ID G3RKM9_GORGO Unreviewed; 3312 AA.
AC G3RKM9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 3 {ECO:0000313|Ensembl:ENSGGOP00000016301.3};
GN Name=CELSR3 {ECO:0000313|Ensembl:ENSGGOP00000016301.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000016301.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000016301.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000016301.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000016301.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; CABD030021211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030021212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000016763.3; ENSGGOP00000016301.3; ENSGGOG00000016683.3.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000160077; -.
DR HOGENOM; CLU_000158_0_0_1; -.
DR OMA; ECETRWG; -.
DR TreeFam; TF323983; -.
DR Proteomes; UP000001519; Chromosome 3.
DR Bgee; ENSGGOG00000016683; Expressed in cerebellum and 3 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 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:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..3312
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014178594"
FT TRANSMEM 2537..2561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2573..2593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2599..2621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2642..2662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2682..2703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2724..2745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..433
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 434..545
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 546..651
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 652..756
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 757..858
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 859..961
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 962..1067
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1068..1169
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1375..1433
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1435..1471
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1475..1514
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1515..1719
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1722..1758
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1764..1944
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1946..1979
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1982..2020
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2077..2124
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2109..2191
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2538..2775
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 90..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2361..2398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2830..2850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2888..2927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2978..3006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3086..3312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2375..2390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2979..3000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3109..3123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3162..3177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3191..3206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3235..3302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1423..1432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1461..1470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1748..1757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2010..2019
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2077..2089
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2079..2096
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2098..2107
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3312 AA; 358239 MW; 890F34CBDA72C903 CRC64;
MMARRPPWRG LGGRSTPILL LLLLSLFPLS QEELGGGGHQ GWDPGLAATT GPRAHIGGGA
LALCPESSGV REDGGPGLGV REPIFVGLRG RRQSARNSRG PPEQPNEELG IEHGVQPSGS
RERETGQGPG SVLYWRSEVS SCGRTGPLQR GSLSPGALSS GVPGLGNSSP LPSDFLVRHH
GPKLVSSQRN AGTGSRKRVG TARCCGELWA TGSKGQGERA TTSGAERTAP RRNCLPGASG
SGPELDSAPR TARTAPASGS APRESRTAPE PAPKRMRSRG LFRRRFLPQR PGPRPPGLPA
RPEARKITSA NRARFRRAAN RHPQFPQYNY QTLVPENEAA GTAVLRVVAQ DPDAGEAGRL
VYSLAALMNS RSLELFSIDP QSGLIRTAAA LDRESMERHY LRVTAQDHGS PRLSATTMVA
VTVADRNDHS PVFEQAQYRE TLRENVEEGY PILQLRATDG DAPPNANLRY RFVGPPAARA
AAAAAFEIDP RSGLISTSGQ VDREHMESYE LVVEASDQGQ EPGPRSATVR VHITVLDEND
NAPQFSEKRY VAQVREDVRP HTVVLRVTAT DRDKDANGLV HYNIISGNSR GHFAIDSLTG
EIQVVAPLDF EAEREYALRI RAQDAGRPPL SNNTGLASIQ VVDINDHIPI FVSTPFQVSV
LENAPLGHSV IHIQAVDADH GENARLEYSL TGVAPDTPFV INSATGWVSV SGPLDRESVE
HYFFGVEARD HGSPPLSASA SVTVTVLDVN DNRPEFTMKE YHLRLNEDAA VGTSVVSVTA
VDRDANSAIS YQITGGNTRN RFAISTQGGV GLVTLALPLD YKQERYFKLV LTASDRALHD
HCYVHINITD ANTHRPVFQS AHYSVSVNED RPVGSTIVVI SASDDDVGEN ARITYLLEDN
LPQFRIDADS GAITLQAPLD YEDQVTYTLA ITARDNGIPQ KADTTYVEVM VNDVNDNAPQ
FVASHYTGLV SEDAPPFTSV LQISATDRDA HANGRVQYTF QNGEDGDGDF TIEPTSGIVR
TVRRLDREAV SVYELTAYAV DRGVPPLRTP VSFQVMVQDV NDNAPVFPAE EFEVRVKENS
IVGSVVAQIT AVDPDEGPNA HIMYQIVEGN IPELFQMDIF SGELTALIDL DYEARQEYVI
VVQATSAPLV SRATVHVRLV DQNDNSPVLN NFQILFNNYV SNRSDTFPSG IIGRIPAYDP
DVSDHLFYSF ERGNELQLLV VNQTSGELRL SRKLDNNRPL VASMLVTVTD GLHSVTAQCV
LRVVIITEEL LANSLTVRLE NMWQERFLSP LLGRFLEGVA AVLATPAEDV FIFNIQNDTD
VGGTVLNVSF SALAPRGAGA GAAGPWFSSE ELQEQLYVRR AALAARSLLD VLPFDDNVCL
REPCENYMKC VSVLRFDSSA PFLASASTLF RPIQPIAGLR CRCPPGFTGD FCETELDLCY
SNPCRNGGAC ARREGGYTCV CRPRFTGEDC ELDTEAGRCV PGVCRNGGTC TDAPNGGFRC
QCPAGGAFEG PRCEVAARSF PPSSFVMFRG LRQRFHLTLS LSFATVQQSG LLFYNGRLNE
KHDFLALELV AGQVRLTYST GESNTVVSPT VPGGLSDGQW HTVHLRYYNK PRTDALGGAQ
GPSKDKVAVL SVDDCDVAVA LQFGAEIGNY SCAAAGVQTS SKKSLDLTGP LLLGGVPNLP
ENFPVSHKDF IGCMRDLHID GRRVDMAAFV ANNGTMAGCQ AKLHFCDSGP CKNSGFCLER
WGGFSCDCPV GFGGKDCRLT MAHPHHFRGN GTLSWNFGSD MAVSVPWYLG LAFRTRATQG
VLMQVQAGPH STLLCQLDRG LLSVTVTRGS GRASHLLLDQ VTVSDGRWHD LRLELQEEPG
GRRGHHVLMV SLDFSLFQDT MAVGSELQGL KVKQLHVGGL PPGSAEEAPQ GLVGCIQGVW
LGSTPSGSPA LLPPSHRVNV EPGCVVTNAC ASGPCPPHAD CRDHWQTFSC TCRPGYYGPG
CVDACLLNPC QNQGSCRHLP GAPHGYTCDC VGGYFGHHCE HRMDQQCPRG WWGSPTCGPC
NCDVHKGFDP NCNKTNGQCH CKEFHYRPRG SDSCLPCDCY PVGSTSRSCA PHSGQCPCRP
GALGRQCNSC DSPFAEVTAS GCRVLYDACP KSLRSGVWWP QTKFGILATV PCPRGALGLT
RGCLPPGAAV RLCDEAQGWL EPDLFNCTSP AFRELSLLLD GLELNKTALD TMEAKKLAQR
LREVTGHTDH YFSQDVRVTA RLLAHLLAFE SHQQGFGLTA TQDAHFNEVG LCPMFSVPWP
PSSQPPAPGS PAQAPAVLLG SEGPGLSLCP CPLQPHPLAC WMLSIDRMEH PSSPRGARRY
PRYHSNLFRG QDAWDPHTHV LLPSQSPRPW ETPGPILPTS SSTENSTTSS VVPPPAPPEP
EPGISIIILL VYRTLGGLLP AQFQAERRGA RLPQNPVMNS PVVSVAVFHG RNFLRGILES
PISLEFRLLQ TANRSKAICV QWDPPGLAEQ HGVWTARDCE LVHRNGSHAR CRCSRTGTFG
VLMDASPRER LEGDLELLAV FTHVVVAVSV AALVLTAAVL LSLRSLKSNV RGIHANVAAA
LGVAELLFLL GIHRTHNQLV CTAVAILLHY FFLSTFAWLF VQGLHLYRMQ VEPRNVDRGA
MRFYHALGWG VPAVLLGLAV GLDPEGYGNP DFCWISVHEP LIWSFAGPVV LVIVMNGTMF
LLAARTSCST GQREAKKTSA LRTLRSSFLL LLLVSASWLF GLLAVNHSIL AFHYLHAGLC
GLQGLAVLLL FCVLNADARA AWTPACLGRK AAPEEARPAP GMGPGAYNNT ALFEESGLIR
ITLGASTVSS VSSTRSGRTQ DQDSQRGRSY LRDNVLVRHG SAADHTDHSL QAHAGPTDLD
VAMFHRDAGA DSDSDSDLSL EEERSLSIPS SESEDNGRTR GRFQRPLCRA AQSERLLTHP
KDVDGNDLLS YWPALGECEA APCALQTWGS ERRLGLDTSK DAANNNQPDP ALTSGDETSL
GRAQRQRKGI LKNRLQYPLV PQTRGAPELS WCRAATLGHR AVPAASYGRI YAGGGTGSLS
QPASRYSSRE QLDLLLRRQL SRERLEEAPA PVLRPLSRPG SQECMDAAPG RLEPRDRGST
LPRRQPPRDY PGAMAGRFGS RDALDLGAPR EWLSTLPPPR RTRDLDPQPP PLPLSPQRQL
SRDPLLPSRP LDSLSRSSNS REQLDQVPSR HPSREALGPP PQLLRAREDP VSGPSHGPST
EQLDILSSIL ASFNSSALSS VQSSSTPLGP HTTATPSATA SVLGPSTPRS ATSHSISELS
PDSEVPRSEG HS
//
