ID A0A452RTP9_URSAM Unreviewed; 3309 AA.
AC A0A452RTP9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 3 {ECO:0000313|Ensembl:ENSUAMP00000022782.1};
GN Name=CELSR3 {ECO:0000313|Ensembl:ENSUAMP00000022782.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000022782.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000022782.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; 9643.ENSUAMP00000022782; -.
DR Ensembl; ENSUAMT00000025456.1; ENSUAMP00000022782.1; ENSUAMG00000017886.1.
DR GeneTree; ENSGT00940000160077; -.
DR OMA; ECETRWG; -.
DR Proteomes; UP000291022; 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: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; 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; 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; 3.
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; 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:UP000291022};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..3309
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019090918"
FT TRANSMEM 2543..2567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2579..2599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2605..2627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2648..2668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2688..2709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2730..2749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..434
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 435..546
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 547..652
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 653..757
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 758..859
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 860..962
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 963..1068
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1069..1170
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1376..1434
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1436..1472
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1476..1515
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1516..1720
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1723..1759
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1765..1945
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1984..2022
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2079..2126
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2111..2184
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2544..2779
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 69..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2362..2406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2887..2946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2982..3004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3092..3139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3159..3245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3258..3309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2376..2394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2919..2946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2983..3004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3112..3127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3166..3181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1424..1433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1462..1471
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1749..1758
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2012..2021
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2079..2091
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2081..2098
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2100..2109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3309 AA; 358562 MW; 52424049490DE75B CRC64;
MVKTASVIRV GMGPTTPLLL LLLLLSLFPL SREELGVDGG QGWDPEVAAA TGPGARTGGG
ALALCPETPG VQEDGEPGLG VREPVFVGPR EGRQSAQRGR GPPEQPDAGL GAKYGVQALN
SRGRETGQGP GSLLCWRAEV SSCRQSGPLR RDSLSPEALS PGVPSLETNS PFPSDLLVRP
RGYKLVSSQR NAGRGTPKKV GTMRCCGGLW APKRRGQGER TATSRAERTA SHPDCTPRAA
GSGSGLDSAP RTERTAPAPG SAPRESRTAP EPTPERMRSR SLFRRRFLPQ RPGPRPPGFP
AQPRVWRISP ASRVRRRRAA NRHPQFPQYN YQALVPENEA AGTAVLRVAA QDPDAGEAGR
LVYSLAALMN SRSLELFSID PLSGLIRTEA ALDRESMERH YLRVTAQDHG SPRLSATTMV
AVTVADRNDH SPVFEQAQYR ETLRENVEEG YPILQLRATD GDAPPNANLR YRFVGPPAAR
AAASAAFEID PRSGLISTSG RVDREHMESY ELVVEASDQG QEPGPRSATV RVHITVLDEN
DNAPQFSEKR YVAQVREDVR PHTVVLRVTA TDRDKDANGL VHYNIISGNS RGHFAIDSLT
GEIQVVAPLD FEAEREYALR IRAQDAGRPP LSNNTGLASI QVVDINDHTP IFVSTPFQVS
VLENAPLGHS VIHIQAVDAD HGENARLEYS LTGVAPDMPF VINSATGWVS VSGPLDRESV
EHYFFGVEAR DHGIPPLSAS ASVTVTVLDV NDNRPEFTMK EYHLRLNEDA AVGTTVVSVT
AVDRDANSAI SYQITGGNTR NRFAISTQGG VGLVTLALPL DYKQERYFKL VLTASDRALH
DHCYVHINIT DANTHRPVFQ SAHYSVSVNE DRPVGSTVVV ISASDDDVGE NARITYLLED
NLPQFRIDAD SGAITLQAPL DYEDQVTYTL AITARDNGIP QKADTTYVEV MVNDVNDNAP
QFVASHYTGL VSEDAPPFTS VLQISATDRD AHANGRVQYT FQNGEDGDGD FTIEPTSGIV
RTVRRLDREA VPVYELTAYA VDRGVPPLRT PVSIQVTVQD VNDNAPVFPA EEFEVRVKEN
SIVGSVVAQI TAVDPDEGPN AHIMYQIVEG NIPELFQMDI FSGELTALID LDYEARQEYV
IVVQATSAPL VSRATVHVRL VDQNDNSPVL NNFQILFNNY VSNRSDTFPS GVIGRIPAYD
PDVSDHLSYS FERGNELQLL VVNQTSGELR LSRKLDNNRP LVASMLVTVT DGLHSVTAQC
VLRVVIITEE LLANSLTVRL ENMWQERFLS PLLGHFLEGV AAVLATPAED VFIFNIQNDT
DVGGTVLNVS FSALAPRGAG AGAAGPWFSS EELQEQLYVR RAALAARSLL EVLPFDDNVC
LREPCENYMK CVSVLRFDSS APFLASASTL FRPIQPIAGL RCRCPPGFTG DFCETELDLC
YSNPCRNGGA CARREGGYTC VCRPRFTGED CELDTEAGRC VPGVCRNGGT CADGPDGGFR
CQCPAGGAFE GPRCEVAARS FPPSSFVMFR GLRQRFHLTL SLSFATVQPS GLLFYNGRLN
EKHDFLALEL VAGQVRLTYS TGESNTVVSP TVPGGLSDGQ WHTVHLRYYN KPRTDALGGA
QGPSKDKVAV LSVDDCDVAV ALQFGAEIGN YSCAAAGVQT SSKKSLDLTG PLLLGGVPNL
PENFPVSHKE FVGCMRDLYI DGRRVDMAAF VANNGTMAGC QAKLHFCDSG PCKNSGFCSE
RWGGFSCDCP VGFGGKDCRL TMAYPHHFRG NGTLSWDFGN DMAVSVPWYL GLAFRTRATQ
GVLMQLQAGP HSTLLCQLDR GLLSVTVTRG TGRAAHLLLD QVTVSDGRWH DLRLELQEEP
GGRRGHHVLM VSLDFSLFQD TMAVGSELQG LKVKRLHVGG LPPSSEEEVP QGLVGCIQGV
WLGSTPLGSP ALLPPSHRVN VEPGCVVTNA CASGPCPPHA DCRDLWQTFS CTCWPGAYFL
PWCVDACLLN PCQNQGSCRH LPGAPHGYTC DCVGGYFGHH CEHRMDQQCP RGWWGSPSCG
PCNCDVHKGF DPNCNKTNGQ CHCKEFHYRP RGSDSCLPCD CYPVGSTSRS CAPHSGQCPC
RPGALGRQCN SCDSPFAEVT ASGCRVLYDA CPKSLRSGVW WPQTKFGMLA SVPCPRGALG
AAMRLCDEDQ GWLEPDLFNC TSPAFRELNL LLDGLELNKT ALDTVEAKKL AQRLREVTGH
TDHYFSQDVR VTARLLAHLL AFESHQQGFG LTATQDAHFN ENLLWAGSAL LAPETGDLWA
ALGQRAPGGS PGSAGLVQHL EEYAATLARN MELTYLNPVG LVTPNIMLSI DRMEHPSPTR
GTRRYPRYHS NLFRGQDAWD PHTHVLLPSQ SPRPSPPEVL STSSSGMENS TTSSAAPPPA
PPEPEPEPGI SIVILLVYRT LGGLLPAQFQ AERRGARLPQ NPVMNSPVVS VAVFHRRNFL
RGVLESPISL EFRLLQTANR SKAICVQWDP PGPADQHGMW TARDCELVHR NGSHARCRCS
RTGTFGVLMD ASPRERLEGD LELLAVFTHV VMAVSVAALL LTAAVLLSLR SLKSNMRGIH
ANVAAALGVA ELLFLLGIHR THNQLVCTVV AILLHYFFLS TFAWLLVQGL HLYRIQVEPR
NVDRGAMRFY HALGWGVPAV LLGLAVGLDP EGYGNPDFCW ISIHEPLIWS FAGPVVLVVM
NGTMLLLAAR TSCSTGQREA KKTSALSLRS CFLLLLLVSA SWLFGLLAVN HSVLAFHYLH
AALCGLQGLA VLLLFCVVNA DARAAWTPAC LGRKAAPEEA RPAPGTGHGA YNNTALFEES
GLIRITLGAS TVSSVSSARS GRTQDQDSQR GRGYLRDNVL VRHGSAADHT DHSLQAHTGP
TDLDVAMFHR DAGGDSDSDS DLSLEEERSL SIPSSESEDN GRTRGRFQRP LRRAAQSERL
LTHPKDVDGN DLLSYWPALG ECEATPCALQ TWGSERRLGL DTSKDAANNN QPDLALTSGD
ETSLGRAQHQ RKGILKNRLQ YPLVPQSRGA PELSWCRAAT LGHRAVPAAS YGRIYAGGAT
GSLSQPASRY SSREQLDLLL RRQLSRERLE EAPAPILRPL SRPGSQERLD AAPGRLEPRD
RGSTLPRRQP PRDYPGARAC RFGSRDALDL GAPCEWLSTL PPPHSARDLD PQPPPLPLSP
QQQLSRDPLL PSRPLDSLSR RSNSGEQLDH VPSRHPSREG LGPPPQLLRV REDPASGPSH
GPSTEQLDIL SSILASFNSS ALSSSVQSSS TPSGPHTTAT PSATASALGP STPRSATSHS
ISELSPDSE
//
