ID LY75_HUMAN Reviewed; 1722 AA. AC O60449; O75913; Q53R46; Q53TF5; Q7Z575; Q7Z577; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 13-FEB-2019, entry version 165. DE RecName: Full=Lymphocyte antigen 75; DE Short=Ly-75; DE AltName: Full=C-type lectin domain family 13 member B; DE AltName: Full=DEC-205; DE AltName: Full=gp200-MR6; DE AltName: CD_antigen=CD205; DE Flags: Precursor; GN Name=LY75; Synonyms=CD205, CLEC13B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAC17636.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PARTIAL PROTEIN SEQUENCE, RP TISSUE SPECIFICITY, GLYCOSYLATION, AND VARIANTS ASP-268 AND GLU-807. RC TISSUE=Thymus; RX PubMed=9862343; RX DOI=10.1002/(SICI)1521-4141(199812)28:12<4071::AID-IMMU4071>3.0.CO;2-O; RA McKay P.F., Imami N., Johns M., Taylor-Fishwick D.A., Sedibane L.M., RA Totty N.F., Hsuan J.J., Palmer D.B., George A.J.T., Foxwell B.M.J., RA Ritter M.A.; RT "The gp200-MR6 molecule which is functionally associated with the IL-4 RT receptor modulates B cell phenotype and is a novel member of the human RT macrophage mannose receptor family."; RL Eur. J. Immunol. 28:4071-4083(1998). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT ASN-1321. RX PubMed=9553150; DOI=10.1007/s002510050381; RA Kato M., Neil T.K., Clark G.J., Morris C.M., Sorg R.V., Hart D.N.J.; RT "cDNA cloning of human DEC-205, a putative antigen-uptake receptor on RT dendritic cells."; RL Immunogenetics 47:442-450(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, AND RP VARIANT ASN-1321. RX PubMed=12824192; DOI=10.1074/jbc.M303112200; RA Kato M., Khan S., Gonzalez N., O'Neill B.P., McDonald K.J., RA Cooper B.J., Angel N.Z., Hart D.N.J.; RT "Hodgkin's lymphoma cell lines express a fusion protein encoded by RT intergenically spliced mRNA for the multilectin receptor DEC-205 RT (CD205) and a novel C-type lectin receptor DCL-1."; RL J. Biol. Chem. 278:34035-34041(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-933, AND IDENTIFICATION RP 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). CC -!- FUNCTION: Acts as an endocytic receptor to direct captured CC antigens from the extracellular space to a specialized antigen- CC processing compartment (By similarity). Causes reduced CC proliferation of B-lymphocytes. {ECO:0000250}. CC -!- INTERACTION: CC Q969F0:FATE1; NbExp=3; IntAct=EBI-10186753, EBI-743099; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=4; CC IsoId=O60449-1; Sequence=Displayed; CC Name=2; Synonyms=Fusion protein variant V34-2; CC IsoId=O60449-2; Sequence=VSP_020909; CC Note=Produced by intergenic splicing of LY75 and CD302.; CC Name=5; CC IsoId=Q8IX05-2; Sequence=External; CC Name=3; Synonyms=Fusion protein variant V33-2; CC IsoId=O60449-3; Sequence=VSP_020908; CC Note=Produced by intergenic splicing of LY75 and CD302.; CC Name=1; CC IsoId=Q8IX05-1; Sequence=External; CC Note=Produced by intergenic splicing of LY75 and CD302.; CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, colon and CC peripheral blood lymphocytes. Detected in myeloid and B-lymphoid CC cell lines. Isoform 2 and isoform 3 are expressed in malignant CC Hodgkin lymphoma cells called Hodgkin and Reed-Sternberg (HRS) CC cells. {ECO:0000269|PubMed:12824192, ECO:0000269|PubMed:9862343}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9862343}. CC -!- MISCELLANEOUS: Isoform 2 and isoform 3 are produced in HRS cells CC by a transcriptional control mechanism which cotranscribe an mRNA CC containing LY75 and CD302 prior to generating the intergenically CC spliced mRNA to produce LY75/CD302 fusion proteins. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=DEC-205; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_250"; 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; AF064827; AAC62622.1; -; mRNA. DR EMBL; AF011333; AAC17636.1; -; mRNA. DR EMBL; AY184222; AAN85434.1; -; mRNA. DR EMBL; AY314006; AAP79899.1; -; mRNA. DR EMBL; AC009961; AAY14943.1; -; Genomic_DNA. DR EMBL; AC093873; AAY24189.1; -; Genomic_DNA. DR CCDS; CCDS2211.1; -. [O60449-1] DR RefSeq; NP_001185688.1; NM_001198759.1. [O60449-2] DR RefSeq; NP_001185689.1; NM_001198760.1. [O60449-3] DR RefSeq; NP_002340.2; NM_002349.3. [O60449-1] DR UniGene; Hs.153563; -. DR ProteinModelPortal; O60449; -. DR IntAct; O60449; 2. DR STRING; 9606.ENSP00000451511; -. DR CarbonylDB; O60449; -. DR GlyConnect; 1472; -. DR iPTMnet; O60449; -. DR PhosphoSitePlus; O60449; -. DR BioMuta; LY75; -. DR jPOST; O60449; -. DR PaxDb; O60449; -. DR PeptideAtlas; O60449; -. DR PRIDE; O60449; -. DR ProteomicsDB; 49406; -. DR ProteomicsDB; 49407; -. [O60449-2] DR ProteomicsDB; 49408; -. [O60449-3] DR DNASU; 4065; -. DR Ensembl; ENST00000263636; ENSP00000263636; ENSG00000054219. [O60449-1] DR GeneID; 100526664; -. DR GeneID; 4065; -. DR KEGG; hsa:100526664; -. DR KEGG; hsa:4065; -. DR UCSC; uc002ubc.6; human. [O60449-1] DR CTD; 100526664; -. DR CTD; 4065; -. DR DisGeNET; 100526664; -. DR DisGeNET; 4065; -. DR EuPathDB; HostDB:ENSG00000054219.10; -. DR GeneCards; LY75; -. DR H-InvDB; HIX0024086; -. DR HGNC; HGNC:6729; LY75. DR HPA; CAB001450; -. DR HPA; HPA049108; -. DR HPA; HPA054073; -. DR MIM; 604524; gene. DR neXtProt; NX_O60449; -. DR OpenTargets; ENSG00000054219; -. DR OpenTargets; ENSG00000248672; -. DR PharmGKB; PA30493; -. DR eggNOG; KOG4297; Eukaryota. DR eggNOG; ENOG410XPJ1; LUCA. DR GeneTree; ENSGT00940000153495; -. DR HOGENOM; HOG000232050; -. DR HOVERGEN; HBG045579; -. DR InParanoid; O60449; -. DR KO; K06559; -. DR OMA; GWEWSDH; -. DR OrthoDB; 29241at2759; -. DR PhylomeDB; O60449; -. DR TreeFam; TF316663; -. DR GeneWiki; LY75; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000054219; Expressed in 189 organ(s), highest expression level in thymus. DR Genevisible; O60449; HS. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR CDD; cd00062; FN2; 1. DR CDD; cd00161; RICIN; 1. DR Gene3D; 2.10.10.10; -; 1. DR Gene3D; 3.10.100.10; -; 10. DR InterPro; IPR001304; C-type_lectin-like. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR018378; C-type_lectin_CS. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR000562; FN_type2_dom. DR InterPro; IPR036943; FN_type2_sf. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. DR Pfam; PF00040; fn2; 1. DR Pfam; PF00059; Lectin_C; 10. DR SMART; SM00034; CLECT; 10. DR SMART; SM00059; FN2; 1. DR SMART; SM00458; RICIN; 1. DR SUPFAM; SSF50370; SSF50370; 1. DR SUPFAM; SSF56436; SSF56436; 10. DR SUPFAM; SSF57440; SSF57440; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 10. DR PROSITE; PS00023; FN2_1; 1. DR PROSITE; PS51092; FN2_2; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Direct protein sequencing; KW Disulfide bond; Endocytosis; Glycoprotein; Lectin; Membrane; KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 27 {ECO:0000269|PubMed:9862343}. FT CHAIN 28 1722 Lymphocyte antigen 75. FT /FTId=PRO_0000017552. FT TOPO_DOM 28 1666 Extracellular. {ECO:0000255}. FT TRANSMEM 1667 1691 Helical. {ECO:0000255}. FT TOPO_DOM 1692 1722 Cytoplasmic. {ECO:0000255}. FT DOMAIN 33 156 Ricin B-type lectin. FT {ECO:0000255|PROSITE-ProRule:PRU00174}. FT DOMAIN 164 211 Fibronectin type-II. FT {ECO:0000255|PROSITE-ProRule:PRU00479}. FT DOMAIN 225 341 C-type lectin 1. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 368 486 C-type lectin 2. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 493 625 C-type lectin 3. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 652 778 C-type lectin 4. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 818 931 C-type lectin 5. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 958 1091 C-type lectin 6. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 1110 1222 C-type lectin 7. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 1251 1374 C-type lectin 8. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 1401 1513 C-type lectin 9. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 1542 1661 C-type lectin 10. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT MOD_RES 933 933 Phosphotyrosine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1703 1703 Phosphoserine. FT {ECO:0000250|UniProtKB:Q60767}. FT MOD_RES 1719 1719 Phosphoserine. FT {ECO:0000250|UniProtKB:Q60767}. FT CARBOHYD 135 135 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 345 345 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 377 377 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 529 529 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 843 843 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 865 865 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 934 934 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1076 1076 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1103 1103 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1225 1225 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1320 1320 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1392 1392 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1593 1593 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1626 1626 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 169 194 {ECO:0000250}. FT DISULFID 183 209 {ECO:0000250}. FT DISULFID 247 340 {ECO:0000250}. FT DISULFID 317 332 {ECO:0000250}. FT DISULFID 389 485 {ECO:0000250}. FT DISULFID 462 477 {ECO:0000250}. FT DISULFID 597 614 {ECO:0000250}. FT DISULFID 840 930 {ECO:0000250}. FT DISULFID 904 922 {ECO:0000250}. FT DISULFID 1060 1080 {ECO:0000250}. FT DISULFID 1197 1211 {ECO:0000250}. FT DISULFID 1488 1502 {ECO:0000250}. FT DISULFID 1635 1650 {ECO:0000250}. FT VAR_SEQ 1608 1722 DQSWSWLDGSEVTFVKWENKSKSGVGRCSMLIASNETWKKV FT ECEHGFGRVVCKVPLGPDYTAIAIIVATLSILVLMGGLIWF FT LFQRHRLHLAGFSSVRYAQGVNEDEIMLPSFHD -> DCPS FT STWIQFQDSCYIFLQEAIKVESIEDVRNQCTDHGADMISIH FT NEEENAFILDTLKKQWKGPDDILLGMFYDTDDASFKWFDNS FT NMTFDKWTDQDDDEDLVDTCAFLHIKTGEWKKGNCEVSSVE FT GTLCKTAIPYKRKYLSDNHILISALVIASTVILTVLGAIIW FT FLYKKHSDSRFTTVFSTAPQSPYNEDCVLVVGEENEYPVQF FT D (in isoform 3). FT {ECO:0000303|PubMed:12824192}. FT /FTId=VSP_020908. FT VAR_SEQ 1664 1722 GPDYTAIAIIVATLSILVLMGGLIWFLFQRHRLHLAGFSSV FT RYAQGVNEDEIMLPSFHD -> DCPSSTWIQFQDSCYIFLQ FT EAIKVESIEDVRNQCTDHGADMISIHNEEENAFILDTLKKQ FT WKGPDDILLGMFYDTDDASFKWFDNSNMTFDKWTDQDDDED FT LVDTCAFLHIKTGEWKKGNCEVSSVEGTLCKTAIPYKRKYL FT SDNHILISALVIASTVILTVLGAIIWFLYKKHSDSRFTTVF FT STAPQSPYNEDCVLVVGEENEYPVQFD (in isoform FT 2). {ECO:0000303|PubMed:12824192}. FT /FTId=VSP_020909. FT VARIANT 20 20 W -> R (in dbSNP:rs35284483). FT /FTId=VAR_056156. FT VARIANT 268 268 E -> D (in dbSNP:rs2271381). FT {ECO:0000269|PubMed:9862343}. FT /FTId=VAR_027824. FT VARIANT 486 486 K -> M (in dbSNP:rs2729709). FT /FTId=VAR_027825. FT VARIANT 666 666 V -> A (in dbSNP:rs34020639). FT /FTId=VAR_056157. FT VARIANT 692 692 D -> N (in dbSNP:rs1397706). FT /FTId=VAR_024522. FT VARIANT 807 807 D -> E (in dbSNP:rs3951216). FT {ECO:0000269|PubMed:9862343}. FT /FTId=VAR_027826. FT VARIANT 884 884 D -> A (in dbSNP:rs3815875). FT /FTId=VAR_027827. FT VARIANT 1202 1202 T -> S (in dbSNP:rs2303549). FT /FTId=VAR_027828. FT VARIANT 1321 1321 K -> N (in dbSNP:rs12692566). FT {ECO:0000269|PubMed:12824192, FT ECO:0000269|PubMed:9553150}. FT /FTId=VAR_027829. FT VARIANT 1347 1347 K -> R (in dbSNP:rs17827158). FT /FTId=VAR_027830. FT VARIANT 1391 1391 Y -> H (in dbSNP:rs2059696). FT /FTId=VAR_027831. FT VARIANT 1393 1393 T -> I (in dbSNP:rs35941588). FT /FTId=VAR_056158. SQ SEQUENCE 1722 AA; 198311 MW; 4BC17EC646BF016F CRC64; MRTGWATPRR PAGLLMLLFW FFDLAEPSGR AANDPFTIVH GNTGKCIKPV YGWIVADDCD ETEDKLWKWV SQHRLFHLHS QKCLGLDITK SVNELRMFSC DSSAMLWWKC EHHSLYGAAR YRLALKDGHG TAISNASDVW KKGGSEESLC DQPYHEIYTR DGNSYGRPCE FPFLIDGTWH HDCILDEDHS GPWCATTLNY EYDRKWGICL KPENGCEDNW EKNEQFGSCY QFNTQTALSW KEAYVSCQNQ GADLLSINSA AELTYLKEKE GIAKIFWIGL NQLYSARGWE WSDHKPLNFL NWDPDRPSAP TIGGSSCARM DAESGLWQSF SCEAQLPYVC RKPLNNTVEL TDVWTYSDTR CDAGWLPNNG FCYLLVNESN SWDKAHAKCK AFSSDLISIH SLADVEVVVT KLHNEDIKEE VWIGLKNINI PTLFQWSDGT EVTLTYWDEN EPNVPYNKTP NCVSYLGELG QWKVQSCEEK LKYVCKRKGE KLNDASSDKM CPPDEGWKRH GETCYKIYED EVPFGTNCNL TITSRFEQEY LNDLMKKYDK SLRKYFWTGL RDVDSCGEYN WATVGGRRRA VTFSNWNFLE PASPGGCVAM STGKSVGKWE VKDCRSFKAL SICKKMSGPL GPEEASPKPD DPCPEGWQSF PASLSCYKVF HAERIVRKRN WEEAERFCQA LGAHLSSFSH VDEIKEFLHF LTDQFSGQHW LWIGLNKRSP DLQGSWQWSD RTPVSTIIMP NEFQQDYDIR DCAAVKVFHR PWRRGWHFYD DREFIYLRPF ACDTKLEWVC QIPKGRTPKT PDWYNPDRAG IHGPPLIIEG SEYWFVADLH LNYEEAVLYC ASNHSFLATI TSFVGLKAIK NKIANISGDG QKWWIRISEW PIDDHFTYSR YPWHRFPVTF GEECLYMSAK TWLIDLGKPT DCSTKLPFIC EKYNVSSLEK YSPDSAAKVQ CSEQWIPFQN KCFLKIKPVS LTFSQASDTC HSYGGTLPSV LSQIEQDFIT SLLPDMEATL WIGLRWTAYE KINKWTDNRE LTYSNFHPLL VSGRLRIPEN FFEEESRYHC ALILNLQKSP FTGTWNFTSC SERHFVSLCQ KYSEVKSRQT LQNASETVKY LNNLYKIIPK TLTWHSAKRE CLKSNMQLVS ITDPYQQAFL SVQALLHNSS LWIGLFSQDD ELNFGWSDGK RLHFSRWAET NGQLEDCVVL DTDGFWKTVD CNDNQPGAIC YYSGNETEKE VKPVDSVKCP SPVLNTPWIP FQNCCYNFII TKNRHMATTQ DEVHTKCQKL NPKSHILSIR DEKENNFVLE QLLYFNYMAS WVMLGITYRN KSLMWFDKTP LSYTHWRAGR PTIKNEKFLA GLSTDGFWDI QTFKVIEEAV YFHQHSILAC KIEMVDYKEE YNTTLPQFMP YEDGIYSVIQ KKVTWYEALN MCSQSGGHLA SVHNQNGQLF LEDIVKRDGF PLWVGLSSHD GSESSFEWSD GSTFDYIPWK GQTSPGNCVL LDPKGTWKHE KCNSVKDGAI CYKPTKSKKL SRLTYSSRCP AAKENGSRWI QYKGHCYKSD QALHSFSEAK KLCSKHDHSA TIVSIKDEDE NKFVSRLMRE NNNITMRVWL GLSQHSVDQS WSWLDGSEVT FVKWENKSKS GVGRCSMLIA SNETWKKVEC EHGFGRVVCK VPLGPDYTAI AIIVATLSIL VLMGGLIWFL FQRHRLHLAG FSSVRYAQGV NEDEIMLPSF HD //