CELR3_MOUSE
ID CELR3_MOUSE Reviewed; 3301 AA.
AC Q91ZI0; E9QLD7; Q9ESD0;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 3;
DE Flags: Precursor;
GN Name=Celsr3;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=11850187; DOI=10.1016/s0925-4773(01)00623-2;
RA Tissir F., De-Backer O., Goffinet A.M., Lambert de Rouvroit C.A.;
RT "Developmental expression profiles of Celsr (Flamingo) genes in the
RT mouse.";
RL Mech. Dev. 112:157-160(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2574-3046, AND DEVELOPMENTAL STAGE.
RX PubMed=11677057; DOI=10.1016/s0925-4773(01)00515-9;
RA Formstone C.J., Little P.F.R.;
RT "The flamingo-related mouse Celsr family (Celsr1-3) genes exhibit distinct
RT patterns of expression during embryonic development.";
RL Mech. Dev. 109:91-94(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10790539; DOI=10.1007/s003350010073;
RA Formstone C.J., Barclay J., Rees M., Little P.F.R.;
RT "Chromosomal localization of Celsr2 and Celsr3 in the mouse; Celsr3 is a
RT candidate for the tippy (tip) lethal mutant on chromosome 9.";
RL Mamm. Genome 11:392-394(2000).
CC -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the CNS and in the eye.
CC {ECO:0000269|PubMed:10790539}.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed in the CNS, the emerging
CC dorsal root ganglia and cranial ganglia. In the CNS, expression is
CC uniform along the rostrocaudal axis. No expression is detected until
CC somite stages. Between 10 and 12 dpc, expression is strong in the
CC marginal zone (MZ), and lower in the ventricular zone (VZ). At 15 dpc,
CC expression is restricted to the brain and olfactory epithelium. In the
CC brain, it is low in VZ but strong in external fields, particularly
CC those with ongoing migration, such as the telencephalic cortical plate,
CC the olfactory bulb, the cerebellum and the tectum. In the newborn and
CC postnatal stages, expression is high in differentiated neuronal fields.
CC {ECO:0000269|PubMed:11677057, ECO:0000269|PubMed:11850187}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG17057.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF427498; AAL25099.1; -; mRNA.
DR EMBL; AC168054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF188752; AAG17057.1; ALT_FRAME; mRNA.
DR RefSeq; NP_536685.2; NM_080437.2.
DR SMR; Q91ZI0; -.
DR BioGRID; 223701; 1.
DR IntAct; Q91ZI0; 1.
DR STRING; 10090.ENSMUSP00000024238; -.
DR GlyGen; Q91ZI0; 15 sites.
DR iPTMnet; Q91ZI0; -.
DR PhosphoSitePlus; Q91ZI0; -.
DR MaxQB; Q91ZI0; -.
DR PaxDb; Q91ZI0; -.
DR PRIDE; Q91ZI0; -.
DR ProteomicsDB; 281580; -.
DR Antibodypedia; 13269; 319 antibodies from 33 providers.
DR DNASU; 107934; -.
DR Ensembl; ENSMUST00000024238; ENSMUSP00000024238; ENSMUSG00000023473.
DR GeneID; 107934; -.
DR KEGG; mmu:107934; -.
DR UCSC; uc009rrb.1; mouse.
DR CTD; 1951; -.
DR MGI; MGI:1858236; Celsr3.
DR VEuPathDB; HostDB:ENSMUSG00000023473; -.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000160077; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; Q91ZI0; -.
DR OrthoDB; 23882at2759; -.
DR PhylomeDB; Q91ZI0; -.
DR TreeFam; TF323983; -.
DR BioGRID-ORCS; 107934; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q91ZI0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91ZI0; protein.
DR Bgee; ENSMUSG00000023473; Expressed in cerebellar cortex and 111 other tissues.
DR ExpressionAtlas; Q91ZI0; baseline and differential.
DR Genevisible; Q91ZI0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IGI:MGI.
DR GO; GO:0036514; P:dopaminergic neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0097475; P:motor neuron migration; IMP:MGI.
DR GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032880; P:regulation of protein localization; IGI:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0036515; P:serotonergic neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 9.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; SSF49313; 9.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 7.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Developmental protein; Disulfide bond;
KW EGF-like domain; G-protein coupled receptor; Glycoprotein; Hydroxylation;
KW Laminin EGF-like domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..3301
FT /note="Cadherin EGF LAG seven-pass G-type receptor 3"
FT /id="PRO_0000012919"
FT TOPO_DOM 32..2531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2532..2552
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2553..2563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2564..2584
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2585..2592
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2593..2613
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2614..2634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2635..2655
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2656..2673
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2674..2694
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2695..2716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2717..2737
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2738..2744
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2745..2765
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2766..3301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 317..424
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 425..536
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 537..642
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 643..747
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 748..849
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 850..952
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 953..1058
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1059..1160
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1161..1257
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1366..1424
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1426..1460
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1464..1503
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1504..1708
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1711..1747
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1751..1933
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1935..1971
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1972..2002
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2003..2042
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2044..2079
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2066..2113
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2468..2520
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 148..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2353..2388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2823..2844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2879..2919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2969..2992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3083..3301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2353..2382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2970..2991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3101..3116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3185..3199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3228..3291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1952
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000255"
FT MOD_RES 2115
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88278"
FT MOD_RES 3042
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88278"
FT MOD_RES 3090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88278"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2042
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1370..1381
FT /evidence="ECO:0000250"
FT DISULFID 1375..1412
FT /evidence="ECO:0000250"
FT DISULFID 1414..1423
FT /evidence="ECO:0000250"
FT DISULFID 1430..1441
FT /evidence="ECO:0000250"
FT DISULFID 1435..1450
FT /evidence="ECO:0000250"
FT DISULFID 1452..1459
FT /evidence="ECO:0000250"
FT DISULFID 1468..1479
FT /evidence="ECO:0000250"
FT DISULFID 1473..1489
FT /evidence="ECO:0000250"
FT DISULFID 1491..1502
FT /evidence="ECO:0000250"
FT DISULFID 1682..1708
FT /evidence="ECO:0000250"
FT DISULFID 1715..1726
FT /evidence="ECO:0000250"
FT DISULFID 1720..1735
FT /evidence="ECO:0000250"
FT DISULFID 1737..1746
FT /evidence="ECO:0000250"
FT DISULFID 1904..1933
FT /evidence="ECO:0000250"
FT DISULFID 1939..1950
FT /evidence="ECO:0000250"
FT DISULFID 1944..1959
FT /evidence="ECO:0000250"
FT DISULFID 1961..1970
FT /evidence="ECO:0000250"
FT DISULFID 1974..1985
FT /evidence="ECO:0000250"
FT DISULFID 1979..1997
FT /evidence="ECO:0000250"
FT DISULFID 1999..2008
FT /evidence="ECO:0000250"
FT DISULFID 2016..2029
FT /evidence="ECO:0000250"
FT DISULFID 2031..2041
FT /evidence="ECO:0000250"
FT DISULFID 2048..2063
FT /evidence="ECO:0000250"
FT DISULFID 2050..2066
FT /evidence="ECO:0000250"
FT DISULFID 2068..2078
FT /evidence="ECO:0000250"
FT DISULFID 2087..2096
FT /evidence="ECO:0000250"
FT DISULFID 2099..2111
FT /evidence="ECO:0000250"
FT CONFLICT 221
FT /note="D -> E (in Ref. 1; AAL25099)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="S -> G (in Ref. 1; AAL25099)"
FT /evidence="ECO:0000305"
FT CONFLICT 2713
FT /note="L -> LR (in Ref. 3; AAG17057)"
FT /evidence="ECO:0000305"
FT CONFLICT 3024
FT /note="R -> P (in Ref. 3; AAG17057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3301 AA; 358478 MW; 29EA6A0D1E5A75AF CRC64;
MARRPLWWGL PGPSTPVLLL LLLSLFPFSR EELGGGGDQD WDPGVATTTG PRAQIGSGAV
ALCPESPGVW EDGDPGLGVR EPVFMRLRVG RQNARNGRGA PEQPNAEVVV QALGSREQEA
GQGPGYLLCW HPEISSCGRT GPLRRGSLPL DALSPGDSDL RNSSPHPSEL LAQPDGSRPV
AFQRNARRSI RKRVETSRCC GKLWEPGHKG QGERSATSTV DRGPFRRDCL PGSLGSGLGE
DSAPRAVRTA PTPGSAPRES RTAPGRMRSR GLFRRRFLFE RPGPRPPGFP TGPEAKQILS
TNQARPRRAA NRHPQFPQYN YQTLVPENEA AGTSVLRVVA QDPDPGEAGR LIYSLAALMN
SRSLELFSID PQSGLIRTAA ALDRESMERH YLRVTAQDHG SPRLSATTMV AVTVADRNDH
APVFEQAQYR ETLRENVEEG YPILQLRATD GDAPPNANLR YRFVGSPAVR TAAAAAFEID
PRSGLISTSG RVDREHMESY ELVVEASDQG QEPGPRSATV RVHITVLDEN DNAPQFSEKR
YVAQVREDVR PHTVVLRVTA TDKDKDANGL VHYNIISGNS RGHFAIDSLT GEIQVMAPLD
FEAEREYALR IRAQDAGRPP LSNNTGLASI QVVDINDHAP IFVSTPFQVS VLENAPLGHS
VIHIQAVDAD HGENSRLEYS LTGVASDTPF VINSATGWVS VSGPLDRESV EHYFFGVEAR
DHGSPPLSAS ASVTVTVLDV NDNRPEFTMK EYHLRLNEDA AVGTSVVSVT AVDRDANSAI
SYQITGGNTR NRFAISTQGG VGLVTLALPL DYKQERYFKL VLTASDRALH DHCYVHINIT
DANTHRPVFQ SAHYSVSMNE DRPVGSTVVV ISASDDDVGE NARITYLLED NLPQFRIDAD
SGAITLQAPL DYEDQVTYTL AITARDNGIP QKADTTYVEV MVNDVNDNAP QFVASHYTGL
VSEDAPPFTS VLQISATDRD AHANGRVQYT FQNGEDGDGD FTIEPTSGIV RTVRRLDREA
VPVYELTAYA VDRGVPPLRT PVSIQVTVQD VNDNAPVFPA EEFEVRVKEN SIVGSVVAQI
TAVDPDDGPN AHIMYQIVEG NIPELFQMDI FSGELTALID LDYEARQEYV IVVQATSAPL
VSRATVHVRL VDQNDNSPVL NNFQILFNNY VSNRSDTFPS GIIGRIPAYD PDVSDHLFYS
FERGNELQLL VVNRTSGELR LSRKLDNNRP LVASMLVTVT DGLHSVTAQC VLRVVIITEE
LLANSLTVRL ENMWQERFLS PLLGHFLEGV AAVLATPTED VFIFNIQNDT DVGGTVLNVS
FSALAPRGAG AGAAGPWFSS EELQEQLYVR RAALAARSLL DVLPFDDNVC LREPCENYMK
CVSVLRFDSS APFLASTSTL FRPIQPIAGL RCRCPPGFTG DFCETELDLC YSNPCRNGGA
CARREGGYTC VCRPRFTDCE LDTEAGRCVP GVCRNGGTCT NAPNGGFRCQ CPAGGAFEGP
RCEVAARSFP PSSFVMFRGL RQRFHLTLSL SFATVQPSGL LFYNGRLNEK HDFLALELVA
GQVRLTYSTG ESNTVVSPTV PGGLSDGQWH TVHLRYYNKP RTDALGGAQG PSKDKVAVLS
VDDCNVAVAL QFGAEIGNYS CAAAGVQTSS KKSLDLTGPL LLGGVPNLPE NFPVSHKDFI
GCMRDLHIDG RRMDMAAFVA NNGTMAGCQA KSHFCASGPC KNNGFCSERW GGFSCDCPVG
FGGKDCRLTM AHPYHFQGNG TLSWDFGNDM AVSVPWYLGL SFRTRATKGI LMQVQLGPHS
VLLCKLDRGL LSVTLNRASG HTVHLLLDQM TVSDGRWHDL RLELQEEPGG RRGHHIFMVS
LDFTLFQDTM AMGGELQGLK VKQLHVGGLP PSSKEEGHQG LVGCIQGVWI GFTPFGSSAL
LPPSHRVNVE PGCTVTNPCA SGPCPPHADC KDLWQTFSCT CRPGYYGPGC VDACLLNPCQ
NQGSCRHLQG APHGYTCDCV SGYFGQHCEH RVDQQCPRGW WGSPTCGPCN CDVHKGFDPN
CNKTNGQCHC KEFHYRPRGS DSCLPCDCYP VGSTSRSCAP HSGQCPCRPG ALGRQCNSCD
SPFAEVTASG CRVLYDACPK SLRSGVWWPQ TKFGVLATVP CPRGALGAAV RLCDEDQGWL
EPDLFNCTSP AFRELSLLLD GLELNKTALD TVEAKKLAQR LREVTGQTDH YFSQDVRVTA
RLLAYLLAFE SHQQGFGLTA TQDAHFNENL LWAGSALLAP ETGHLWAALG QRAPGGSPGS
AGLVQHLEEY AATLARNMEL TYLNPVGLVT PNIMLSIDRM EHPSSTQGAR RYPRYHSNLF
RGQDAWDPHT HVLLPSQASQ PSPSEVLPTS SNAENATASS VVSPPAPLEP ESEPGISIVI
LLVYRALGGL LPAQFQAERR GARLPQNPVM NSPVVSVAVF HGRNFLRGVL VSPINLEFRL
LQTANRSKAI CVQWDPPGPT DQHGMWTARD CELVHRNGSH ARCRCSRTGT FGVLMDASPR
ERLEGDLELL AVFTHVVVAV SVTALVLTAA VLLSLRSLKS NVRGIHANVA AALGVAELLF
LLGIHRTHNQ LLCTAVAILL HYFFLSTFAW LLVQGLHLYR MQVEPRNVDR GAMRFYHALG
WGVPAVLLGL AVGLDPEGYG NPDFCWISIH EPLIWSFAGP IVLVIVMNGT MFLLAARTSC
STGQREAKKT SVLTLRSSFL LLLLVSASWL FGLLAVNHSI LAFHYLHAGL CGLQGLAVLL
LFCVLNADAR AAWTPACLGK KAAPEETRPA PGPGSGAYNN TALFEESGLI RITLGASTVS
SVSSARSGRA QDQDSQRGRS YLRDNVLVRH GSTAEHTERS LQAHAGPTDL DVAMFHRDAG
ADSDSDSDLS LEEERSLSIP SSESEDNGRT RGRFQRPLRR AAQSERLLAH PKDVDGNDLL
SYWPALGECE AAPCALQAWG SERRLGLDSN KDAANNNQPE LALTSGDETS LGRAQRQRKG
ILKNRLQYPL VPQSRGTPEL SWCRAATLGH RAVPAASYGR IYAGGGTGSL SQPASRYSSR
EQLDLLLRRQ LSKERLEEVP VPAPVLHPLS RPGSQERLDT APARLEARDR GSTLPRRQPP
RDYPGTMAGR FGSRDALDLG APREWLSTLP PPRRNRDLDP QHPPLPLSPQ RQLSRDPLLP
SRPLDSLSRI SNSREGLDQV PSRHPSREAL GPAPQLLRAR EDPASGPSHG PSTEQLDILS
SILASFNSSA LSSVQSSSTP SGPHTTATAS ALGPSTPRSA TSHSISELSP DSEVPRSEGH
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