DSCAM_MOUSE
ID DSCAM_MOUSE Reviewed; 2013 AA.
AC Q9ERC8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cell adhesion molecule DSCAM {ECO:0000305};
DE AltName: Full=Down syndrome cell adhesion molecule homolog;
DE Flags: Precursor;
GN Name=Dscam;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=ICR;
RX PubMed=11237714; DOI=10.1006/bbrc.2001.4420;
RA Agarwala K.L., Ganesh S., Amano K., Suzuki T., Yamakawa K.;
RT "DSCAM, a highly conserved gene in mammals, expressed in differentiating
RT mouse brain.";
RL Biochem. Biophys. Res. Commun. 281:697-705(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11856873; DOI=10.1159/000048808;
RA Barlow G.M., Micales B., Lyons G.E., Korenberg J.R.;
RT "Down syndrome cell adhesion molecule is conserved in mouse and highly
RT expressed in the adult mouse brain.";
RL Cytogenet. Cell Genet. 94:155-162(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH PAK1.
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, AND INTERACTION WITH DCC AND NTN1.
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, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18216855; DOI=10.1038/nature06514;
RA Fuerst P.G., Koizumi A., Masland R.H., Burgess R.W.;
RT "Neurite arborization and mosaic spacing in the mouse retina require
RT DSCAM.";
RL Nature 451:470-474(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19945391; DOI=10.1016/j.neuron.2009.09.027;
RA Fuerst P.G., Bruce F., Tian M., Wei W., Elstrott J., Feller M.B.,
RA Erskine L., Singer J.H., Burgess R.W.;
RT "DSCAM and DSCAML1 function in self-avoidance in multiple cell types in the
RT developing mouse retina.";
RL Neuron 64:484-497(2009).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
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 [9]
RP FUNCTION, INTERACTION WITH UNC5C; PTK2 AND FYN, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
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:18216855, PubMed:19196994,
CC PubMed:19945391). Receptor for netrin required for axon guidance
CC independently of and in collaboration with the receptor DCC
CC (PubMed:18585357). Might also collaborate with UNC5C in NTN1-mediated
CC axon repulsion independently of DCC (PubMed:22685302). In spinal cord
CC development plays a role in guiding commissural axons projection and
CC pathfinding across the ventral midline to reach the floor plate upon
CC ligand binding. Enhances netrin-induced phosphorylation of PAK1 and
CC FYN. Mediates intracellular signaling by stimulating the activation of
CC MAPK8 and MAP kinase p38. Adhesion molecule that promotes lamina-
CC specific synaptic connections in the retina: expressed in specific
CC subsets of interneurons and retinal ganglion cells (RGCs) and promotes
CC synaptic connectivity via homophilic interactions (By similarity).
CC {ECO:0000250|UniProtKB:F1NY98, ECO:0000250|UniProtKB:O60469,
CC ECO:0000269|PubMed:18216855, ECO:0000269|PubMed:18585357,
CC ECO:0000269|PubMed:19196994, ECO:0000269|PubMed:19945391,
CC ECO:0000269|PubMed:22685302}.
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 (PubMed:18585357). Interacts (via
CC extracellular domain) with NTN1 (PubMed:18585357). Probably found in a
CC ternary complex composed of DSCAM, PAK1 and RAC1 (By similarity). The
CC interaction with PAK1 is direct and enhanced in presence of RAC1
CC (PubMed:15169762). Interacts with RAC1; the interaction requires PAK1
CC (By similarity). Interacts (via cytoplasmic domain) with PAK1 (By
CC similarity). Interacts (via extracellular domain) with UNC5C (via Ig-
CC like C2-type domain) (PubMed:22685302). Interacts with PTK2
CC (PubMed:22685302). Interacts with FYN (PubMed:22685302).
CC {ECO:0000250|UniProtKB:F1NY98, ECO:0000250|UniProtKB:O60469,
CC ECO:0000269|PubMed:15169762, ECO:0000269|PubMed:18585357,
CC ECO:0000269|PubMed:22685302}.
CC -!- INTERACTION:
CC Q9ERC8; P70211: Dcc; NbExp=4; IntAct=EBI-1798601, EBI-1798863;
CC Q9ERC8; Q63155: Dcc; Xeno; NbExp=4; IntAct=EBI-1798601, EBI-1798965;
CC Q9ERC8; Q90922: NTN1; Xeno; NbExp=7; IntAct=EBI-1798601, EBI-1798593;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19196994};
CC Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC axon {ECO:0000269|PubMed:19196994, ECO:0000269|PubMed:22685302}.
CC Synapse {ECO:0000250|UniProtKB:F1NY98}. Cell projection, dendrite
CC {ECO:0000269|PubMed:22685302}. Cell projection, growth cone
CC {ECO:0000269|PubMed:22685302}. Note=Localized in the soma, cell
CC membrane, axon and growth cone of dissociated commissural axons.
CC {ECO:0000269|PubMed:19196994}.
CC -!- TISSUE SPECIFICITY: Expressed in cortical and cerebellar neurons, in
CC cells of the external and internal granular layer and of the Purkinje
CC cell layer (at protein level) (PubMed:22685302). In the retina,
CC expressed in dopaminergic and Nos1-positive amacrine cells and most
CC retinal ganglion cells (at protein level). Expressed in the brain with
CC highest levels in the cortex, olfactory bulb, hippocampus, thalamus,
CC cerebellum and spinal cord. Expressed in the retinal ganglion layer
CC (RGL). {ECO:0000269|PubMed:11237714, ECO:0000269|PubMed:11856873,
CC ECO:0000269|PubMed:18216855, ECO:0000269|PubMed:19945391,
CC ECO:0000269|PubMed:22685302}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 11 dpc. Expressed in the
CC spinal cord, including the motor columns, motor axons, dorsal root
CC ganglions, commissural axons and ventral funiculus at 11.5 dpc (at
CC protein level). Detected at 15 dpc in the cortex and cerebellum and at
CC postnatal day 2 in the cerebellum (at protein level) (PubMed:22685302).
CC Expressed in the retinal ganglion layer (RGL) at 12.5, 14.5 and 17 dpc.
CC Expressed in hindbrain (cerebellar plate neurons), midbrain and
CC forebrain at 10 dpc. Expressed in follicles of vibrissae and nasal
CC processes at 12 dpc. Expressed in eyes at 14 dpc. Expressed in spinal
CC cord, heart, liver, forelimb and hindlimb, buds at 14 dpc onwards.
CC {ECO:0000269|PubMed:11237714, ECO:0000269|PubMed:19196994,
CC ECO:0000269|PubMed:19945391, ECO:0000269|PubMed:22685302}.
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.
CC -!- PTM: Phosphorylated at tyrosine residues (PubMed:22685302).
CC Phosphorylation is enhanced by NTN1 (PubMed:22685302).
CC {ECO:0000269|PubMed:22685302}.
CC -!- DISRUPTION PHENOTYPE: The ganglion cell layer and developing inner
CC plexiform layer in the retina are disorganised at postnatal day 4 (P4).
CC This desorganisation persisted into adulthood in amacrine and ganglions
CC cells. Amacrine and ganglion cell populations show fasciculated
CC dendrites that self-crossed and their cell bodies are randomly
CC distributed or pulled into clumps. {ECO:0000269|PubMed:18216855,
CC ECO:0000269|PubMed:19945391}.
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DR EMBL; AY005483; AAF99440.1; -; mRNA.
DR EMBL; AF315558; AAG28796.1; -; mRNA.
DR EMBL; CH466602; EDL03664.1; -; Genomic_DNA.
DR CCDS; CCDS37415.1; -.
DR RefSeq; NP_112451.1; NM_031174.4.
DR AlphaFoldDB; Q9ERC8; -.
DR SMR; Q9ERC8; -.
DR BioGRID; 199321; 8.
DR IntAct; Q9ERC8; 5.
DR STRING; 10090.ENSMUSP00000056040; -.
DR GlyGen; Q9ERC8; 5 sites.
DR iPTMnet; Q9ERC8; -.
DR PhosphoSitePlus; Q9ERC8; -.
DR PaxDb; Q9ERC8; -.
DR PRIDE; Q9ERC8; -.
DR ProteomicsDB; 279810; -.
DR Antibodypedia; 23484; 170 antibodies from 32 providers.
DR DNASU; 13508; -.
DR Ensembl; ENSMUST00000056102; ENSMUSP00000056040; ENSMUSG00000050272.
DR GeneID; 13508; -.
DR KEGG; mmu:13508; -.
DR UCSC; uc008add.2; mouse.
DR CTD; 1826; -.
DR MGI; MGI:1196281; Dscam.
DR VEuPathDB; HostDB:ENSMUSG00000050272; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000154678; -.
DR HOGENOM; CLU_001038_0_1_1; -.
DR InParanoid; Q9ERC8; -.
DR OMA; WTTAHRT; -.
DR OrthoDB; 14047at2759; -.
DR PhylomeDB; Q9ERC8; -.
DR TreeFam; TF316846; -.
DR Reactome; R-MMU-376172; DSCAM interactions.
DR BioGRID-ORCS; 13508; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Dscam; mouse.
DR PRO; PR:Q9ERC8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9ERC8; protein.
DR Bgee; ENSMUSG00000050272; Expressed in cortical plate and 124 other tissues.
DR ExpressionAtlas; Q9ERC8; baseline and differential.
DR Genevisible; Q9ERC8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA: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; IPI:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0070593; P:dendrite self-avoidance; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0038007; P:netrin-activated signaling pathway; IDA:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; IMP:MGI.
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; 4.
DR SUPFAM; SSF48726; SSF48726; 10.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 10.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..2013
FT /note="Cell adhesion molecule DSCAM"
FT /id="PRO_0000392478"
FT TOPO_DOM 18..1594
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1595..1615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1616..2013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..119
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 1616..2013
FT /note="Required for netrin-mediated axon repulsion of
FT neuronal growth cones"
FT /evidence="ECO:0000269|PubMed:22685302"
FT REGION 1718..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1946..1970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..1997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 666
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 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"
SQ SEQUENCE 2013 AA; 222268 MW; 1F4AF07947BEBA77 CRC64;
MWILALSLFQ SFANVFSEEP HSSLYFVNAS LQEVVFASTS GTLVPCPAAG IPPVTLRWYL
ATGEEIYDVP GIRHVHPNGT LQIFPFPPSS FSTLIHDNTY YCTAENPSGK IRSQDVHIKA
VLREPYTVRV EDQKTMRGNV AVFKCIIPSS VEAYVTVVSW EKDTVSLVSG SRFLITSTGA
LYIKDVQNED GLYNYRCITR HRYTGETRQS NSARLFVSDP ANSAPSILDG FDHRKAMAGQ
RVELPCKALG HPEPDYRWLK DNMPLELSGR FQKTVTGLLI ENSRPSDSGS YVCEVSNRYG
TAKVIGRLYV KQPLKATISP RKVKSSVGSQ VSLSCSVTGN EDQELSWYRN GEILNPGKNV
RITGLNHANL IMDHMVKSDG GAYQCFVRKD KLSAQDYVQV VLEDGTPKII SAFSEKVVSP
AEPVSLVCNV KGTPLPTVTW TLDDDPILKG SGHRISQMIT SEGNVVSYLN ISSSQVRDGG
VYRCTANNSA GVVLYQARIN VRGPASIRPM KNITAIAGRD TYIHCRVIGY PYYSIKWYKN
ANLLPFNHRQ VAFENNGTLK LSDVQKEVDE GEYTCNVLVQ PQLSTSQSVH VTVKVPPFIQ
PFEFPRFSIG QRVFIPCVVV SGDLPITITW QKDGRPIPAS LGVTIDNIDF TSSLRISNLS
LMHNGNYTCI ARNEAAAVEH QSQLIVRVPP KFVVQPRDQD GIYGKAVILN CSAEGYPVPT
IVWKFSKGAG VPQFQPIALN GRIQVLSNGS LLIKHVVEED SGYYLCKVSN DVGADVSKSM
YLTVKIPAMI TSYPNTTLAT QGQRKEMSCT AHGEKPIIVR WEKEDRIINP EMARYLVSTK
EVGEEVISTL QILPTVREDS GFFSCHAINS YGEDRGIIQL TVQEPPDPPE IEIKDVKART
ITLRWTMGFD GNSPITGYDI ECKNKSDSWD SAQRTKDVSP QLNSATIIDI HPSSTYSIRM
YAKNRIGKSE PSNEITITAD EAAPDGPPQE VHLEPTSSQS IRVTWKAPKK HLQNGIIRGY
QIGYREYSTG GNFQFNIISI DTTGDSEVYT LDNLNKFTQY GLVVQACNRA GTGPSSQEII
TTTLEDVPSY PPENVQAIAT SPESISISWS TLSKEALNGI LQGFRVIYWA NLIDGELGEI
KNVTTTQPSL ELDGLEKYTN YSIQVLAFTR AGDGVRSEQI FTRTKEDVPG PPAGVKAAAA
SASMVFVSWL PPLKLNGIIR KYTVFCSHPY PTVISEFEAS PDSFSYRIPN LSRNRQYSVW
VVAVTSAGRG NSSEIITVEP LAKAPARILT FSGTVTTPWM KDIVLPCKAV GDPSPAVKWM
KDSNGTPSLV TIDGRRSIFS NGSFIIRTVK AEDSGYYSCV ANNNWGSDEI ILNLQVQVPP
DQPRLTVSKT TSSSITLSWL PGDNGGSSIR GYILQYSEDN SEQWGSFPIS PSERSYRLEN
LKCGTWYKFT LTAQNGVGPG RISEIIEAKT LGKEPQFSKE QELFASINTT RVRLNLIGWN
DGGCPITSFT LEYRPFGTTV WTTAQRTSLS KSYILYDLQE ATWYELQMRV CNSAGCAEKQ
ANFATLNYDG STIPPLIKSV VQSEEGLTTN EGLKILVTIS CILVGVLLLF VLLLVVRRRR
REQRLKRLRD AKSLAEMLMS KNTRTSDTLS KQQQTLRMHI DIPRAQLLIE ERDTMETIDD
RSTVLLTDAD FGEAAKQKSL TVTHTVHYQS VSQATGPLVD VSDARPGTNP TTRRNAKAGP
TARNRYASQW TLNRPHPTIS AHTLTTDWRL PTPRATGSVD KESDSYSVSP SQDTDRARSS
MVSTESASST YEELARAYEH AKMEEQLRHA KFTITECFIS DTSSEQLTAG TNEYTDSLTS
STPSESGICR FTASPPKPQD GGRVVNMAVP KAHRPGDLIH LPPYLRMDFL LNRGAPGTSR
DLSLGQACLE PQKSRTLKRP TVLEPTPMEA SSSTSSTREG QQSWQQGAVA TLPQREGAEL
GQAAKMSSSQ ESLLDSRGHL KGNNPYAKSY TLV
