ID E0V8A5_MICOH Unreviewed; 3310 AA.
AC E0V8A5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Cadherin, EGF LAG seven-pass G-type receptor 3 (Flamingo homolog) {ECO:0000313|EMBL:ADN07503.1};
GN Name=CELSR3 {ECO:0000313|EMBL:ADN07503.1};
OS Microtus ochrogaster (Prairie vole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Microtus.
OX NCBI_TaxID=79684 {ECO:0000313|EMBL:ADN07503.1};
RN [1] {ECO:0000313|EMBL:ADN07503.1}
RP NUCLEOTIDE SEQUENCE.
RA Benjamin B., Blakesley R.W., Bouffard G.G., Brooks S., Chodroff R., Chu G.,
RA Chub I., Coleman H., Fuksenko T., Gestole M., Gregory M., Guan X.,
RA Gupta J., Gurson N., Han J., Hansen N., Hargrove A., Hines-Harris K.,
RA Ho S.-L., Hu P., Hurle B., Idol J.R., Johnson T., Kwong P., Lee-Lin S.-Q.,
RA Legaspi R., Lovett S., Madden M., Maduro Q.L., Maduro V.B., Margulies E.H.,
RA Masiello C., Maskeri B., McDowell J., Montemayor C., Mullikin J.C.,
RA Myrick J., Palumbo A., Park M., Prasad A., Ramsahoye C., Reddix-Dugue N.,
RA Riebow N., Schandler K., Schmidt B., Schueler M.G., Sison C., Smith L.,
RA Stantripop S., Thomas J.W., Thomas P.J., Tsipouri V., Young A., Green E.D.;
RT "NISC Comparative Sequencing Initiative.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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; DP001222; ADN07503.1; -; Genomic_DNA.
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; 3.
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, ECO:0000313|EMBL:ADN07503.1};
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..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..3310
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003141573"
FT TRANSMEM 2533..2557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2569..2589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2595..2617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2638..2658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2678..2700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2721..2740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..428
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 429..540
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 541..646
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 647..751
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 752..853
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 854..956
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 957..1062
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1063..1164
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1370..1428
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1430..1464
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1468..1507
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1508..1712
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1715..1751
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1755..1937
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1939..1972
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1975..2013
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2070..2117
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2102..2175
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2534..2770
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 153..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2353..2396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2827..2847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2883..2921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2974..3003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3089..3310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2975..2996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3106..3121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3190..3204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3233..3300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1418..1427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1741..1750
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2003..2012
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2070..2082
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2072..2089
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2091..2100
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3310 AA; 359709 MW; 904BEC7EADE6F48D CRC64;
MARRPLWWGL RGPSTPILLL LLLSLFPFSR EELGGGGDQG WDPGVATATG PRAQTGSGAV
ALCPDSPGVW EDGESGLGVR EPVFMRLRVG RQSARNQRGT PEQPNAELVV QALGSREQEA
GRGPGYLLCW HPEISSCGRT GPLRRGSLPL EALSPGNPDL GNIPPHPSDL LAQPDGSRSV
SFQRNARRAF RKRAETSRCC GKLWAPGHKG QGERSAISLT ERGPLRRNCL PGSLGSDLGE
NSAPRAGRTV PTPDSAPREP RTAPEPAPER MRFRGPFRRR FLFLRPGPRP PGFQTGSEAK
QIPSKNQGRP RRAANRHPQF PQYNYQTLVP ENEAAGTSVL RVVAQDPDPG EAGRLVYSLA
ALMNSRSLEL FSIDPQSGLI RTAAALDRES MERHYLRVTA QDHGSPRLSA TTMVAVTVAD
RNDHAPVFEQ AQYRETLREN VEEGYPILQL RATDGDAPPN ANLRYRFVGS PAARKEAAAA
FEIDPRSGLI STSGRVDREH MESYELVVEA SDQGQEPGPR SATVRVHITV LDENDNAPQF
SEKRYVAQVR EDVRPHTVVL RVTATDQDKD ANGLVHYNII SGNSRGHFAI DSLTGEIQVV
APLDFEAERE YALRIRAQDA GRPPLSNNTG LASIQVVDIN DHTPIFVSTP FQVSVLENAP
LGHSVIHIQA VDADHGENSR LEYSLTGVAP DTPFVINSAT GWVSVSGPLD RESVEHYFFG
VEARDHGSPP LSASASVTVT VLDVNDNRPE FTMKEYHLRL NEDAAVGTSV VSVTAVDRDA
NSAISYQITG GNTRNRFAIS TQGGVGLVTL ALPLDYKQER YFKLVLTASD RALHDHCYVH
INITDANTHR PVFQSAHYSV SMNEDRPVGS TVVVISASDD DVGENARITY LLEDNLPQFR
IDADSGAITL QAPLDYEDQV TYTLAITARD NGIPQKADTT YVEVMVNDVN DNAPQFVASH
YTGLVSEDAP PFTSVLQISA TDRDAHANGR VQYTFQNGED GDGDFTIEPT SGIVRTVRRL
DREAVPVYEL TAYAVDRGVP PLRTPVSIQV TVQDVNDNAP VFPAEEFEVR VKENSIVGSV
VAQITAVDPD EGPNAHIMYQ IVEGNIPELF QMDIFSGELT ALIDLDYEAR QEYVIVVQAT
SAPLVSRATV HVRLVDQNDN SPVLNNFQIL FNNYVSNRSD TFPSGIIGRI PAYDPDVSDH
LFYSFERGNE LQLLVVNQTS GELRLSRKLD NNRPLVASML VTVTDGLHSV TAQCVLRVVI
ITEELLANSL TVRLENMWQE RFLSPLLGHF LEGVAAVLAT PTEDVFIFNI QNDTDVGGTV
LNVSFSALAP RGAGAGAAGP WFSSEELQEQ LYVRRAALAA RSLLDVLPFD DNVCLREPCE
NYMKCVSVLR FDSSAPFLAS ASTLFRPIQP IAGLRCRCPP GFTGDFCETE LDLCYSNPCR
NGGACARREG GYTCVCRPRF TDCELDTEAG RCVPGVCRNG GTCTNAPNGG FRCQCPAGGA
FEGPRCEVAA RSFPPSSFVM FRGLRQRFHL TLSLSFATVQ PSGLLFYNGR LNEKHDFLAL
ELVAGQVRLT YSTGESNTVV SPTVPGGLSD GQWHTVHLRY YNKPRTDALG GAQGPSKDKV
AVLSVDDCNV AVALQFGAEI GNYACAAAGV QTSSKKSLDL TGPLLLGGVP NLPENFPVSH
KDFIGCMRDL HIDGRRMDMA AFVANNGTMA GCQAKLHFCA SGPCKNSGFC SERWGGFSCD
CPVGFGGKDC RLTMAHPYRF HGNGTLSWDF GNDMTVSVPW YLGLAFRTRA TKGVLMQVQL
GPHSVLLCQL DQGLLSVTLS RASGHAAHLL LDHTTVSDGR WHDLRLELQE EPGGRRGHHI
FMISLDFNLF QDTMAVGGEL QGLKVKQLHV GGLPPSSKEE GPQGLVGCIQ GVWIGFTPFG
SSALPPPSHR VNVEPGCVVT NACASGPCPP HANCKDLWQT FTCTCWPGYY GPGCVDACLL
NPCQNQGSCR HLQGTPHGYI CDCPNGYFGQ HCEHRMDQQC PRGWWGSPTC GPCNCDVHKG
FDPNCNKTNG QCHCKEFYYR PRGSDSCLPC DCYPVGSTSR SCAPHSGQCP CRPGALGRQC
NSCDSPFAEV TASGCRVLYD ACPKSLRSGV WWPQTKFGVL ATVPCPRGAL GAAVRLCDED
QGWLEPDLFN CTSPAFRELS LLLDGLELNK TALDTMEAKK LAQRLREVTG QTDHYFSQDV
RVTARLLAYL LAFESHQQGF GLTATQDAHF NENLLWAGSA LLAPETGDLW AALGQRAPGG
SPGSAGLVRH LEEYAATLAR NMELTYLNPV GLVTPNIMLS IDRMEHPSSA QGARRYPRYH
SNLFRGQDAW DPHTHVLLPS QSPQPSPSEA LPTSSNTENT TASSVVSPTA PPEPEPEPGI
SIVILLVYRT LGGLLPAQFQ AERRGARLPQ NPVMNSPVVS VAVFHGRNFL SGVLVSPINL
EFRLLQTANR SKAICVQWDP PGPADQHGMW TARDCELVHR NGSHARCRCS RTGTFGVLMD
ASPRERLEGD LELLAVFTHV VVAVSVTALV LTAAVLLSLR SLKSNVRGIH ANVAAALGVA
ELLFLLGIHR THNQLLCTAV AILLHYFFLS TFAWLLVQGL HLYRMQVEPR NVDRGAMRFY
HALGWGVPAV LLGLAVGLDP EGYGNSDFCW ISIHEPLIWS FAGPIVLVIV MNGTMFLLAA
RTSCSTGQRE AKKTSVLTLR SSFLLLLLVS ASWLFGLLAV NHSVLAFHYL HAGLCGLQGL
AVLLLFCVLN ADARAAWTPA CLGKKAAPEE TRPAPGTGSG VYNNTALFEE SGLIRITLGA
STVSSVSSAR SGRAQDQDSQ RGRSYLRDNV LVRHGSTADH IEHSLQAHTG PTDLDVAMFH
RDAGADSDSD SDLSLEEERS LSIPSSESED NGRTRGRFQR PLCRAAQSER LLAHPKDMDG
NDLLSYWPAL GECEAAAPCA LQAWGSERRL GLDTNKDAAN NNQPDLALTS GDETSLGRAQ
RQRKGILKNR LQYPLVPKTR GTPELSWCRA ATLGHRAVPA ASYGRIYAGG GTGSLSQPAS
RYSSREQLDL LLRRQLSRER LEEVPVPAPV LRPLSRPGSQ EHLDVAPSRP EPRDRVSTLP
RRQPPRDYPG TMAGRFGSRD PLDLGAPREW LNTLPPPRRN RDLDPQHPPL PLTPQRQLSR
DPLLPSRPLD SLSRISNSRE QLDQVPSRHP SREALGPAPQ LLRAREDPGS GPSHGPSTEQ
LDILSSILAS FNSSALSSVR SSSTPSGPHT TATPSATASA PGPSTPRSAT SHSISELSPD
SEIPRSEGHS
//
