ID A0A2I2YQV9_GORGO Unreviewed; 3277 AA.
AC A0A2I2YQV9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 3 {ECO:0000313|Ensembl:ENSGGOP00000037115.1};
GN Name=CELSR3 {ECO:0000313|Ensembl:ENSGGOP00000037115.1};
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:ENSGGOP00000037115.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000037115.1, 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:ENSGGOP00000037115.1, 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:ENSGGOP00000037115.1}
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; ENSGGOT00000046583.1; ENSGGOP00000037115.1; ENSGGOG00000016683.3.
DR GeneTree; ENSGT00940000160077; -.
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; 4.
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; 6.
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; 2.
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; 5.
DR SMART; SM00179; EGF_CA; 4.
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; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 5.
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..3277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014179774"
FT TRANSMEM 2515..2539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2551..2571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2577..2599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2620..2640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2660..2680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2692..2710
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..1734
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1753..1933
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1935..1968
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1971..2009
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2066..2113
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2098..2171
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2516..2740
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 2337..2376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2795..2815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2853..2892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2943..2971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3051..3277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2343..2368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2944..2965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3074..3088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3127..3142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3156..3171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3200..3267
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 1999..2008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2066..2078
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2068..2085
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2087..2096
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3277 AA; 354395 MW; C987D317BD050401 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 ANNGTMAGRP EASTSLAHGS GQICSWGRGC
NPVSLIHSAM AHPHHFRGNG TLSWNFGSDM AVSVPWYLGL AFRTRATQGV LMQVQAGPHS
TLLCQLDRGL LSVTVTRGSG RASHLLLDQV TVSDGRWHDL RLELQEEPGG RRGHHVLMVS
LDFSLFQDTM AVGSELQGLK VKQLHVGGLP PGSAEEAPQG LVGCIQGVWL GSTPSGSPAL
LPPSHRVNVE PGCVVTNACA SGPCPPHADC RDHWQTFSCT CRPGYYGPGC VDACLLNPCQ
NQGSCRHLPG APHGYTCDCV GGYFGHHCEH RMDQQCPRGW WGSPTCGPCN CDVHKGFDPN
CNKTNGQCHC KEFHYRPRGS DSCLPCDCYP VGSTSRSCAP HSGQCPCRPG ALGRQCNSCD
SPFAEVTASG CRVLYDACPK SLRSGVWWPQ TKFGILATVP CPRGALGAAV RLCDEAQGWL
EPDLFNCTSP AFRELSLLLD GLELNKTALD TMEAKKLAQR LREVTGHTDH YFSQDVRVTA
RLLAHLLAFE SHQQGFGLTA TQDAHFNEVG LCPMFSVPWP PSSQPPAPGS PAQAPAVLLG
SEGPGLSLCP CPLQPHPLAC WMLSIDRMEH PSSPRGARRY PRYHSNLFRG QDAWDPHTHV
LLPSQSPRPS PSEVLPTSSS TENSTTSSVV PPPAPPEPEP GISIIILLVY RTLGGLLPAQ
FQAERRGARL PQNPVMNSPV VSVAVFHGRN FLRGILESPI SLEFRLLQTA NRSKAICVQW
DPPGLAEQHG VWTARDCELV HRNGSHARCR CSRTGTFGVL MDASPRERLE GDLELLAVFT
HVVVAVSVAA LVLTAAVLLS LRSLKSNVRG IHANVAAALG VAELLFLLGI HRTHNQLVCT
AVAILLHYFF LSTFAWLFVQ GLHLYRMQVE PRNVDRGAMR FYHALGWGVP AVLLGLAVGL
DPEGYGNPDF CWISVHEPLI WSFAGPVVLV IVVSALDLWT QLRAVSRTLR SSFLLLLLVS
ASWLFGLLAV NHSILAFHYL HAGLCGLQGL AVLLLFCVLN ADARAAWTPA CLGRKAAPEE
ARPAPGMGPG AYNNTALFEE SGLIRITLGA STVSSVSSTR SGRTQDQDSQ RGRSYLRDNV
LVRHGSAADH TDHSLQAHAG PTDLDVAMFH RDAGADSDSD SDLSLEEERS LSIPSSESED
NGRTRGRFQR PLCRAAQSER LLTHPKDVDG NDLLSYWPAL GECEAAPCAL QTWGSERRLG
LDTSKDAANN NQPDPALTSG DETSLGRAQR QRKGILKNRL QYPLVPQTRG APELSWCRAA
TLGHRAVPAA SYGRIYAGGG TGSLSQPASR YSSREQLDLL LRRQLSRERL EEAPAPVLRP
LSRPGSQECM DAAPGRLEPR DRGSTLPRRQ PPRDYPGAMA GRFGSRDALD LGAPREWLST
LPPPRRTRDL DPQPPPLPLS PQRQLSRDPL LPSRPLDSLS RSSNSREQLD QVPSRHPSRE
ALGPPPQLLR AREDPVSGPS HGPSTEQLDI LSSILASFNS SALSSVQSSS TPLGPHTTAT
PSATASVLGP STPRSATSHS ISELSPDSEV PRSEGHS
//
