ID A0A1S2ZPF6_ERIEU Unreviewed; 3054 AA.
AC A0A1S2ZPF6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 1 {ECO:0000313|RefSeq:XP_007522530.1};
GN Name=CELSR1 {ECO:0000313|RefSeq:XP_007522530.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007522530.1};
RN [1] {ECO:0000313|RefSeq:XP_007522530.1}
RP IDENTIFICATION.
RG RefSeq;
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.
CC Adhesion G-protein coupled receptor (ADGR) subfamily.
CC {ECO:0000256|ARBA:ARBA00007343}.
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 RefSeq; XP_007522530.1; XM_007522468.2.
DR GeneID; 103112989; -.
DR CTD; 9620; -.
DR eggNOG; KOG4289; Eukaryota.
DR InParanoid; A0A1S2ZPF6; -.
DR OrthoDB; 4006628at2759; -.
DR Proteomes; UP000079721; Unplaced.
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:InterPro.
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; 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; 5.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026:SF36; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 1; 1.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 1.
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; 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; 2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 9.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 1.
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 ECO:0000313|RefSeq:XP_007522530.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..3054
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010193285"
FT TRANSMEM 2504..2527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2539..2557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2563..2585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2606..2626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2646..2666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2687..2709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2715..2738
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 269..376
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 377..482
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 483..588
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 589..721
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 722..823
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 824..926
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 927..1033
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1034..1135
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1158..1258
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1337..1395
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1397..1433
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1437..1475
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1476..1680
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1683..1719
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1723..1904
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1906..1942
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1943..1980
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2037..2084
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2069..2142
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2502..2739
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 227..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2326..2365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2811..3054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2826..2844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2846..2860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2861..2875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2906..2936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2976..2990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3033..3054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1385..1394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1423..1432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1709..1718
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1932..1941
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1970..1979
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2037..2049
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2039..2056
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2058..2067
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3054 AA; 331943 MW; DE1F93AE1B4E31D1 CRC64;
MAPPPPPVLP ALLLLAAAAA LPALGLRAAA WELRVPGGAR AFALGPGWTY ALDAARTPRA
LRELLDVSHE GLLAGRRRGP GGEPPDCARL GGRPLPLQVR LEARGAPTSL SLRIRARAHG
PACGPRSRRG RSPRAELRAR TVLTVPGAGA ALCFPGPGGG GSGGAGTLHS ALAALTTFPA
CSCPPLSRPR CPRRPVCLPP GGSARLHLLC ALRRAAGAVR VQLHLQAAAA TPSPSPSLSP
SPPSLLRAGA GTARRARRGA GGSTSPQFPL PSYQVSVPEN EPAGTAVIEL RAHDPDEGEA
GRLSYQMEAL FDERSNGYFL IDAATGAVST ARALDRETKD THVLKVSALD HGSPRRSGAT
YLTVTVSDTN DHGPVFEQSE YRERVRENLE VGYEVLTIRA TDGDAPSNAN MRYRLLEGAA
GVFEIDARSG VVRTRAVVDR EEAAAYQLLV EANDQGRNPG PLSATATVHI VVEDENDNYP
QFSEKRYVVQ VPEDVAVNTA VLRVQATDRD QGQNAAIHYS IVSGNLKGQF YLHSLSGSLD
VINPLDFEAI REYTLRIKAQ DGGRPPLINS SGLVSVQVLD VNDNAPIFVS SPFQAAVLEN
VPLGHSVLHI QAVDADSGEN SRLSYRLVDT ASASPGVGGT GPQDPSAAST SSSPGGTVAA
DFPFQIHNSS GWITVCAELD RETVEHYSFG VEAVDHGLPP MSSSASVSIT VLDVNDNDPV
FTQPVYELRL NEDAAVGSSV LTLRARDRDA NSVITYQLTG GNTRNRFALS SQSGGGLVTL
ALPLDYKQER QYVLAVTASD GTRSHTVQVF VNVTDANTHR PVFQSSHYTV SVSEDRPVGT
SIATISASDE DTGENARITY VLEDPVPQFR IDPDTGTVYT VTELDYEDQA AYTLAITAQD
NGIPQKSDTT SLEILILDAN DNAPRFLRDL YQGSVLEDAP PSTSVLQVSA SDRDSGPNGR
LLYTFQGGDD GDGDFYIEPT SGVIRTQRRL DRENVAVYNL RALAVDRGSP TPLSASVDIQ
VTVLDINDNP PVFERDELEL YVEENSPVGS VVARIHANDP DEGPNAQIMY QIVEGNVPEV
FQLDLLSGDL RALVELDFEV RREYVLVVQA TSAPLVSRAT VHIRLLDQND NPPVLPDFQI
LFNNYVTNKS NSFPTGVIGR IPAHDPDLSD SLNYTFLQGN ELQLLLLDPA TGELQLSRDL
DNNRPLEALM EVSVSDGIHS VAALCTLRVT IITDDMLTNS ITVRLENMSQ EKFLSPLLSL
FMEGVATVLS TTKDDVFVFN IQNDTDVSAN ILNVTFSALL PGGVRDKFFP SEDLQEQIYL
NRTLLTAVST QRVLPFDDNI CLREPCENYM KCVSVLKFDS SAPFISSTTV LFRPIHPING
LRCRCPPGFT GDYCETEIDL CYSSPCGANG RCRSREGGYS CECLEDFTGE HCEVSVRSGR
CAHGVCKNGG TCVNLLIGGF RCVCPPGAYE RPYCEVTTRS FPPQSFVTFR GLRQRFHFTV
SLAFATQERN ALLLYNGRFN EKHDFIALEI VDEQVQLTFS AGETKTTVAP QVPGGVSDGR
WHSVQVQYYN KPNIGHLGLP HGPSGEKVAV VTVDACDTTV SVRFGSFVGN YSCAAQGTQS
GSKKSLDLTG PLLLGGVPNL PEDFPVRNRQ FVGCMRNLSV DGKNVDMASF IANNGTRAGC
AAQRNFCEGA GCQNGGTCVS RWNTYLCECP LRYGGKNCEQ VMPHPQRFTG ESVVSWSDLD
ITISVPWYLG LMFRTRKEDG VLLEATAGVS SRLHLQILNS YVHFEVSHGP SDVASMKLPR
SRVTDGEWHH LLIELKSAKE GKDIKYLAVM TLDYGLDQDT VQIGNQLPGL KMRSIVVGGV
SEDKVSVQRG FRGCMQGVRM GETSTNIATL NMKDALKVRV KDGCDVEDLC ASNPCPLHSR
CHNTWDSFSC ICDKGYFGRK CVDVCHLNPC EHVAACVHST SAPWGYVCEC GASHYGQYCE
NRIDLPCPKG WWGNPVCGPC HCAVGKGFDP DCNKTNGQCQ CKENHYKPPE QDSCLPCDCF
PHGSHSRACV TDTGQCACKP GVIGRQCNRC DNPFAEVTTL GCEVIYNGCP RAFEAGIWWP
QTKFGQPAAV PCPKGSVGNA IRHCSGEKGW LPPELFNCTT GSFVELKVLN EKLNRNETRM
DSDRTLRLAK ALHNATQHTP TLFGNDVRTA YQLLARILQH ESRQQGFELA ATRDADFHED
VVQVGSSLLA PGTRAAWELI HRSEGGAGQL LQHFEAYFSN VARNVRRTYV KPFIIVTTNM
ILAVDVFNKF NFTGARVPRF QDVREEYPKE LESSVIFPAD FFKPAERKEG PTMRPAGRKA
ALQTTRPGPS TEGEAPSRRR KRHPDEPGQF AVALVIIYRT LGQLLPEHYD PDRRSLRLPN
RPVINTPVVT TVVYSEGTPL PTPLERPVLV EYTLLETEER TKPVCVFWNH SINTGDSGGW
SAKGCELLSR NRTHVACQCS HASSSAVLMD ISRREHGEVL PLKIITYAAV ALSLAALLVA
FVLLTLVRTL HSNLHNIHKN LIVALFFSQL VFVVGIAQTE NPFLCTVIAI LLHYVYMSTF
AWTFVESLHV YRMLTEVRNI DVGPMRFYYV VGWGIPAVIT GLAVGLDPQG YGNPDFCWLS
LQDTLIWSFA GPVGTVIVVN TVIFVLSAKV SCQRKHHYYE RKGIVTLLRT AFLLLLLSSA
TWLLGLLAVN SDALAFHYLF AIFTCLQGLF VLLFHCVLNR EVRKHLKGVL AGKKPYPDDS
ATTRATLLTR SLNCNNTYIE EPNMFRTALG ESTASLDSTV RNEGGQKLSV ASGLARGGHG
EPDASFIPRS TKKPHDHDSD SDSELSLDEQ SSSYASSHSS DSEEDGVEAE DKWDPALGPV
HSTPKVDTVL NHISAGWPDE SLAGSDSEEP GEKPRLKVET KVSVELHQDG QGNHCREHPP
EPGGSGGGGA PTKLPEQRKG ILKNKVTYPP PLVDKTLKSR LREKLAECEH SPASSRSSSL
GSGDGVRAPD GAITVKTPRR EPGCEYHNGM AMNVRTGSAQ ANGSDSEGSN ETSI
//