SIAE_HUMAN
ID SIAE_HUMAN Reviewed; 523 AA.
AC Q9HAT2; B3KPB0; Q8IUT9; Q9HAU7; Q9NT71;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Sialate O-acetylesterase;
DE EC=3.1.1.53;
DE AltName: Full=H-Lse;
DE AltName: Full=Sialic acid-specific 9-O-acetylesterase;
DE Flags: Precursor;
GN Name=SIAE; Synonyms=YSG2;
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 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15292578; DOI=10.1155/s1110724304307084;
RA Zhu H., Chan H.C., Zhou Z., Li J.M., Zhu H., Yin L., Xu M., Cheng L.,
RA Sha J.H.;
RT "A gene encoding sialic-acid-specific 9-O-acetylesterase found in human
RT adult testis.";
RL J. Biomed. Biotechnol. 2004:130-136(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-523 (ISOFORM 1).
RC TISSUE=Amygdala;
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-401 AND ASN-422.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP SUBCELLULAR LOCATION, VARIANTS AIS6 PHE-196; ARG-212; TRP-230; GLY-266;
RP PRO-309; CYS-349; HIS-393; SER-404 AND CYS-479, VARIANTS GLY-3; SER-33;
RP HIS-62; SER-64; ARG-71; VAL-89; LYS-161; MET-312; HIS-314; ASN-400;
RP ARG-447; ILE-456 AND ARG-462, CHARACTERIZATION OF VARIANTS AIS6 PHE-196;
RP ARG-212; TRP-230; GLY-266; PRO-309; CYS-349; HIS-393; SER-404 AND CYS-479,
RP AND CHARACTERIZATION OF VARIANTS GLY-3; SER-33; HIS-62; SER-64; VAL-89;
RP LYS-161; MET-312; HIS-314; ASN-400; ARG-447; ILE-456 AND ARG-462.
RX PubMed=20555325; DOI=10.1038/nature09115;
RA Surolia I., Pirnie S.P., Chellappa V., Taylor K.N., Cariappa A., Moya J.,
RA Liu H., Bell D.W., Driscoll D.R., Diederichs S., Haider K., Netravali I.,
RA Le S., Elia R., Dow E., Lee A., Freudenberg J., De Jager P.L., Chretien Y.,
RA Varki A., Macdonald M.E., Gillis T., Behrens T.W., Bloch D., Collier D.,
RA Korzenik J., Podolsky D.K., Hafler D., Murali M., Sands B., Stone J.H.,
RA Gregersen P.K., Pillai S.;
RT "Functionally defective germline variants of sialic acid acetylesterase in
RT autoimmunity.";
RL Nature 466:243-247(2010).
RN [8]
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 removal of O-acetyl ester groups from position
CC 9 of the parent sialic acid, N-acetylneuraminic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-4-O-acetylneuraminate = acetate + H(+) + N-
CC acetylneuraminate; Xref=Rhea:RHEA:25564, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29006, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35418; EC=3.1.1.53;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HAT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAT2-2; Sequence=VSP_018993;
CC -!- TISSUE SPECIFICITY: Widely expressed with high expression in the
CC testis, prostate, and colon. {ECO:0000269|PubMed:15292578}.
CC -!- DISEASE: Autoimmune disease 6 (AIS6) [MIM:613551]: Individuals
CC manifesting susceptibility to autoimmune disease type 6 can suffer from
CC juvenile idiopathic arthritis, rheumatoid arthritis, multiple
CC sclerosis, Sjogren syndrome, systemic lupus erythematosus, type 1
CC diabetes, ulcerative colitis, and Crohn disease.
CC {ECO:0000269|PubMed:20555325}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
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DR EMBL; AF300796; AAG15386.1; -; mRNA.
DR EMBL; AF303378; AAG14897.1; -; mRNA.
DR EMBL; AK056093; BAG51622.1; -; mRNA.
DR EMBL; CH471065; EAW67591.1; -; Genomic_DNA.
DR EMBL; BC068450; AAH68450.1; -; mRNA.
DR EMBL; AL137496; CAB70771.1; -; mRNA.
DR CCDS; CCDS55795.1; -. [Q9HAT2-2]
DR CCDS; CCDS8449.1; -. [Q9HAT2-1]
DR PIR; T46250; T46250.
DR RefSeq; NP_001186851.1; NM_001199922.1. [Q9HAT2-2]
DR RefSeq; NP_733746.1; NM_170601.4. [Q9HAT2-1]
DR AlphaFoldDB; Q9HAT2; -.
DR SMR; Q9HAT2; -.
DR BioGRID; 119945; 69.
DR IntAct; Q9HAT2; 32.
DR STRING; 9606.ENSP00000263593; -.
DR ChEMBL; CHEMBL4523459; -.
DR GlyConnect; 1742; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9HAT2; 7 sites, 4 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9HAT2; -.
DR PhosphoSitePlus; Q9HAT2; -.
DR BioMuta; SIAE; -.
DR DMDM; 74734243; -.
DR EPD; Q9HAT2; -.
DR jPOST; Q9HAT2; -.
DR MassIVE; Q9HAT2; -.
DR MaxQB; Q9HAT2; -.
DR PaxDb; Q9HAT2; -.
DR PeptideAtlas; Q9HAT2; -.
DR PRIDE; Q9HAT2; -.
DR ProteomicsDB; 81429; -. [Q9HAT2-1]
DR ProteomicsDB; 81430; -. [Q9HAT2-2]
DR Antibodypedia; 32895; 67 antibodies from 16 providers.
DR DNASU; 54414; -.
DR Ensembl; ENST00000263593.8; ENSP00000263593.3; ENSG00000110013.13. [Q9HAT2-1]
DR Ensembl; ENST00000545756.5; ENSP00000437877.1; ENSG00000110013.13. [Q9HAT2-2]
DR Ensembl; ENST00000618733.4; ENSP00000478211.1; ENSG00000110013.13. [Q9HAT2-2]
DR GeneID; 54414; -.
DR KEGG; hsa:54414; -.
DR MANE-Select; ENST00000263593.8; ENSP00000263593.3; NM_170601.5; NP_733746.1.
DR UCSC; uc001qan.4; human. [Q9HAT2-1]
DR CTD; 54414; -.
DR DisGeNET; 54414; -.
DR GeneCards; SIAE; -.
DR HGNC; HGNC:18187; SIAE.
DR HPA; ENSG00000110013; Tissue enhanced (intestine).
DR MalaCards; SIAE; -.
DR MIM; 610079; gene.
DR MIM; 613551; phenotype.
DR neXtProt; NX_Q9HAT2; -.
DR OpenTargets; ENSG00000110013; -.
DR PharmGKB; PA142670922; -.
DR VEuPathDB; HostDB:ENSG00000110013; -.
DR eggNOG; ENOG502QUKD; Eukaryota.
DR GeneTree; ENSGT00390000010608; -.
DR HOGENOM; CLU_015150_1_0_1; -.
DR InParanoid; Q9HAT2; -.
DR OMA; PCEFKAC; -.
DR OrthoDB; 745508at2759; -.
DR PhylomeDB; Q9HAT2; -.
DR TreeFam; TF328611; -.
DR BRENDA; 3.1.1.53; 2681.
DR PathwayCommons; Q9HAT2; -.
DR SignaLink; Q9HAT2; -.
DR BioGRID-ORCS; 54414; 12 hits in 1081 CRISPR screens.
DR ChiTaRS; SIAE; human.
DR GenomeRNAi; 54414; -.
DR Pharos; Q9HAT2; Tbio.
DR PRO; PR:Q9HAT2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9HAT2; protein.
DR Bgee; ENSG00000110013; Expressed in mucosa of sigmoid colon and 177 other tissues.
DR Genevisible; Q9HAT2; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0106331; F:sialate 4-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0106330; F:sialate 9-O-acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0001681; F:sialate O-acetylesterase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0002682; P:regulation of immune system process; IMP:UniProtKB.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR005181; SASA.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR039329; SIAE.
DR PANTHER; PTHR22901; PTHR22901; 1.
DR Pfam; PF03629; SASA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Glycoprotein; Hydrolase; Lysosome;
KW Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..523
FT /note="Sialate O-acetylesterase"
FT /id="PRO_0000042241"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15292578"
FT /id="VSP_018993"
FT VARIANT 3
FT /note="A -> G (rare variant found in a patient with Crohn
FT disease; probably not involved in disease susceptibility;
FT the mutant enzyme has normal activity and is normally
FT secreted; dbSNP:rs144571829)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064438"
FT VARIANT 33
FT /note="N -> S (rare variant found in a patient with
FT rheumatoid arthritis; probably not involved in disease
FT susceptibility; the mutant enzyme has normal activity and
FT is normally secreted; dbSNP:rs762824510)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064439"
FT VARIANT 62
FT /note="R -> H (the mutant enzyme has normal activity and is
FT normally secreted; dbSNP:rs377634657)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064440"
FT VARIANT 64
FT /note="G -> S (the mutant enzyme has normal activity and is
FT normally secreted; dbSNP:rs76655561)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064441"
FT VARIANT 71
FT /note="K -> R (in dbSNP:rs12282107)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_051356"
FT VARIANT 89
FT /note="M -> V (at homozygosity may predispose to
FT autoimmunity; normal enzyme activity; dbSNP:rs78778622)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064442"
FT VARIANT 161
FT /note="Q -> K (the mutant enzyme has normal activity and is
FT normally secreted; dbSNP:rs200739060)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064443"
FT VARIANT 196
FT /note="C -> F (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs143070599)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064444"
FT VARIANT 212
FT /note="G -> R (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs149466359)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064445"
FT VARIANT 230
FT /note="R -> W (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs200862001)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064446"
FT VARIANT 266
FT /note="C -> G (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs746914032)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064447"
FT VARIANT 309
FT /note="Q -> P (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs757586703)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064448"
FT VARIANT 312
FT /note="T -> M (may predispose to autoimmunity; defective
FT enzyme secretion and activity; dbSNP:rs144510878)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064449"
FT VARIANT 314
FT /note="R -> H (defective enzyme secretion and activity;
FT dbSNP:rs147649509)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064450"
FT VARIANT 349
FT /note="Y -> C (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs749579541)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064451"
FT VARIANT 393
FT /note="R -> H (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs552372846)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064452"
FT VARIANT 400
FT /note="K -> N (rare variant found in a patient with Crohn
FT disease; probably not involved in disease susceptibility;
FT the mutant protein has normal activity; dbSNP:rs766047951)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064453"
FT VARIANT 404
FT /note="F -> S (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs201877149)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064454"
FT VARIANT 447
FT /note="H -> R (the mutant enzyme has normal activity and is
FT normally secreted; dbSNP:rs147161431)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064455"
FT VARIANT 456
FT /note="M -> I (the mutant enzyme has normal activity and is
FT normally secreted)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064456"
FT VARIANT 462
FT /note="Q -> R (the mutant enzyme has normal activity and is
FT normally secreted; dbSNP:rs143668140)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064457"
FT VARIANT 467
FT /note="A -> V (in dbSNP:rs7941523)"
FT /id="VAR_051357"
FT VARIANT 479
FT /note="R -> C (in AIS6; defective enzyme secretion and
FT activity; dbSNP:rs376857712)"
FT /evidence="ECO:0000269|PubMed:20555325"
FT /id="VAR_064458"
SQ SEQUENCE 523 AA; 58315 MW; B72CF69636DBFED8 CRC64;
MVAPGLVLGL VLPLILWADR SAGIGFRFAS YINNDMVLQK EPAGAVIWGF GTPGATVTVT
LRQGQETIMK KVTSVKAHSD TWMVVLDPMK PGGPFEVMAQ QTLEKINFTL RVHDVLFGDV
WLCSGQSNMQ MTVLQIFNAT RELSNTAAYQ SVRILSVSPI QAEQELEDLV AVDLQWSKPT
SENLGHGYFK YMSAVCWLFG RHLYDTLQYP IGLIASSWGG TPIEAWSSGR SLKACGVPKQ
GSIPYDSVTG PSKHSVLWNA MIHPLCNMTL KGVVWYQGES NINYNTDLYN CTFPALIEDW
RETFHRGSQG QTERFFPFGL VQLSSDLSKK SSDDGFPQIR WHQTADFGYV PNPKMPNTFM
AVAMDLCDRD SPFGSIHPRD KQTVAYRLHL GARALAYGEK NLTFEGPLPE KIELLAHKGL
LNLTYYQQIQ VQKKDNKIFE ISCCSDHRCK WLPASMNTVS TQSLTLAIDS CHGTVVALRY
AWTTWPCEYK QCPLYHPSSA LPAPPFIAFI TDQGPGHQSN VAK
