GenomeNet

Database: UniProt
Entry: G1TW62_RABIT
LinkDB: G1TW62_RABIT
Original site: G1TW62_RABIT 
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
//
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