ID G1TW62_RABIT Unreviewed; 3381 AA.
AC G1TW62;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 24-JAN-2024, entry version 86.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 3 {ECO:0000313|Ensembl:ENSOCUP00000021305.3};
GN Name=CELSR3 {ECO:0000313|Ensembl:ENSOCUP00000021305.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000021305.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000021305.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000021305.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000021305.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000021305.3};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC {ECO:0000256|ARBA:ARBA00002066}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000256|ARBA:ARBA00010933}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AAGW02044069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; G1TW62; -.
DR STRING; 9986.ENSOCUP00000021305; -.
DR PaxDb; 9986-ENSOCUP00000021305; -.
DR Ensembl; ENSOCUT00000022227.3; ENSOCUP00000021305.3; ENSOCUG00000025952.3.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000160077; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; G1TW62; -.
DR TreeFam; TF323983; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000025952; Expressed in frontal cortex and 4 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0022008; P:neurogenesis; IEA:UniProt.
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; 3.
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 PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 3.
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 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2606..2630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2642..2662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2668..2690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2711..2731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2751..2773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2794..2813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 395..502
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 503..614
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 615..720
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 721..825
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 826..927
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 928..1030
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1031..1136
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1137..1238
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1444..1502
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1504..1540
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1544..1583
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1584..1788
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1791..1827
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1833..2013
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2015..2048
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2051..2089
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2146..2193
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2178..2251
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2607..2843
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2429..2471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2956..3010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3044..3076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3160..3311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3324..3381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2983..3010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3047..3069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3177..3192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3229..3243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3265..3281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3324..3371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1492..1501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1530..1539
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1817..1826
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2079..2088
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2146..2158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2148..2165
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2167..2176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3381 AA; 365533 MW; 14517A80E41B71EF CRC64;
MLWWGRQKPG PLAKGALARN RCAQGAAARS DRPRGGGPGR RQGPGRGPER RGGPKARTGA
GGGGGRVGRW RVMARRPPWQ GLERPSTPVL LLLLLLSLFP LSREELGGGG DQGWDPGVDL
PRARISGGAL ALCPKPPGAR EDEGPGLGVG EPVSVALRGG KQSAQSGQGS SEQPNAELAA
EHGIQALGSR ARDTGQEPRS LLCWRPEVSS CRRTGPLRRG SLSPEALSLG VPGPGNSLSL
PSDFLIQPGG PKPASFQANS GRSARKRVGT VRCCGELWVT GRRGQGERAA PSRRERTDPR
RECPPWAAES GPGLDSAPRT ARTAPLAGSA PRELRTAPEA VPRRMRSRGL ARRRFLPQRP
GPRPPGDPAA PEAWRTPPAS RARPRRAANR HPQFPQYNYQ TLVPENEAAG TAVLRVVAQD
PDAGEAGRLV YSLAALMNSR SLELFSIDPQ TGLIRTAAAL DRESMERHYL RVTAQDHGSP
RLSATTMVAV TVADRNDHAP VFEQAQYRET LRENVEEGYP ILQLRATDGD APPNANLRYR
FVGPPAARTA AAAAFEIDPR SGLISTSGRV DREHMESYEL VVEASDQGQE PGPRSATVRV
HITVLDENDN APQFSEKRYV AQVREDVRPH TVVLRVTATD RDKDANGLVH YNIISGNSRG
HFAIDSLTGE IQVVAPLDFE AEREYALRIR AQDAGRPPLS NNTGLASIQV VDINDHAPIF
VSTPFQVSVL ENAPLGHSVI HIQAVDADHG ENARLEYSLT GVAPDTPFVI NSATGWVSVS
GPLDRESVEH YFFGVEARDH GSPPLSASAS VTVTVLDVND NRPEFTMKEY HLRLNEDAAV
GTSVVSVTAV DRDANSAISY QITGGNTRNR FAISTQGGVG LVTLALPLDY KQERYFKLVL
TASDRALHDH CYVHINITDA NTHRPVFQSA HYSVSMNEDR PVGSTVVVIS ASDDDVGENA
RITYFLEDNL PQFRINADSG AITLQAPLDY EDQVTYTLAI TARDNGIPQK ADTTYVEVMV
NDVNDNAPQF VASHYTGLVS EDAPPFTSVL QISATDRDAH ANGRVQYTFQ NGEDGDGDFT
IEPTSGIVRT VRRLDREAVP VYELTAYAVD RGVPPLRTPV SIQVTVQDVN DNAPVFPAEE
FEVRVKENSI VGSVVAQITA VDPDEGPNAH IMYQIVDGNI PELFQMDIFS GELTALIDLD
YEARQEYVIV VQATSAPLVS RATVHVRLVD QNDNSPVLNN FQILFNNYVS NRSDTFPSGV
IGRIPAYDPD VSDHLFYSFE RGNELQLLVV NQTSGELRLS RKLDNNRPLV ASMLVTVTDG
LHSVTAQCVL RVIIITEELL ANSLTVRLEN MWQERFLSPL LGHFLEGVAA VLATPAEDVF
IFNIQNDTDV GGTVLNVSFS ALAPRGAGAG AAGPWFSSEE LQEQLYVRRA ALAARSLLDV
LPFDDNVCLR EPCENYMKCV SVLRFDSSAP FLASASTLFR PIQPIAGLRC RCPPGFTGDF
CETELDLCYS NPCRNGGACA RREGGYTCVC RPRFTGEDCE LDTEAGRCVP GVCRNGGTCT
DAPHGGFRCQ CPVGGAFEGP RCEVAARSFP PSSFVMFRGL RQRFHLTLSL SFATVQPSGL
LFYNGRLNEK HDFLALELVA GQVRLTYSTG ESNTVVSPTV PGGLSDGQWH TVHLRYYNKP
RTDALGSAQG PSKDKVAVLS VDDCDVAVAL QFGAEIGNYS CAAAGVQTSS KKSLDLTGPL
LLGGVPNLPE NFPVSHKDFI GCMRDLHIDG RRVDMATFVA NNGTTAGCQA KLHFCDSSPC
KNSGSCSERW GGFSCDCPVG FGGKDCRLTM AHPHHFRGNG SLSWDFGGDT VVSVPWYLGL
VFRTRATQGV LMYMQAGQHS TLLCQLERGL LSVTVARGSG RAAHLLLDQV TVSDGRWHDL
RLELQEEPGG QRGRHVLMVS LDFSLFQDTL AVGSELQGLK VKQLHVGGLP PSSKEAVPQG
LVGCIQGVWL GSTPSGAPAL PPPSHRVNVE PGCVVTNSCA SAPCPPHADC RDLWQTFSCT
CRPGYYGPGC VDACLLNPCQ NQGLCRRLPG APHGYTCDCA SGYFGHHCEH RMDQQCPRGW
WGSPTCGPCN CDVHKGFDPN CNKTNGQCHC KEFHYRPRGS DLCLPCDCYP VGSTSRSCAP
HSGQCPCRPG ALGRQCNSCD SPFAEVTASG CRVLYNACPK SLRSGVWWPQ TKFGALATVP
CPRGALGAAV RLCDEDRGWL EPDLFNCTSA AFRELSLLLD GLELNKTALD TLEAKKLAQR
LREVTGHAGH YFSQDVRVTA RLLAYLLAFE SHQQGFGLTA TQDAHFNENL LWAGSALLAP
ETGDLWAALG QRAPGGSPGS AGLVRHLEEY AATLARNMEL TYLNPVGLVT PNIMLSIDRM
EHPGPTRGAR RYPRYHSNLF RGQDAWDPHT HVLLPSQPPR PSPSEVLPTG SSAENSSVGP
PPAPPEPEPE PGMSIVILLV YRTLGGLLPA QFQAERRGAR LPQNPVMNSP VVSVAVFHGR
SFLSGLLESP ISLEFRLLQT ANRSKAICVQ WDPPGPADQH GMWTARDCEL VHRNGSHARC
RCSRTGTFGI LMDASPRERL EGDLELLAVF THVVVALSVA ALVLTAAILL SLRSLKSNVR
GIHANVAAAL GVAELLFLLG IHRTHNQLVC TAVAILLHYF FLSTFAWLLV QGLHLYRMQV
EPRNVDHGAM RFYHALGWGV PAVLLGLAVG LDPEGYGNPD FCWISIHDPL IWSFAGPVVL
VIMMNGTLFL LAAHTSCSTG QREAKKTSVL PLRSSFLLLL LVSTSWLFGL LAVNHSVLAF
HYLHAALSGL QGLAVLLLFC VLNADARAAW TPACLGRKAA PEEARPAPGT GPGAYNNTAL
FEESGLIRIT LGASTVSSVS SARSGRAQDQ DSQRGRGYLR DNVLVRHGSA ADHTDHSLQA
HAGPTDLDVA MFHRDAGADS DSDSDLSLEE ERSLSIPSSE SEDNGRTRGR FQRPLRRAAQ
SERLLTHPKD VDGNDLLSYW PALGECEAAP CALQTWGSER RLGLDSSKDA ANNNNQPDLA
LTSGDETSVG RAQRQRKGIL KNRLQYPLVP QTRGATELSW CRAATLGHRA VPAASYGRIY
AGGGTGSLSQ PASRYSSREQ LDLLLRRQLS RERLEEAPAP VLCPLNRPGS QERLDAAPGR
LEPRDRGSTL PRRQPPRDYP GAVAGRFGSR DALNLGAPRE WLSTLPPPRR PQDLDPQHPP
VSPSPQRQLS RDPLLPSRPL DSVSRSSNSR ERLDEVPSRH PSREALGPPL QLLRAREDPA
SGPSHGPSTE QLDILSSILA SFNSSALSSM QSSSTPSGPH TTATPSATAS ALGPSTPRSA
TSHSISELSP DSEVPRSEGH S
//