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Database: UniProt
Entry: A0A1S2ZPF6_ERIEU
LinkDB: A0A1S2ZPF6_ERIEU
Original site: A0A1S2ZPF6_ERIEU 
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
//
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