDKS KLYTVDLESG LHYLLRVELA AHKSLAGAEL KTLKDFVTVL
AKLFPGRPPV KKLLEMLQEW LASLPLDRIP YNAVLDLVNN KMRISGIFLT NHIKWVGCQG
SRSELRGYPC SLWKLFHTLT VEASTHPDAL VGTGFEDDPQ AVLQTMRRYV HTFFGCKECG
EHFEEMAKES MDSVKTPDQA ILWLWKKHNM VNGRLAGHLS EDPRFPKLQW PTPDLCPACH
EEIKGLASWD EGHVLTFLKQ HYGRDNLLDT YSADQGDSSE GGTLARGEEE EKRLTPPEVS
HGDRDTQSVR PPGALGPRPA LPESLHHSLD GKLQSLDGPG AHKEVGGAAP FLGVDFSSLD
MSLCVVLYVA SSLFLMVMYF FFRVRSRRWK VKHHHPAV
