ID CELR3_RAT Reviewed; 3313 AA.
AC O88278;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 24-JAN-2024, entry version 183.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 3;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 2;
DE Short=Multiple EGF-like domains protein 2;
DE Flags: Precursor;
GN Name=Celsr3; Synonyms=Megf2;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT "Identification of high-molecular-weight proteins with multiple EGF-like
RT motifs by motif-trap screening.";
RL Genomics 51:27-34(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2117; TYR-3050 AND SER-3098,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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 brain. Expressed in cerebellum,
CC olfactory bulb, cerebral cortex, hippocampus and brain stem.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AB011528; BAA32459.1; -; mRNA.
DR RefSeq; NP_112610.1; NM_031320.1.
DR SMR; O88278; -.
DR STRING; 10116.ENSRNOP00000068821; -.
DR GlyCosmos; O88278; 15 sites, No reported glycans.
DR GlyGen; O88278; 15 sites.
DR iPTMnet; O88278; -.
DR PhosphoSitePlus; O88278; -.
DR PaxDb; 10116-ENSRNOP00000041011; -.
DR Ensembl; ENSRNOT00000112823.1; ENSRNOP00000079747.1; ENSRNOG00000053889.2.
DR Ensembl; ENSRNOT00055011835; ENSRNOP00055009347; ENSRNOG00055007121.
DR Ensembl; ENSRNOT00060028987; ENSRNOP00060023340; ENSRNOG00060016910.
DR Ensembl; ENSRNOT00065010630; ENSRNOP00065007851; ENSRNOG00065006816.
DR GeneID; 83466; -.
DR KEGG; rno:83466; -.
DR UCSC; RGD:621787; rat.
DR AGR; RGD:621787; -.
DR CTD; 1951; -.
DR RGD; 621787; Celsr3.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000160077; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; O88278; -.
DR OMA; ECETRWG; -.
DR OrthoDB; 4006628at2759; -.
DR PhylomeDB; O88278; -.
DR PRO; PR:O88278; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000053889; Expressed in cerebellum and 7 other cell types or tissues.
DR Genevisible; O88278; RN.
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; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0036514; P:dopaminergic neuron axon guidance; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0097475; P:motor neuron migration; ISO:RGD.
DR GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0036515; P:serotonergic neuron axon guidance; ISO:RGD.
DR CDD; cd11304; Cadherin_repeat; 9.
DR CDD; cd00054; EGF_CA; 5.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 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_7TM.
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 PANTHER; PTHR24026:SF38; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 3; 1.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 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; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF111418; Hormone receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 7.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 6.
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 1: Evidence at protein 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..3313
FT /note="Cadherin EGF LAG seven-pass G-type receptor 3"
FT /id="PRO_0000012920"
FT TOPO_DOM 32..2538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2539..2559
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2560..2570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2571..2591
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2592..2599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2600..2620
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2621..2641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2642..2662
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2663..2679
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2680..2700
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2701..2724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2725..2745
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2746..2752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2753..2773
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2774..3313
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..1462
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1466..1505
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1506..1710
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1713..1749
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1753..1935
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1937..1972
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1973..2011
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2012..2044
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2046..2081
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2068..2115
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2475..2527
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 148..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2356..2395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2887..2927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2977..3004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3091..3242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3255..3313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2360..2386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2978..2999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3109..3124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3197..3211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3255..3303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1954
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000255"
FT MOD_RES 2117
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 3050
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 3098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
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 1640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2504
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..1461
FT /evidence="ECO:0000250"
FT DISULFID 1470..1481
FT /evidence="ECO:0000250"
FT DISULFID 1475..1491
FT /evidence="ECO:0000250"
FT DISULFID 1493..1504
FT /evidence="ECO:0000250"
FT DISULFID 1684..1710
FT /evidence="ECO:0000250"
FT DISULFID 1717..1728
FT /evidence="ECO:0000250"
FT DISULFID 1722..1737
FT /evidence="ECO:0000250"
FT DISULFID 1739..1748
FT /evidence="ECO:0000250"
FT DISULFID 1906..1935
FT /evidence="ECO:0000250"
FT DISULFID 1941..1952
FT /evidence="ECO:0000250"
FT DISULFID 1946..1961
FT /evidence="ECO:0000250"
FT DISULFID 1963..1972
FT /evidence="ECO:0000250"
FT DISULFID 1976..1987
FT /evidence="ECO:0000250"
FT DISULFID 1981..1999
FT /evidence="ECO:0000250"
FT DISULFID 2001..2010
FT /evidence="ECO:0000250"
FT DISULFID 2018..2031
FT /evidence="ECO:0000250"
FT DISULFID 2033..2043
FT /evidence="ECO:0000250"
FT DISULFID 2050..2065
FT /evidence="ECO:0000250"
FT DISULFID 2052..2068
FT /evidence="ECO:0000250"
FT DISULFID 2070..2080
FT /evidence="ECO:0000250"
FT DISULFID 2089..2098
FT /evidence="ECO:0000250"
FT DISULFID 2101..2113
FT /evidence="ECO:0000250"
SQ SEQUENCE 3313 AA; 359355 MW; B11DA09517288764 CRC64;
MARRPLWWGL PGPSTPLLLL LLFSLFPSSR EEMGGGGDQG WDPGVATATG PRAQIGSGAV
ALCPESPGVW EDGDPGLGVR EPVFMKLRVG RQNARNGRGA PEQPNREPVV QALGSREQEA
GQGSGYLLCW HPEISSCGRT GHLRRGSLPL DALSPGDSDL RNSSPHPSEL LAQPDSPRPV
AFQRNGRRSI RKRVETFRCC GKLWEPGHKG QGERSATSTV DRGPLRRDCL PGSLGSGLGE
DSAPRAVRTA PAPGSAPHES RTAPERMRSR GLFRRGFLFE RPGPRPPGFP TGAEAKRILS
TNQARSRRAA NRHPQFPQYN YQTLVPENEA AGTAVLRVVA QDPDPGEAGR LVYSLAALMN
SRSLELFSID PQSGLIRTAA ALDRESMERH YLRVTAQDHG SPRLSATTMV AVTVADRNDH
APVFEQAQYR ETLRENVEEG YPILQLRATD GDAPPNANLR YRFVGSPAAR TAAAAAFEID
PRSGLISTSG RVDREHMESY ELVVEASDQG QEPGPRSATV RVHITVLDEN DNAPQFSEKR
YVAQVREDVR PHTVVLRVTA TDKDKDANGL VHYNIISGNS RGHFAIDSLT GEIQVMAPLD
FEAEREYALR IRAQDAGRPP LSNNTGLASI QVVDINDHSP IFVSTPFQVS VLENAPLGHS
VIHIQAVDAD HGENSRLEYS LTGVASDTPF VINSATGWVS VSGPLDRESV EHYFFGVEAR
DHGSPPLSAS ASVTVTVLDV NDNRPEFTMK EYHLRLNEDA AVGTSVVSVT AVDRDANSAI
SYQITGGNTR NRFAISTQGG MGLVTLALPL 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 VVNQTSGELR LSRKLDNNRP LVASMLVTVT DGLHSVTAQC VLRVVIITEE
LLANSLTVRL ENMWQERFLS PLLGHFLEGV AAVLATPTED VFIFNIQNDT DVGGTVLNVS
FSALAPRGAG AGAAGPWFSS EELQEQLYVR RAALAARSLL DVLPFDDNVC LREPCENYMK
CVSVLRFDSS APFLASASTL FRPIQPIAGL RCRCPPGFTG DFCETELDLC YSNPCRNGGA
CARREGGYTC VCRPRFTGED CELDTEAGRC VPGVCRNGGT CTNAPNGGFR CQCPAGGAFE
GPRCEVAARS FPPSSFVMFR GLRQRFHLTL SLSFATVQPS GLLFYNGRLN EKHDFLALEL
VAGQVRLTYS TGESSTVVSP TVPGGLSDGQ WHTVHLRYYN KPRTDALGGA QGPSKDKVAV
LSVDDCNVAV ALRFGAEIGN YSCAAAGVQT SSKKSLDLTG PLLLGGVPNL PENFPVSRKD
FIGCMRDLHI DGRRVDMAAF VANNGTTAGC QAKSHFCASG PCKNGGLCSE RWGGFSCDCP
VGFGGKDCRL TMAHPYHFQG NGTLSWDFGN DMPVSVPWYL GLSFRTRATK GVLMQVQLGP
HSVLLCKLDQ GLLSVTLSRA SGHAVHLLLD QMTVSDGRWH DLRLELQEEP GGRRGHHIFM
VSLDFTLFQD TMAMGSELEG LKVKHLHVGG PPPSSKEEGP QGLVGCIQGV WTGFTPFGSS
ALPPPSHRIN VEPGCTVTNP CASGPCPPHA NCKDLWQTFS CTCWPGYYGP GCVDACLLNP
CQNQGSCRHL QGGPHGYTCD CASGYFGQHC EHRMDQQCPR GWWGSPTCGP CNCDVHKGFD
PNCNKTSGQC HCKEFHYRPR GSDSCLPCDC YPVGSTSRSC APHSGQCPCR PGALGRQCNS
CDSPFAEVTA SGCRVLYDAC PKSLRSGVWW PQTKFGVLAT VPCPRGALGL RGTGAAVRLC
DEDHGWLEPD FFNCTSPAFR ELSLLLDGLE LNKTALDTVE AKKLAQRLRE VTGQTDHYFS
QDVRVTARLL AYLLAFESHQ QGFGLTATQD AHFNENLLWA GSALLAPETG DLWAALGQRA
PGGSPGSAGL VRHLEEYAAT LARNMDLTYL NPVGLVTPNI MLSIDRMEQP SSSQGAHRYP
RYHSNLFRGQ DAWDPHTHVL LPSQSPQPSP SEVLPTSSNA ENATASGVVS PPAPLEPESE
PGISIVILLV YRALGGLLPA QFQAERRGAR LPQNPVMNSP VVSVAVFRGR NFLRGALVSP
INLEFRLLQT ANRSKAICVQ WDPPGPADQH GMWTARDCEL VHRNGSHARC RCSRTGTFGV
LMDASPRERL EGDLELLAVF THVVVAASVT ALVLTAAVLL SLRSLKSNVR GIHANVAAAL
GVAELLFLLG IHRTHNQLLC TVVAILLHYF FLSTFAWLLV QGLHLYRMQV EPRNVDRGAM
RFYHALGWGV PAVLLGLAVG LDPEGYGNPD FCWISIHEPL IWSFAGPIVL VIVMNGIMFL
LAARTSCSTG QREAKKTSVL RTLRSSFLLL LLVSASWLFG LLAVNHSVLA FHYLHAGLCG
LQGLAVLLLF CVLNADARAA WTPACLGKKA APEETRPAPG PGSGAYNNTA LFEESGLIRI
TLGASTVSSV SSARSGRAQD QDSQRGRSYL RDNVLVRHGS TAEHAEHSLQ AHAGPTDLDV
AMFHRDAGAD SDSDSDLSLE EERSLSIPSS ESEDNGRTRG RFQRPLRRAA QSERLLAHPK
DVDGNDLLSY WPALGECEAA PCALQAWGSE RRLGLDSNKD AANNNQPELA LTSGDETSLG
RAQRQRKGIL KNRLQYPLVP QTRGTPELSW CRAATLGHRA VPAASYGRIY AGGGTGSLSQ
PASRYSSREQ LDLLLRRQLS RERLEEVPVP APVLHPLSRP GSQERLDTAP ARLEPRDRGS
TLPRRQPPRD YPGTMAGRFG SRDALDLGAP REWLSTLPPP RRNRDLDPQH PPLPLSPQRP
LSRDPLLPSR PLDSLSRISN SRERLDQVPS RHPSREALGP APQLLRARED PASGPSHGPS
TEQLDILSSI LASFNSSALS SVQSSSTPSG PHTTATPSAT ASALGPSTPR SATSHSISEL
SPDSEVPRSE GHS
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