DSCAM_HUMAN
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 03-AUG-2022, entry version 200.
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 FUNCTION, AND INTERACTION WITH PAK1 AND RAC1.
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 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 [6]
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 [7]
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). Enhances
CC netrin-induced phosphorylation of PAK1 and FYN (PubMed:15169762).
CC Mediates intracellular signaling by stimulating the activation of MAPK8
CC and MAP kinase p38 (PubMed:18585357, PubMed:19196994). Adhesion
CC molecule that promotes lamina-specific synaptic connections in the
CC retina: expressed in specific subsets of interneurons and retinal
CC ganglion cells (RGCs) and promotes synaptic connectivity via homophilic
CC interactions (By similarity). {ECO:0000250|UniProtKB:F1NY98,
CC ECO:0000250|UniProtKB:Q9ERC8, ECO:0000269|PubMed:10925149,
CC ECO:0000269|PubMed:15169762, ECO:0000269|PubMed:18585357,
CC 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). Probably found in a
CC ternary complex composed of DSCAM, PAK1 and RAC1 (PubMed:15169762).
CC Interacts (via cytoplasmic domain) with PAK1; the interaction is direct
CC and enhanced in presence of RAC1 (PubMed:15169762). Interacts with
CC RAC1; the interaction requires PAK1 (PubMed:15169762). 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:15169762,
CC ECO:0000269|PubMed:19196994, ECO:0000269|PubMed:22685302}.
CC -!- INTERACTION:
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}.
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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; 3.
DR IntAct; O60469; 1.
DR STRING; 9606.ENSP00000383303; -.
DR GlyGen; O60469; 18 sites.
DR iPTMnet; O60469; -.
DR PhosphoSitePlus; O60469; -.
DR BioMuta; DSCAM; -.
DR EPD; O60469; -.
DR jPOST; O60469; -.
DR MassIVE; O60469; -.
DR PaxDb; O60469; -.
DR PeptideAtlas; O60469; -.
DR PRIDE; O60469; -.
DR ProteomicsDB; 49414; -. [O60469-1]
DR ProteomicsDB; 49415; -. [O60469-2]
DR Antibodypedia; 23484; 170 antibodies from 32 providers.
DR DNASU; 1826; -.
DR Ensembl; ENST00000400454.6; ENSP00000383303.1; ENSG00000171587.15. [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 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; WTTAHRT; -.
DR OrthoDB; 14047at2759; -.
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; 5 hits in 1066 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 58 other tissues.
DR ExpressionAtlas; O60469; baseline and differential.
DR Genevisible; O60469; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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: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 Gene3D; 2.60.40.10; -; 16.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR033027; DSCAM_metazoan.
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; PTHR10075; 1.
DR PANTHER; PTHR10075:SF51; PTHR10075:SF51; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 5.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF48726; SSF48726; 9.
DR SUPFAM; SSF49265; SSF49265; 3.
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
