ID F7HVM7_CALJA Unreviewed; 3311 AA.
AC F7HVM7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 3 {ECO:0000313|Ensembl:ENSCJAP00000005829.5};
GN Name=CELSR3 {ECO:0000313|Ensembl:ENSCJAP00000005829.5};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000005829.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000005829.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000005829.5}
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 STRING; 9483.ENSCJAP00000005829; -.
DR Ensembl; ENSCJAT00000006137.5; ENSCJAP00000005829.5; ENSCJAG00000003177.5.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000160077; -.
DR TreeFam; TF323983; -.
DR Proteomes; UP000008225; Chromosome 15.
DR Bgee; ENSCJAG00000003177; Expressed in cerebellum and 2 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:UP000008225};
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..3311
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035265072"
FT TRANSMEM 2538..2562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2574..2594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2600..2622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2643..2663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2683..2705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2726..2745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2751..2773
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..2182
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2539..2774
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 89..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2362..2399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2887..2941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2977..2999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3085..3219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3254..3311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2366..2393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2914..2941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2978..2992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3107..3122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3162..3176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3190..3205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3254..3301
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 3311 AA; 358092 MW; 380D57EF1510FE15 CRC64;
MMARRPPCWG LGERLTPIFL LLLLSLFPLS QEELGGGGHQ GWDPGLAATT GPGAQIRGGA
LALCPESPGV REDGGPGVGV REPVFVGLRG RRQNTRNSRG SPEQPNEELG IEHGIQQLGS
RKRETGQGPG SMVYWRPEVS SCGRTGSLQR GNLSPGALSS GVPCSGNSSP LPSDFLVRHH
GPKPVSSQRN SGTGARKRVS TARCCGESWV TGSKGQDERA MTSGGERTAP RRNCLPGASG
SGPELDSAPR TARTAPTSGS ALHESRTAPE PAPERMRSRG LFRRRFLQQR PGPRPPGLLA
GPEAGKITSA NPARFRRAAN RHPQFPQYNY QALVPENEAA GTAVLRVVAQ DPDAGEAGRL
VYSLAALMNS RSLELFSIDP QSGLIRTAAA LDRESMERHY LRVTAQDHGS PRLSATTMVA
VTVADRNDHS PVFEQAQYRE TLRENVEEGY PILQLRATDG DAPPNANLRY RFVGPPAARA
AAAAAFEIDP RSGLISTSGR VDREHMESYE LVVEASDQGQ EPGPRSATVR VHITVLDEND
NAPQFSEKRY VAQVREDVRP HTVVLRVTAT DRDKDANGLV HYNIISGNSR GHFAIDSLTG
EIQVVAPLDF EAEREYALRI RAQDAGRPPL SNNTGLASIQ VMDINDHIPI FVSTPFQVSV
LENAPLGHSV IHIQAVDADH GENARLEYSL TGVAPDTPFV INSATGWVSV SGPLDRESVE
HYFFGVEARD HGSPPLSASA SVTVTVLDVN DNRPEFTMKE YHLRLNEDAA VGTSVVSVTA
VDRDANSAIS YQITGGNTRN RFAISTQGGV GLVTLALPLD YKQERYFKLV LTASDRALHD
HCYVHINITD ANTHRPVFQS AHYSVSVNED RSVGSTIVVI SASDDDVGEN ARITYLLEDN
LPQFRIDADS GAITLQAPLD YEDQVTYTLA ITARDNGIPQ KADTTYVEVM VNDVNDNAPQ
FVASHYTGLV SEDAPPFTSV LQISATDRDA HANGRVQYTF QNGEDGDGDF TIEPTSGIVR
TVRRLDREAV PVYELTAYAV DRGVPPLRTP VSIQVTVQDV NDNAPVFPAE EFEVRVKENS
IVGSVVAQIT AVDPDEGPNA HIMYQIVEGN IPELFQMDIF SGELTALIDL DYEARQEYVI
VVQATSAPLV SRATVHVRLV DQNDNSPVLN NFQILFNNYV SNHSDTFPSG IIGRIPAYDP
DVSDHLFYSF ERGNELQLLV VNQTSGELRL SRKLDNNRPL VASMLVTVTD GLHSVTAQCV
LRVVIITEEL LANSLTVRLE NMWQERFLSP LLGHFLEGVA 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 PRTDALGGVQ
GPSKDKVAVL SVDDCDVAVA LQFGAEIGNY SCAAAGVQTS SKKSLDLTGP LLLGGVPNLP
ENFPVSHKDF IGCMRDLHID GRRMDMAAFV ANNGTMAGCQ AKLHFCDSGP CKNSGFCSER
WGGFSCDCPV GFGGKDCRLT MAHPHHFRGN GTLSWNFGSD MAVSVPWYLG LAFRTRATQG
VLMQVQAGPH STLLCQLDRG LLSVTVTRGA GRASHLLLDQ VTVSDGRWHD LRLELQEEPG
GRRGHHVLMV SLDFSLFQDT MAVGSELQGL KVKQLHVGGL PPGSAEEAPQ GLVGCIQGVW
LGSTPSGSPA LLPPSHGVNV EPGCVVTNAC ASGPCPPHAD CLDLWQTFSC TCRPGYYGAG
CVDACLLNPC QNQGSCRHLP GDPHGYTCDC VGGYFGHHCE YRMDQQCPRG WWGSPTCGPC
NCDVHKGFDP NCNKTNGQCH CKEFHYRPRG SDSCLPCDCY PVGSTSRSCA PHSGQCPCRP
GALGRQCNSC DSPFAEVTAS GCRVLYDACP KSLRSGVWWP QTKFGVLATV PCPRGALGAA
VRLCDEAQGW LEPDLFNCTS PAFRELSLLL DGLELNKTAL DTVEAKKLAQ RLREVTGHTD
HYFSQDVRVT ARLLAHLLAF ESHQQGFGLT ATQDAHFNEN LLWAGSALLA PETGDLWAAL
GQRAPGGSPG SAGLVRHLEE YAATLARNME LTYLNPMGLV TPNIMLSIDR MEHPSSPRGA
RRYPRYHSNL FRGQDAWDPH THVLLPSQSP WPSPSEVLPT SSSTENSTTS SVIPPPAPAE
PEPGISIVIL LVYRTLGGLL PAQFQAERRG ARLPQNPVMN SPVVSVAVFH GRNFLRGVLE
SPISLEFRLL QTANRSKAIC VQWDPPGLAE QHGVWTARDC ELVHRNGSHA RCRCSRTGTF
GVLMDASPRE RLEGDLELLA VFTHVVVAVS VAALVLTAAI LLSLRSLKSN VRGIHANVAA
ALGVAELLFL LGIHRTHNQL VCTAVAILLH YFFLSTFAWL LVQGLHLYRM QVEPRNVDRG
AMRFYHALGW GVPAVLLGLA VGLDPEGYGN PDFCWVSVHE PLIWSFAGPV VLVIVMNGTM
FLLAARTSCS TGQREAKKAS ALTLRSSFLL LLLVSASWLF GLLAVNHSIL AFYLHAGLCG
LQGLAVLLLF CVLNADARAA WTPACLGRKA APEEARPAPG TGPGAYNNTA LFEESGLIRI
TLGASTVSSV SSARSGRTQD QDSQRGRSYL RDNVLVRHGS AADHTDHSLQ AHAGPTDLDV
AMFHQDAGAD SDSDSDLSLE EERSLSIPSS ESEDNGRTRG RFQRPLHRAA QSERLLTHPK
DVDGNDLLSY WPALGECEAA PCALQTWGSE RRLGLDTSKD AANNNQPDPA LTSGDEISLG
RAQRQRKGIL KNRLQYPLVP QTRGAPELSW CRAATLGHRA VPAASYGRIY AGGGTGSLSQ
PASRYSSREQ LDLLLRRQMS RERLEEAPAP VLRPLTRPGS QERMDTALGR LEPRDRGSTL
PRRQPPRDYP GTMAGRFGSR DVLDLGAPRE WLSTLPPPRR TRDLDLQPPP LPLSPQRQLS
RDPLLPSQPL DPLSKSSNSG DRLDQVPSRH PSREALGPPP QLLRAREDLA SGPSHGLSTE
QLDILSSILA SFNSSALSSM QSSSTPSGPQ TTATPSATAS VLGPSTPRSA TSHSISELSP
DSEVPRSEGH S
//
