SIGL6_HUMAN
ID SIGL6_HUMAN Reviewed; 453 AA.
AC O43699; A8MV71; B2RTS8; C9JBE5; F8WA78; O15388; O43700;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Sialic acid-binding Ig-like lectin 6;
DE Short=Siglec-6;
DE AltName: Full=CD33 antigen-like 1;
DE AltName: Full=CDw327;
DE AltName: Full=Obesity-binding protein 1;
DE Short=OB-BP1;
DE AltName: CD_antigen=CD327;
DE Flags: Precursor;
GN Name=SIGLEC6; Synonyms=CD33L, CD33L1, OBBP1;
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).
RC TISSUE=Placenta;
RX PubMed=9465907; DOI=10.1159/000134676;
RA Takei Y., Sasaki S., Fujiwara T., Takahashi E., Muto T., Nakamura Y.;
RT "Molecular cloning of a novel gene similar to myeloid antigen CD33 and its
RT specific expression in placenta.";
RL Cytogenet. Cell Genet. 78:295-300(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), AND VARIANT
RP VAL-57.
RC TISSUE=Placenta;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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 [MRNA] OF 3-453 (ISOFORM 1), AND INTERACTION WITH LEP.
RC TISSUE=Erythroleukemia;
RX PubMed=10428856; DOI=10.1074/jbc.274.32.22729;
RA Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C.,
RA Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F.,
RA Varki A., Kastelein R.A.;
RT "OB-BP1/Siglec-6. A leptin- and sialic acid-binding protein of the
RT immunoglobulin superfamily.";
RL J. Biol. Chem. 274:22729-22738(1999).
RN [6]
RP ERRATUM OF PUBMED:10428856.
RA Patel N., Brinkman-Van der Linden E.C.M., Altmann S.W., Gish K.C.,
RA Balasubramanian S., Timans J.C., Peterson D., Bell M.P., Bazan J.F.,
RA Varki A., Kastelein R.A.;
RL J. Biol. Chem. 274:28058-28058(1999).
CC -!- FUNCTION: Putative adhesion molecule that mediates sialic-acid
CC dependent binding to cells. Binds to alpha-2,6-linked sialic acid. The
CC sialic acid recognition site may be masked by cis interactions with
CC sialic acids on the same cell surface.
CC -!- SUBUNIT: Interacts with LEP. {ECO:0000269|PubMed:10428856}.
CC -!- INTERACTION:
CC O43699; Q14192: FHL2; NbExp=3; IntAct=EBI-2814604, EBI-701903;
CC O43699; P15884: TCF4; NbExp=3; IntAct=EBI-2814604, EBI-533224;
CC O43699-3; Q13021: MALL; NbExp=3; IntAct=EBI-12161783, EBI-750078;
CC O43699-3; P26367: PAX6; NbExp=3; IntAct=EBI-12161783, EBI-747278;
CC O43699-3; O00206: TLR4; NbExp=2; IntAct=EBI-12161783, EBI-528701;
CC O43699-3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-12161783, EBI-625509;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Membrane-bound, CD33L1;
CC IsoId=O43699-1; Sequence=Displayed;
CC Name=2; Synonyms=Secreted, CD33L2;
CC IsoId=O43699-2; Sequence=VSP_002553, VSP_002554;
CC Name=3;
CC IsoId=O43699-3; Sequence=VSP_035812;
CC Name=4;
CC IsoId=O43699-4; Sequence=VSP_035811, VSP_002553, VSP_002554;
CC Name=5;
CC IsoId=O43699-5; Sequence=VSP_045387, VSP_045388;
CC Name=6;
CC IsoId=O43699-6; Sequence=VSP_046070, VSP_035812;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in placenta (cyto- and
CC syncytiotrophoblastic cells) and at lower levels in spleen, peripheral
CC blood leukocytes (predominantly B-cells) and small intestine.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- MISCELLANEOUS: [Isoform 2]: Should not be confused with SIGLEC5 which
CC has been called CD33L2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH35359.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI40799.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA24983.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA24984.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-6;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_273";
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; D86358; BAA24983.1; ALT_INIT; mRNA.
DR EMBL; D86359; BAA24984.1; ALT_INIT; mRNA.
DR EMBL; AK300170; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK300182; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC020914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035359; AAH35359.2; ALT_INIT; mRNA.
DR EMBL; BC140798; AAI40799.1; ALT_INIT; mRNA.
DR EMBL; U71382; AAB70702.1; ALT_INIT; mRNA.
DR CCDS; CCDS12834.3; -. [O43699-1]
DR CCDS; CCDS12835.3; -. [O43699-3]
DR CCDS; CCDS12836.3; -. [O43699-2]
DR CCDS; CCDS54307.1; -. [O43699-6]
DR CCDS; CCDS54308.1; -. [O43699-5]
DR CCDS; CCDS59417.1; -. [O43699-4]
DR RefSeq; NP_001171018.1; NM_001177547.2. [O43699-6]
DR RefSeq; NP_001171019.1; NM_001177548.2. [O43699-5]
DR RefSeq; NP_001171020.1; NM_001177549.2. [O43699-4]
DR RefSeq; NP_001236.4; NM_001245.6. [O43699-1]
DR RefSeq; NP_942142.3; NM_198845.5. [O43699-3]
DR RefSeq; NP_942143.3; NM_198846.5. [O43699-2]
DR AlphaFoldDB; O43699; -.
DR SMR; O43699; -.
DR BioGRID; 107384; 7.
DR IntAct; O43699; 14.
DR STRING; 9606.ENSP00000401502; -.
DR GlyGen; O43699; 5 sites.
DR iPTMnet; O43699; -.
DR PhosphoSitePlus; O43699; -.
DR BioMuta; SIGLEC6; -.
DR MassIVE; O43699; -.
DR PaxDb; O43699; -.
DR PeptideAtlas; O43699; -.
DR PRIDE; O43699; -.
DR ProteomicsDB; 30448; -.
DR ProteomicsDB; 49120; -. [O43699-1]
DR ProteomicsDB; 49121; -. [O43699-2]
DR ProteomicsDB; 49122; -. [O43699-3]
DR ProteomicsDB; 49123; -. [O43699-4]
DR ProteomicsDB; 9453; -.
DR Antibodypedia; 2300; 385 antibodies from 34 providers.
DR DNASU; 946; -.
DR Ensembl; ENST00000343300.8; ENSP00000345907.4; ENSG00000105492.16. [O43699-2]
DR Ensembl; ENST00000346477.7; ENSP00000344064.4; ENSG00000105492.16. [O43699-3]
DR Ensembl; ENST00000359982.8; ENSP00000353071.4; ENSG00000105492.16. [O43699-5]
DR Ensembl; ENST00000391797.3; ENSP00000375674.3; ENSG00000105492.16. [O43699-4]
DR Ensembl; ENST00000425629.8; ENSP00000401502.2; ENSG00000105492.16. [O43699-1]
DR Ensembl; ENST00000436458.5; ENSP00000410679.1; ENSG00000105492.16. [O43699-6]
DR GeneID; 946; -.
DR KEGG; hsa:946; -.
DR MANE-Select; ENST00000425629.8; ENSP00000401502.2; NM_001245.7; NP_001236.4.
DR UCSC; uc002pwy.4; human. [O43699-1]
DR CTD; 946; -.
DR DisGeNET; 946; -.
DR GeneCards; SIGLEC6; -.
DR HGNC; HGNC:10875; SIGLEC6.
DR HPA; ENSG00000105492; Tissue enriched (placenta).
DR MIM; 604405; gene.
DR neXtProt; NX_O43699; -.
DR OpenTargets; ENSG00000105492; -.
DR PharmGKB; PA35776; -.
DR VEuPathDB; HostDB:ENSG00000105492; -.
DR eggNOG; ENOG502S41V; Eukaryota.
DR GeneTree; ENSGT01040000240469; -.
DR HOGENOM; CLU_024444_6_1_1; -.
DR InParanoid; O43699; -.
DR OMA; HYAFLQF; -.
DR OrthoDB; 416689at2759; -.
DR PhylomeDB; O43699; -.
DR TreeFam; TF332441; -.
DR PathwayCommons; O43699; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; O43699; -.
DR BioGRID-ORCS; 946; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; SIGLEC6; human.
DR GenomeRNAi; 946; -.
DR Pharos; O43699; Tbio.
DR PRO; PR:O43699; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43699; protein.
DR Bgee; ENSG00000105492; Expressed in buccal mucosa cell and 95 other tissues.
DR ExpressionAtlas; O43699; baseline and differential.
DR Genevisible; O43699; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Lectin; Membrane; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..453
FT /note="Sialic acid-binding Ig-like lectin 6"
FT /id="PRO_0000014946"
FT TOPO_DOM 27..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..123
FT /note="Ig-like V-type"
FT DOMAIN 148..231
FT /note="Ig-like C2-type 1"
FT DOMAIN 238..333
FT /note="Ig-like C2-type 2"
FT MOTIF 424..429
FT /note="ITIM motif"
FT MOTIF 444..449
FT /note="SLAM-like motif"
FT BINDING 122
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 51..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 166..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 274..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 23..58
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046070"
FT VAR_SEQ 143..153
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035811"
FT VAR_SEQ 236..252
FT /note="YAPQKVAISIFQGNSAA -> S (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035812"
FT VAR_SEQ 236
FT /note="Y -> WMLRRPPLSTPD (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045387"
FT VAR_SEQ 339..391
FT /note="KPEGRAGGVLGAVWGASITTLVFLCVCFIFRVKTRRKKAAQPVQNTDDVNPV
FT M -> SSAPVPDRHSFRPPC (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9465907"
FT /id="VSP_002553"
FT VAR_SEQ 371..453
FT /note="KTRRKKAAQPVQNTDDVNPVMVSGSRGHQHQFQTGIVSDHPAEAGPISEDEQ
FT ELHYAVLHFHKVQPQEPKVTDTEYSEIKIHK -> ISTSSRQA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045388"
FT VAR_SEQ 392..453
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9465907"
FT /id="VSP_002554"
FT VARIANT 57
FT /note="L -> V (in dbSNP:rs2305773)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_014252"
FT VARIANT 262
FT /note="L -> F (in dbSNP:rs2005199)"
FT /id="VAR_014253"
FT CONFLICT 6
FT /note="E -> K (in Ref. 1; BAA24983/BAA24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..138
FT /note="LS -> IY (in Ref. 5; AAB70702)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..161
FT /note="TLESGHP -> PGVWPS (in Ref. 5; AAB70702)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="M -> T (in Ref. 2; AK300170)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="TS -> HL (in Ref. 5; AAB70702)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..206
FT /note="RP -> A (in Ref. 5; AAB70702)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="P -> L (in Ref. 2; AK300170)"
FT /evidence="ECO:0000305"
FT CONFLICT O43699-5:246
FT /note="P -> S (in Ref. 5; AK300182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 49913 MW; 9DD7FBD8F059E452 CRC64;
MQGAQEASAS EMLPLLLPLL WAGALAQERR FQLEGPESLT VQEGLCVLVP CRLPTTLPAS
YYGYGYWFLE GADVPVATND PDEEVQEETR GRFHLLWDPR RKNCSLSIRD ARRRDNAAYF
FRLKSKWMKY GYTSSKLSVR VMALTHRPNI SIPGTLESGH PSNLTCSVPW VCEQGTPPIF
SWMSAAPTSL GPRTTQSSVL TITPRPQDHS TNLTCQVTFP GAGVTMERTI QLNVSYAPQK
VAISIFQGNS AAFKILQNTS SLPVLEGQAL RLLCDADGNP PAHLSWFQGF PALNATPISN
TGVLELPQVG SAEEGDFTCR AQHPLGSLQI SLSLFVHWKP EGRAGGVLGA VWGASITTLV
FLCVCFIFRV KTRRKKAAQP VQNTDDVNPV MVSGSRGHQH QFQTGIVSDH PAEAGPISED
EQELHYAVLH FHKVQPQEPK VTDTEYSEIK IHK