RELN_RAT
ID RELN_RAT Reviewed; 3462 AA.
AC P58751; Q80T65;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Reelin;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Reln;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RA Kikkawa S., Terashima T.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE.
RC TISSUE=Cerebellum;
RX PubMed=12670697; DOI=10.1016/s0169-328x(02)00650-2;
RA Yokoi N., Namae M., Wang H.-W., Kojima K., Fuse M., Yasuda K., Serikawa T.,
RA Seino S., Komeda K.;
RT "Rat neurological disease creeping is caused by a mutation in the reelin
RT gene.";
RL Brain Res. Mol. Brain Res. 112:1-7(2003).
RN [3]
RP ALTERNATIVE SPLICING.
RX PubMed=10328932; DOI=10.1006/exnr.1999.7019;
RA Lambert de Rouvroit C., Bernier B., Royaux I., de Bergeyck V.,
RA Goffinet A.M.;
RT "Evolutionarily conserved, alternative splicing of reelin during brain
RT development.";
RL Exp. Neurol. 156:229-238(1999).
CC -!- FUNCTION: Extracellular matrix serine protease that plays a role in
CC layering of neurons in the cerebral cortex and cerebellum. Regulates
CC microtubule function in neurons and neuronal migration. Affects
CC migration of sympathetic preganglionic neurons in the spinal cord,
CC where it seems to act as a barrier to neuronal migration. Enzymatic
CC activity is important for the modulation of cell adhesion. Binding to
CC the extracellular domains of lipoprotein receptors VLDLR and
CC LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of
CC TAU phosphorylation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomer of disulfide-linked homodimers. Binds to the
CC ectodomains of VLDLR and LRP8/APOER2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P58751-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58751-2; Sequence=VSP_005579;
CC Name=3;
CC IsoId=P58751-3; Sequence=VSP_005580;
CC -!- TISSUE SPECIFICITY: Abundantly produced during brain ontogenesis by the
CC Cajal-Retzius cells and other pioneer neurons located in the
CC telencephalic marginal zone and by granule cells of the external
CC granular layer of the cerebellum.
CC -!- DOMAIN: The basic C-terminal region is essential for secretion.
CC {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Reln are the cause of the creeping phenotype,
CC which is characterized by tremor, gait ataxia, cerebellar hypoplasia
CC and abnormal neuronal migration (particularly in the cerebral cortex
CC and hippocampus). The mutation is due to a nucleotide insertion at
CC codon 1892 which results in a translational frameshift and truncation
CC of the protein. {ECO:0000269|PubMed:12670697}.
CC -!- SIMILARITY: Belongs to the reelin family. {ECO:0000305}.
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DR EMBL; AB049473; BAB78470.1; -; mRNA.
DR EMBL; AB062680; BAC75467.1; -; mRNA.
DR RefSeq; NP_536319.2; NM_080394.2.
DR SMR; P58751; -.
DR BioGRID; 246846; 1.
DR STRING; 10116.ENSRNOP00000058574; -.
DR GlyGen; P58751; 20 sites.
DR iPTMnet; P58751; -.
DR PhosphoSitePlus; P58751; -.
DR PaxDb; P58751; -.
DR PRIDE; P58751; -.
DR GeneID; 24718; -.
DR KEGG; rno:24718; -.
DR CTD; 5649; -.
DR RGD; 3553; Reln.
DR eggNOG; ENOG502QSIP; Eukaryota.
DR InParanoid; P58751; -.
DR OrthoDB; 9177at2759; -.
DR PhylomeDB; P58751; -.
DR Reactome; R-RNO-8866376; Reelin signalling pathway.
DR PRO; PR:P58751; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0110157; C:reelin complex; ISO:RGD.
DR GO; GO:0070325; F:lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISS:UniProtKB.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0021800; P:cerebral cortex tangential migration; ISS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0021542; P:dentate gyrus development; IMP:RGD.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0021854; P:hypothalamus development; IEP:RGD.
DR GO; GO:0097477; P:lateral motor column neuron migration; ISO:RGD.
DR GO; GO:0021819; P:layer formation in cerebral cortex; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; IMP:RGD.
DR GO; GO:0007616; P:long-term memory; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0007613; P:memory; IEP:RGD.
DR GO; GO:0007494; P:midgut development; IEP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; ISO:RGD.
DR GO; GO:0021769; P:orbitofrontal cortex development; IEP:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; ISO:RGD.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISO:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:1902078; P:positive regulation of lateral motor column neuron migration; ISO:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISO:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:RGD.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISO:RGD.
DR GO; GO:0035418; P:protein localization to synapse; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0097120; P:receptor localization to synapse; ISO:RGD.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0050795; P:regulation of behavior; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISO:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0048265; P:response to pain; ISS:UniProtKB.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0035176; P:social behavior; IEP:RGD.
DR GO; GO:0021511; P:spinal cord patterning; IEP:RGD.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISO:RGD.
DR GO; GO:0021517; P:ventral spinal cord development; ISO:RGD.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.60.40.4060; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR InterPro; IPR034968; Reelin.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR11841; PTHR11841; 12.
DR Pfam; PF02014; Reeler; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF50939; SSF50939; 4.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51019; REELIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Developmental protein;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..3462
FT /note="Reelin"
FT /id="PRO_0000030306"
FT DOMAIN 28..192
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT REPEAT 594..605
FT /note="BNR 1"
FT DOMAIN 672..703
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 800..811
FT /note="BNR 2"
FT REPEAT 953..964
FT /note="BNR 3"
FT DOMAIN 1031..1062
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1158..1169
FT /note="BNR 4"
FT REPEAT 1324..1335
FT /note="BNR 5"
FT DOMAIN 1410..1443
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1536..1547
FT /note="BNR 6"
FT REPEAT 1687..1698
FT /note="BNR 7"
FT DOMAIN 1766..1797
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1885..1896
FT /note="BNR 8"
FT REPEAT 2044..2055
FT /note="BNR 9"
FT DOMAIN 2130..2162
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2251..2262
FT /note="BNR 10"
FT REPEAT 2400..2411
FT /note="BNR 11"
FT DOMAIN 2479..2510
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2599..2610
FT /note="BNR 12"
FT REPEAT 2779..2790
FT /note="BNR 13"
FT DOMAIN 2854..2885
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 2980..2991
FT /note="BNR 14"
FT REPEAT 3144..3156
FT /note="BNR 15"
FT DOMAIN 3229..3261
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 3364..3375
FT /note="BNR 16"
FT BINDING 2062
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2075
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1922
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2963
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3074
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 156..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 541..582
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 610..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 676..686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 693..702
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 896..938
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 969..976
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1035..1045
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1052..1061
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1272..1311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1340..1349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1634..1674
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1703..1710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2102
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2134..2144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2138..2150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2152..2161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2196..2236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2349..2388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2394..2560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2483..2493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2487..2498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2500..2509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2545..2585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2795..2802
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2920..2967
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3161..3171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3233..3243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3237..3249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3251..3260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3297..3347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 3430..3462
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005580"
FT VAR_SEQ 3430..3431
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005579"
FT CONFLICT 336
FT /note="H -> R (in Ref. 2; BAC75467)"
FT /evidence="ECO:0000305"
FT CONFLICT 2714
FT /note="V -> L (in Ref. 2; BAC75467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3462 AA; 387531 MW; FCCF89B090E035F6 CRC64;
MERGCWAPRT LVLAVLLLLL ATLRARAATG YYPRFSPFFF LCTHHGELEG DGEQGEVLIS
LHIAGNPTYY VPGQEYHVTI STSTFFDGLL VTGLYTSTSI QSSQSIGGSS AFGFGIMSDH
QFGNQFMCSV VASHVSHLPT TNLSFVWIAP PAGTGCVNFM ATATHRGQVI FKDALAQQLC
EQGAPTEATA YSHLAEIHSD SVILRDDFDS YHQLELNPNI WAECSNCDTG EQCGTIMHGN
AVTFCEPYGP RELTTTYLNT TTASVLQFSI GSGSCRFSYS DPSIIVSYAK NNTADWIQLE
KIRAPSNVST IIHILYLPED AKGENVQFQW KQDSLHVGEV YEACWALDNI LVINSAHRQV
ILEDSLDPVD TGNWLFFPGA TVKHSCQSDG NAIYFHGNEG SQLNFATTRD VDLSTEDIQE
QWSEEFESQP TGWDILGAVV GSECGTIESG LSLVFLKDGE RKLCTPYMDT TGYGNLRFYF
AMGGTCDPGD SHENDVILYA KIEGKKEHIA LDTLSYSSYK VPTLVSVVIN PELQTPATKF
CLRQKNHQGH NQNVWAVDFF HVLPILPSTM SHMIQFSINL GCGTHQPGNS VSLEFSTNHG
RSWSLLHTEC LPEICAGPHL PHSTIYSSEN YSGWNRVTIP LPNAALTRDT RIRWRQTGPI
LGNMWAIDNV YIGPSCLKFC SGRGQCTRHG CKCDPGFSGP ACEMASQTFP MFISESFGSS
RLSSYHNFYS IRGAEVSFGC GVLASGKALV FNKDGRRQLI TSFLDSSQSR FLQFTLRLGS
KSVLSTCRAP DQPGEGVLLH YSYDNGITWK LLEHYSYLNY HEPRIISVEL PDDAKQFGIQ
FRWWQPYHSS QGEDVWAIDE ILMTSVLFNS ISLDFTNLVE VTQSLGFYLG NIQPYCGHDW
TLCFTGDSKL ASSMRYVETQ SMQIGASYMI QFSLVMGCGQ KYTPHMDNQV KLEYSTNHGL
TWHLVQDECL PSMPSCQEFT SASIYHASEF TQWRRVTVIL PQKTWSGATR FRWSQSYYTA
QDEWALDDIY IGQQCPNMCS GHGSCDHGVC RCDQGYQGTE CHPEAALPST IMSDFENPSS
WDSDWQEVIG GEVVKPEQGC GVVSSGSSLY FSKAGKRQLV SWDLDTSWVD FVQFYIQIGG
ESAACNKPDS REEGVLLQYS NNGGIQWHLL AEMYFSDFGK PRFVYLELPA AAKTPCTRFR
WWQPVFSGED YDQWAVDDII ILSEKQKQVI PVVNPTLPQN FYEKPAFDYP INQMSVWLML
ANEGMAKNDS FCATTPSAMV FGKSDGDRFA VTRDLTLKPG YVLQFKLNIG CASQFSSTAP
VLLQYSHDAG MSWFLVKEGC FPASAGKGCE GNSRELSEPT VYYTGDFEEW TRVTIAIPRS
LASSKTRFRW IQESSSQKNV PPFGLDGVYI SEPCPSYCSG HGDCISGVCF CDLGYTAAQG
TCVSNIPNHS EMFDRFEGKL SPLWYKISGG QVGTGCGTLS DGRSLYFNGL GKREARTVPL
DTRNIRLVQF YIQIGSKTSG ITCIKPRARN EGLVVQYSND NGILWHLLRE LDFLSFLEPQ
IISIDLPREA KTPATAFRWW QPQHGKHSAQ WALDDVLIGV NDSSQTGFQD KFDGSIDLQA
NWYRIQGGQV DIDCLSMDTA LIFTENIGKP RYAETWDFHV SASSFLQFDM SMGCSKPFSA
THSVQLQYSL NNGKDWHPVT EECVPPTIGC VHYTESSTYT SERFQNWRRV TVYLPLATNS
PRTRFRWIQA NYTMGADAWA IDNVLLASGC PWLCSGRGIC DSGRCVCDRG FGGPFCVPVV
PLPSILKDDF NGNLHPDLWP EVYGAERGNL NGETIKSGTS LIFKGEGLRM LISRDLDCTN
TMYVQFSLRF IAKGTPERSH SILLQSSING GVTWRLMDEF YFPQTTSILF INVPLPYSAQ
TNATRFRLWQ PYNNGKKEEI WIIDDFIIDG DNLNNPVMLL DTFDFGPRED NWFFYPGGNI
GLYCPYSSKG APEEDSAMVF VSNEIGEHSI TTRDLSVNEN TIIQFEINVG CSTDSSSADP
VRLEFSRDFG ATWHLLLPLC YHSSSLVSSL CSTEHHPSST YYAGTTQGWR REVVHFGKLH
LCGSVRFRWY QGFYPAGSQP VTWAIDNVYI GPQCEEMCCG HGSCVNGTKC ICDPGYSGPT
CKISTKNPDF LKDDFEGQLE SDRFLLMSGG KPSRKCGILS SGNNLFFNED GLRMLVTRDL
DLSHARFVQF FMRLGCGKGV PDPRSQPVLL QYSLNGGLSW SLLQEFLFSN SSNVGRYIAL
EMPLKARSGS TRLRWWQPSE NGHFYSPWVI DQILIGGNIS GNTVLEDDFS TLDSRKWLLH
PGGTKMPVCG STGDALVFIE KASTRYVVTT DIAVNEDSFL QIDFAASCSV TDSCYAIELE
YSVDLGLSWH PLVRDCLPTN VECSRYHLQR ILVSDTFNKW TRITLPLPAY TRSQATRFRW
HQPAPFDKQQ TWAIDNVYIG DGCLDMCSGH GRCIQGSCVC DEQWGGLYCD EPETSLPTQL
KDNFNRAPSN QNWLTVNGGK LSTVCGAVAS GLALHFSGGC SRLLVTVDLN LTNAEFIQFY
FMYGCLITPS NRNQGVLLEY SVNGGITWTL LMEIFYDQYS KPGFVNILLP PDAKEIGTRF
RWWQPRHDGL DQNDWAIDNV LISGSADQRT VMLDTFSSAP VPQHERSPAD AGPVGRIAFD
MFMEDKTSVN ENWVFHDDCT VERFCDSPDG VMLCGSHDGR EVYAVTHDLT PTENWIMQFK
ISVGCKVPEK IAQNQIHVQF STDFGVSWSY LVPQCLPADP KCSGTVSQPS VFFPTKGWKR
ITYPLPESLM GNPVRFRFYQ KYSDVQWAID NFYLGPGCLD NCGGHGDCLK EQCICDPGYS
GPHCYLTHTL KTFLKERFDS EEIKPDLWMS LEGGSTCTEC GILAENTALY FGGSTVRQAI
TQDLDLRGAK FLQYWGRIGS ENNMTSCHRP VCRKEGVLLD YSKDGGITWT LLHEMDFQKY
ISVRHDYILL PEGALTNTTR LRWWQPFVIS NGLVVSGVER AQWALDNILI GGAEINPSQL
VDTFDDEGSS HEENWSFYPN AVRTAGFCGN PSFHLYWPNK KKDKTHNALS SRELIIQPGY
MMQFKIVVGC EATSCGDLHS VMLEYTKDAR SDSWQLVQTQ CLPSSSNSIG CSPFQFHEAT
IYNAVNSSSW KRITIQLPDH VSSSATQFRW IQKGEETEKQ SWAIDHVYIG EACPRLCSGH
GYCTTGAVCI CDESFQGDDC SVFSHELPSY IKDNFESARV TEANWETIQG GAIGSGCGQL
APYAHGDSLY FNGCQIRQAA TKPLDLTRAS KIMFVLQIGS TAQTDSCNSD LSGPHTVDKA
VLLQYSVNNG ITWHVIAQHQ PKDFTQAQRV SYNVPLEARM KGVLLRWWQP RHNGTGHDQW
ALDHVEVVLV STRKQNYMMN FSRQHGLRHF YNRRRRSLRR YP
