ID H3D3A2_TETNG Unreviewed; 2976 AA.
AC H3D3A2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Cadherin, EGF LAG seven-pass G-type receptor 3 {ECO:0000313|Ensembl:ENSTNIP00000014990.1};
GN Name=CELSR3 {ECO:0000313|Ensembl:ENSTNIP00000014990.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000014990.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000014990.1}
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 STRING; 99883.ENSTNIP00000014990; -.
DR Ensembl; ENSTNIT00000015192.1; ENSTNIP00000014990.1; ENSTNIG00000012029.1.
DR GeneTree; ENSGT00940000160077; -.
DR HOGENOM; CLU_000158_1_1_1; -.
DR InParanoid; H3D3A2; -.
DR OMA; ECETRWG; -.
DR TreeFam; TF323983; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
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:0048731; P:system development; IEA:UniProt.
DR CDD; cd11304; Cadherin_repeat; 9.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd00055; EGF_Lam; 1.
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; 4.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 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; IPR000203; GPS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00180; EGF_Lam; 2.
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; 2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 5.
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; 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 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 Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 2209..2232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2268..2290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2311..2330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2350..2374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2395..2413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2419..2442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..121
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 122..231
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 232..337
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 338..442
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 443..544
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 545..647
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 648..752
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 753..854
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1114..1150
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1154..1192
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1193..1397
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1400..1436
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1442..1619
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1621..1657
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1658..1695
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1752..1799
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1784..1856
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2207..2443
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 2554..2587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2729..2911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2928..2976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2731..2747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2787..2802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2846..2868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2936..2955
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2956..2976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1140..1149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1426..1435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1647..1656
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1685..1694
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1752..1764
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1754..1771
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1773..1782
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2976 AA; 327736 MW; CB4E1CF6F8E1BBC6 CRC64;
SRSRRAANRH PFFPQYNYQV QVAENQPPGT SVILMSASDP DPGDAGRVSY SMAPLMNSRS
SDYFHIHPET GLITTTQTLD REHMDLHYFR VTATDYGSSR LSGTTMVAIT VSDRNDHSPI
FEQTEYRETI RENVEEGYPI LQLRATDSDS PTNANIRYRF IGDMVAVARA AFEIDPRSGL
ITTRGVVDRE LNEHYTLQVE ASDQGKEPGP RSATVKVFIT VLDENDNVPQ FSEKRYVVAV
KENVRPHSEI LRVSATDRDK DSNAAVHYNI ISGNSRGQFS IDSVTGEIQV VAPLDYEAER
EYTLRVRAQD NGRPPLSNNT GIVSVQVTDV NDNPPIFVST PFQASVLESS PVGSSILHIQ
AIDTDSGDNA RLEYKLTGTS SDTPFIINSA TGWVTVRSTL DRESVEHYFF GVEARDYGTP
PLSATASVTI TVMDVNDNHP EFLQKEYYAR LNEDAAVGTS VVTVTAVDRD VNSAVTYQIT
GGNTRNRFAI STAGGAGLLS LALPLDYKQE RRYVLTVTAS DRTLHDTCQV HINITDANTH
RPVFQSAHYS VSVNEDSPPG SLVVMISATD DDVGENARIT YLLEDNIPQF RIDSATGAIT
LQAELDYEDQ MTYTLAITAK DNGIPQKSDT TYVEVNVNDV NDNAPQFLSP RYQGSVSEDA
PPFTSVLQIS ATDRDAHANG RVQYTFQNGE DGDGDFTIEP TSGILRTVRR LDRESVPFYE
LTAYAVDRGM PPRTPVHIQV TVLDVNDKAP VFPADDFEVL VKENSAVGSV VAQITATDPD
EGANAQIMYQ IVEGNIPEIF QMDIFSGELT SLIDLDYETR NEYVIVVQAT SAPLVSRATV
RIKLVDQNDN RPTLQDFQII FNNFVSNRSN SFPSGVIGRI PAHDPDVSDR LYYTIDRGNE
LHLLLLNHTS GEIRLSRKLD NNRPLVAPML ITVTDGIHSI SAQCVLRVLI ITEDMLGSSV
TVRLQNMSQE HFLSPLLGNF LEGVSAVLSV PVEDVFIFNI QPDLDAAPGR ILNVSFSAAL
PGGLFFPSEA LEEQLYLNRP RLTSLTQMEV LPFDDNVCLR EPCKNYMKCV SVLRFNSSAP
FISSPSILFR PIHPIAGLRC RCPVGFTGDY CETEINLCYS NPCLNGGVCA PREGGFTCIC
RENYTGDRCE FDHRQGGCVP GVCRNGGTCL ELSRGGFRCE CPEGAYEPPY CAVTARSFPP
KSFAMFRGLR QRFHLTISLT FATLENSGLL FYNGRFNEKH DFIALEIQEG QVVLKYSTGE
SSTQVTPFLP GGVSDGNWHS VHIHYYNKPK RSIGGEAQGP SDEKIAVVRV DDCDAALSLR
FSTQLGNYSC AAQGKQSSSK KSLDLTGPLF LGGVPNGADN FPFSSREFIG CLKDFHIDNK
QLDLAGFIAN NGTTAGCSAK TPFCNSNPCQ NGGTCRVGWE TFLCDCPLGY GGKDCSHVMP
HPHRFLGNSV QWWDLKNEVT ISTPWYLGLV FRTRSREGTL LQAQAGQYTS LLFQVVNSQL
VFSVTRGAAR PVRLRLDQVL VADGRWHDLQ LELRDVRSDR ETRYVATLRL DFGIYQGTVI
VGNEIHGLKV KHLHVGGVFG SGKVQNGIRG CIQGVRLGVR PDAPPLRPPT RTVNVEAGCN
VGNYCVSSPC PTHSRCADQW ERHTCVCDPG YYGKSCTDAC HLNPCENEAQ CHRKPSSSHG
YVCDCGDNHF GQYCQHRSDH QCPRGWWGSP TCGPCDCDTD KGFDPNCNKT SGHCHCKEFH
YHPRGSDTCL PCDCYPVGSF SRSCDAETGQ CQCRPGVIGR QCNACDNPFA EVTNSGCEVI
YDGCPKTITQ GIWWPRTKFL RAAVSCPKGS VGAAIRHCDV ERGWLEPELY NCTSPPFVEL
NAALDSLERN ETELSTIMEK KLAHQLRDVT EATARLYGND LHIAERLLSR LLNFETQQSG
FGLTATQDAY FNENLIRACS ALLGPGTSGL WRALIQSQNH IQGGGPAELT GLLRQYSQNL
AKNMKLTYLN PVALVAPNLV MNLDRVETQT HVRRRFPRYH TTIFRGQSPW DPYTHIIMPP
HHSQPPASIT VSTNQTVEYA SARRALPAPE QPITIVILLI YRSLGAALPP KYHTDRRGVR
LPRHPVMNSP VVSISVFNNE TFVSGHLDQP VLLEFKLLET ANRSKPLCVQ WNHSSQHDLG
GCWTVRDCMV VYRNTSHVRC QCQRLGTFGV LMDSSQREQL EGDLETLALV TYSTLCLSML
ALILTVLVLS CLRGLKSNTR SIHSNTAAAM FLSELVFLLG INQTEQQFLC TVVAILLHYF
FMSTFAWMFV EGLHIYRMQT EQRNINYGAM RFYAIGWGVP AIITGLAVGL DPEGYGNPDF
CWISIYDKLL WSFAGPIAIV ILMNGGIFMI VAKISCSPSQ KETKKLPVIG TIRDAFLLLL
VATSTWLCGL MAVNNSVLAF YYIFNVLCLL QGLCVMLVFT VFNTEFKEAW RVACLGKKTP
GEDPPRPPQN AAQNPYHNAS LLEQSGLHRI TLGTSTVSSV SSASIKTTLT PSLESGRDSP
RLTVLQIREN LLARQTLEQN LVHTGATDLD VAMFHRDPGE DSDSDSDLSM EEERSLSIPS
SESEDNVRLR GRIQRRFKRS NHGERLLTEP KDLDGNDLLS YWPALEEGEM NTMQKWGSER
PLGGDYSKDA ANNNQTDAAL TSGDENNLTQ PHKHRKGILK NRLGCPPALQ ALSSKGRAPS
ELNWYRTSTL GHRGVPAASY GRMYSATAAA GGGSGSLSQP ASRYSSREHL DSLTRRQLSR
DPLGRQTIGG SRDRLDSRGS RDNLDLLPRS GSRSQLNALG RRQASSREHL GGVLISSRSR
EQLDTNGGGA QAPPCREWLR SLPPRQPSLP DQPLSSCASP PPPISEEPQQ EQLPGSGQAR
GRLDSGPPCR YPAQAVPQAP GSNPLARQPS SEHLDILSSI LASFNSTVLT PPAVSGPGPN
GSPAALPPPP PPQSTTSHSI SEVSPDSEAN RSEGQS
//
