ID DSCAM_HUMAN Reviewed; 2012 AA. AC O60469; O60468; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 24-JUL-2024, entry version 211. DE RecName: Full=Cell adhesion molecule DSCAM {ECO:0000305}; DE AltName: Full=CHD2; DE AltName: Full=Down syndrome cell adhesion molecule; DE Flags: Precursor; GN Name=DSCAM; 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], AND ALTERNATIVE SPLICING. RC TISSUE=Brain; RX PubMed=9426258; DOI=10.1093/hmg/7.2.227; RA Yamakawa K., Huot Y.-K., Haendelt M.A., Hubert R., Chen X.-N., Lyons G.E., RA Korenberg J.R.; RT "DSCAM: a novel member of the immunoglobulin superfamily maps in a Down RT syndrome region and is involved in the development of the nervous system."; RL Hum. Mol. Genet. 7:227-237(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=10925149; DOI=10.1016/s0169-328x(00)00108-x; RA Agarwala K.L., Nakamura S., Tsutsumi Y., Yamakawa K.; RT "Down syndrome cell adhesion molecule DSCAM mediates homophilic RT intercellular adhesion."; RL Brain Res. Mol. Brain Res. 79:118-126(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [4] RP RETRACTED PAPER. RX PubMed=15169762; DOI=10.1074/jbc.m401878200; RA Li W., Guan K.L.; RT "The Down syndrome cell adhesion molecule (DSCAM) interacts with and RT activates Pak."; RL J. Biol. Chem. 279:32824-32831(2004). RN [5] RP RETRACTION NOTICE OF PUBMED:15169762. RX PubMed=26048998; DOI=10.1074/jbc.a115.401878; RA Li W., Guan K.L.; RT "The Down syndrome cell adhesion molecule (DSCAM) interacts with and RT activates Pak."; RL J. Biol. Chem. 290:14797-14797(2015). RN [6] RP FUNCTION. RX PubMed=18585357; DOI=10.1016/j.cell.2008.05.030; RA Ly A., Nikolaev A., Suresh G., Zheng Y., Tessier-Lavigne M., Stein E.; RT "DSCAM is a netrin receptor that collaborates with DCC in mediating turning RT responses to netrin-1."; RL Cell 133:1241-1254(2008). RN [7] RP FUNCTION, INTERACTION WITH NTN1, AND PHOSPHORYLATION. RX PubMed=19196994; DOI=10.1073/pnas.0811083106; RA Liu G., Li W., Wang L., Kar A., Guan K.L., Rao Y., Wu J.Y.; RT "DSCAM functions as a netrin receptor in commissural axon pathfinding."; RL Proc. Natl. Acad. Sci. U.S.A. 106:2951-2956(2009). RN [8] RP INTERACTION WITH UNC5C. RX PubMed=22685302; DOI=10.1074/jbc.m112.340174; RA Purohit A.A., Li W., Qu C., Dwyer T., Shao Q., Guan K.L., Liu G.; RT "Down syndrome cell adhesion molecule (DSCAM) associates with RT uncoordinated-5C (UNC5C) in netrin-1-mediated growth cone collapse."; RL J. Biol. Chem. 287:27126-27138(2012). CC -!- FUNCTION: Cell adhesion molecule that plays a role in neuronal self- CC avoidance. Promotes repulsion between specific neuronal processes of CC either the same cell or the same subtype of cells. Mediates within CC retinal amacrine and ganglion cell subtypes both isoneuronal self- CC avoidance for creating an orderly dendritic arborization and CC heteroneuronal self-avoidance to maintain the mosaic spacing between CC amacrine and ganglion cell bodies (PubMed:10925149). Receptor for CC netrin required for axon guidance independently of and in collaboration CC with the receptor DCC. Might also collaborate with UNC5C in NTN1- CC mediated axon repulsion independently of DCC (By similarity). In spinal CC cord development plays a role in guiding commissural axons projection CC and pathfinding across the ventral midline to reach the floor plate CC upon ligand binding (PubMed:18585357, PubMed:19196994). Mediates CC intracellular signaling by stimulating the activation of MAPK8 and MAP CC kinase p38 (PubMed:18585357, PubMed:19196994). Adhesion molecule that CC promotes lamina-specific synaptic connections in the retina: expressed CC in specific subsets of interneurons and retinal ganglion cells (RGCs) CC and promotes synaptic connectivity via homophilic interactions (By CC similarity). {ECO:0000250|UniProtKB:F1NY98, CC ECO:0000250|UniProtKB:Q9ERC8, ECO:0000269|PubMed:10925149, CC ECO:0000269|PubMed:18585357, ECO:0000269|PubMed:19196994}. CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell CC adhesion (By similarity). Interacts with DCC; the interaction is CC abolished in response to NTN1 (By similarity). Interacts (via CC extracellular domain) with NTN1 (PubMed:19196994). Interacts (via CC extracellular domain) with UNC5C (via Ig-like C2-type domain) CC (PubMed:22685302). Interacts with PTK2 (By similarity). Interacts with CC FYN (By similarity). {ECO:0000250|UniProtKB:F1NY98, CC ECO:0000250|UniProtKB:Q9ERC8, ECO:0000269|PubMed:19196994, CC ECO:0000269|PubMed:22685302}. CC -!- INTERACTION: CC O60469; Q15700: DLG2; NbExp=3; IntAct=EBI-19949317, EBI-80426; CC O60469; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-19949317, EBI-10232538; CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Secreted {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane CC {ECO:0000250|UniProtKB:Q9ERC8}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:Q9ERC8}. Synapse {ECO:0000250|UniProtKB:F1NY98}. CC Note=Localized in the soma, cell membrane, axon and growth cone of CC dissociated commissural axons. {ECO:0000250|UniProtKB:Q9ERC8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; Synonyms=CHD2-42; CC IsoId=O60469-1; Sequence=Displayed; CC Name=Short; Synonyms=CHD2-52; CC IsoId=O60469-2; Sequence=VSP_002502, VSP_002503; CC -!- TISSUE SPECIFICITY: Primarily expressed in brain. CC -!- DOMAIN: Ig-like C2-type domains 7 to 9 are sufficient for interaction CC with NTN1 and commissural axon outgrowth. The transmembrane domain is CC necessary for interaction with DCC (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated at tyrosine residues. Phosphorylation is enhanced CC by NTN1. {ECO:0000269|PubMed:19196994}. CC -!- CAUTION: Has been reported to enhance netrin-induced phosphorylation of CC PAK1 and FYN; and the interaction between DSCAM, PAK1 and RAC1 has been CC described. This article has been withdrawn by the authors. CC {ECO:0000305|PubMed:15169762, ECO:0000305|PubMed:26048998}. 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; AF023450; AAC17967.1; -; mRNA. DR EMBL; AF023449; AAC17966.1; -; mRNA. DR EMBL; AF217525; AAF27525.1; -; mRNA. DR EMBL; AL163283; CAB90464.1; -; Genomic_DNA. DR EMBL; AL163282; CAB90436.1; -; Genomic_DNA. DR EMBL; AL163281; CAB90444.1; -; Genomic_DNA. DR CCDS; CCDS42929.1; -. [O60469-1] DR RefSeq; NP_001380.2; NM_001389.3. [O60469-1] DR PDB; 6ZR7; X-ray; 1.85 A; AAA=595-884. DR PDBsum; 6ZR7; -. DR AlphaFoldDB; O60469; -. DR SMR; O60469; -. DR BioGRID; 108160; 159. DR IntAct; O60469; 155. DR STRING; 9606.ENSP00000383303; -. DR GlyCosmos; O60469; 18 sites, No reported glycans. DR GlyGen; O60469; 18 sites. DR iPTMnet; O60469; -. DR PhosphoSitePlus; O60469; -. DR BioMuta; DSCAM; -. DR jPOST; O60469; -. DR MassIVE; O60469; -. DR PaxDb; 9606-ENSP00000383303; -. DR PeptideAtlas; O60469; -. DR ProteomicsDB; 49414; -. [O60469-1] DR ProteomicsDB; 49415; -. [O60469-2] DR Antibodypedia; 23484; 172 antibodies from 32 providers. DR DNASU; 1826; -. DR Ensembl; ENST00000400454.6; ENSP00000383303.1; ENSG00000171587.15. [O60469-1] DR Ensembl; ENST00000708009.1; ENSP00000517071.1; ENSG00000291561.1. [O60469-1] DR GeneID; 1826; -. DR KEGG; hsa:1826; -. DR MANE-Select; ENST00000400454.6; ENSP00000383303.1; NM_001389.5; NP_001380.2. DR UCSC; uc002yyq.2; human. [O60469-1] DR AGR; HGNC:3039; -. DR CTD; 1826; -. DR DisGeNET; 1826; -. DR GeneCards; DSCAM; -. DR HGNC; HGNC:3039; DSCAM. DR HPA; ENSG00000171587; Group enriched (brain, pituitary gland, retina). DR MIM; 602523; gene. DR neXtProt; NX_O60469; -. DR OpenTargets; ENSG00000171587; -. DR PharmGKB; PA27491; -. DR VEuPathDB; HostDB:ENSG00000171587; -. DR eggNOG; KOG3510; Eukaryota. DR GeneTree; ENSGT00940000154678; -. DR HOGENOM; CLU_001038_0_1_1; -. DR InParanoid; O60469; -. DR OMA; DGFDHHK; -. DR OrthoDB; 3427297at2759; -. DR PhylomeDB; O60469; -. DR TreeFam; TF316846; -. DR PathwayCommons; O60469; -. DR Reactome; R-HSA-376172; DSCAM interactions. DR SignaLink; O60469; -. DR SIGNOR; O60469; -. DR BioGRID-ORCS; 1826; 7 hits in 1144 CRISPR screens. DR ChiTaRS; DSCAM; human. DR GenomeRNAi; 1826; -. DR Pharos; O60469; Tbio. DR PRO; PR:O60469; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; O60469; Protein. DR Bgee; ENSG00000171587; Expressed in endometrium epithelium and 59 other cell types or tissues. DR ExpressionAtlas; O60469; baseline and differential. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0030426; C:growth cone; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; ISS:UniProtKB. DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central. DR GO; GO:1990890; F:netrin receptor binding; IPI:UniProtKB. DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl. DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB. DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; ISS:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central. DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl. DR GO; GO:0070593; P:dendrite self-avoidance; ISS:UniProtKB. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl. DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IDA:UniProtKB. DR GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB. DR GO; GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; IEA:Ensembl. DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB. DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB. DR CDD; cd00063; FN3; 6. DR CDD; cd00096; Ig; 2. DR CDD; cd05734; Ig_DSCAM; 1. DR CDD; cd05735; Ig_DSCAM; 1. DR CDD; cd20958; IgI_5_Dscam; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 16. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR10075; BASIGIN RELATED; 1. DR PANTHER; PTHR10075:SF51; DOWN SYNDROME CELL ADHESION MOLECULE; 1. DR Pfam; PF00041; fn3; 5. DR Pfam; PF07679; I-set; 5. DR Pfam; PF13927; Ig_3; 3. DR SMART; SM00060; FN3; 6. DR SMART; SM00409; IG; 9. DR SMART; SM00408; IGc2; 9. DR SMART; SM00406; IGv; 3. DR SUPFAM; SSF49265; Fibronectin type III; 3. DR SUPFAM; SSF48726; Immunoglobulin; 9. DR PROSITE; PS50853; FN3; 6. DR PROSITE; PS50835; IG_LIKE; 9. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Cell projection; Disulfide bond; Glycoprotein; Immunoglobulin domain; KW Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Repeat; KW Secreted; Signal; Synapse; Transmembrane; Transmembrane helix. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT CHAIN 18..2012 FT /note="Cell adhesion molecule DSCAM" FT /id="PRO_0000014747" FT TOPO_DOM 18..1595 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1596..1616 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1617..2012 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 39..129 FT /note="Ig-like C2-type 1" FT DOMAIN 125..216 FT /note="Ig-like C2-type 2" FT DOMAIN 225..305 FT /note="Ig-like C2-type 3" FT DOMAIN 313..401 FT /note="Ig-like C2-type 4" FT DOMAIN 407..500 FT /note="Ig-like C2-type 5" FT DOMAIN 504..592 FT /note="Ig-like C2-type 6" FT DOMAIN 596..685 FT /note="Ig-like C2-type 7" FT DOMAIN 690..783 FT /note="Ig-like C2-type 8" FT DOMAIN 787..883 FT /note="Ig-like C2-type 9" FT DOMAIN 885..982 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 987..1086 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1091..1187 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1191..1285 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1285..1377 FT /note="Ig-like C2-type 10" FT DOMAIN 1379..1473 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1474..1575 FT /note="Fibronectin type-III 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 1617..2012 FT /note="Required for netrin-mediated axon repulsion of FT neuronal growth cones" FT /evidence="ECO:0000250|UniProtKB:Q9ERC8" FT REGION 1718..1810 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1855..1883 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1971..2012 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1725..1767 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1782..1810 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1855..1869 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1982..1996 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 28 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 78 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 470 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 487 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 512 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 556 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 658 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 666 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 710 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 748 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 795 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 924 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1142 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1160 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1250 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1271 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1341 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1488 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 46..102 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 145..197 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 246..293 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 335..385 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 428..484 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 525..575 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 617..669 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 711..766 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 809..865 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1307..1359 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1562..1571 FT /note="NFATLNYDGS -> KEAARCKEFS (in isoform Short)" FT /evidence="ECO:0000305" FT /id="VSP_002502" FT VAR_SEQ 1572..2012 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000305" FT /id="VSP_002503" FT VARIANT 232 FT /note="D -> E (in dbSNP:rs2297270)" FT /id="VAR_020080" FT CONFLICT 1893..2012 FT /note="HRPGDLIHLPPYLRMDFLLNRGGPGTSRDLSLGQACLEPQKSRTLKRPTVLE FT PIPMEAASSASSTREGQSWQPGAVATLPQREGAELGQAAKMSSSQESLLDSRGHLKGNN FT PYAKSYTLV -> IGQVTSYICLHTLEWTFC (in Ref. 1; AAC17966)" FT /evidence="ECO:0000305" SQ SEQUENCE 2012 AA; 222260 MW; 0E33CFB781A08334 CRC64; MWILALSLFQ SFANVFSEDL HSSLYFVNAS LQEVVFASTT GTLVPCPAAG IPPVTLRWYL ATGEEIYDVP GIRHVHPNGT LQIFPFPPSS FSTLIHDNTY YCTAENPSGK IRSQDVHIKA VLREPYTVRV EDQKTMRGNV AVFKCIIPSS VEAYITVVSW EKDTVSLVSG SRFLITSTGA LYIKDVQNED GLYNYRCITR HRYTGETRQS NSARLFVSDP ANSAPSILDG FDHRKAMAGQ RVELPCKALG HPEPDYRWLK DNMPLELSGR FQKTVTGLLI ENIRPSDSGS YVCEVSNRYG TAKVIGRLYV KQPLKATISP RKVKSSVGSQ VSLSCSVTGT EDQELSWYRN GEILNPGKNV RITGINHENL IMDHMVKSDG GAYQCFVRKD KLSAQDYVQV VLEDGTPKII SAFSEKVVSP AEPVSLMCNV KGTPLPTITW TLDDDPILKG GSHRISQMIT SEGNVVSYLN ISSSQVRDGG VYRCTANNSA GVVLYQARIN VRGPASIRPM KNITAIAGRD TYIHCRVIGY PYYSIKWYKN SNLLPFNHRQ VAFENNGTLK LSDVQKEVDE GEYTCNVLVQ PQLSTSQSVH VTVKVPPFIQ PFEFPRFSIG QRVFIPCVVV SGDLPITITW QKDGRPIPGS LGVTIDNIDF TSSLRISNLS LMHNGNYTCI ARNEAAAVEH QSQLIVRVPP KFVVQPRDQD GIYGKAVILN CSAEGYPVPT IVWKFSKGAG VPQFQPIALN GRIQVLSNGS LLIKHVVEED SGYYLCKVSN DVGADVSKSM YLTVKIPAMI TSYPNTTLAT QGQKKEMSCT AHGEKPIIVR WEKEDRIINP EMARYLVSTK EVGEEVISTL QILPTVREDS GFFSCHAINS YGEDRGIIQL TVQEPPDPPE IEIKDVKART ITLRWTMGFD GNSPITGYDI ECKNKSDSWD SAQRTKDVSP QLNSATIIDI HPSSTYSIRM YAKNRIGKSE PSNELTITAD EAAPDGPPQE VHLEPISSQS IRVTWKAPKK HLQNGIIRGY QIGYREYSTG GNFQFNIISV DTSGDSEVYT LDNLNKFTQY GLVVQACNRA GTGPSSQEII TTTLEDVPSY PPENVQAIAT SPESISISWS TLSKEALNGI LQGFRVIYWA NLMDGELGEI KNITTTQPSL ELDGLEKYTN YSIQVLAFTR AGDGVRSEQI FTRTKEDVPG PPAGVKAAAA SASMVFVSWL PPLKLNGIIR KYTVFCSHPY PTVISEFEAS PDSFSYRIPN LSRNRQYSVW VVAVTSAGRG NSSEIITVEP LAKAPARILT FSGTVTTPWM KDIVLPCKAV GDPSPAVKWM KDSNGTPSLV TIDGRRSIFS NGSFIIRTVK AEDSGYYSCI ANNNWGSDEI ILNLQVQVPP DQPRLTVSKT TSSSITLSWL PGDNGGSSIR GYILQYSEDN SEQWGSFPIS PSERSYRLEN LKCGTWYKFT LTAQNGVGPG RISEIIEAKT LGKEPQFSKE QELFASINTT RVRLNLIGWN DGGCPITSFT LEYRPFGTTV WTTAQRTSLS KSYILYDLQE ATWYELQMRV CNSAGCAEKQ ANFATLNYDG STIPPLIKSV VQNEEGLTTN EGLKMLVTIS CILVGVLLLF VLLLVVRRRR REQRLKRLRD AKSLAEMLMS KNTRTSDTLS KQQQTLRMHI DIPRAQLLIE ERDTMETIDD RSTVLLTDAD FGEAAKQKSL TVTHTVHYQS VSQATGPLVD VSDARPGTNP TTRRNAKAGP TARNRYASQW TLNRPHPTIS AHTLTTDWRL PTPRAAGSVD KESDSYSVSP SQDTDRARSS MVSTESASST YEELARAYEH AKMEEQLRHA KFTITECFIS DTSSEQLTAG TNEYTDSLTS STPSESGICR FTASPPKPQD GGRVMNMAVP KAHRPGDLIH LPPYLRMDFL LNRGGPGTSR DLSLGQACLE PQKSRTLKRP TVLEPIPMEA ASSASSTREG QSWQPGAVAT LPQREGAELG QAAKMSSSQE SLLDSRGHLK GNNPYAKSYT LV //