ID H3BCX4_LATCH Unreviewed; 2952 AA.
AC H3BCX4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 2 {ECO:0000313|Ensembl:ENSLACP00000019745.1};
GN Name=CELSR2 {ECO:0000313|Ensembl:ENSLACP00000019745.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000019745.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000019745.1}
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 EMBL; AFYH01013981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01013990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000019745; -.
DR Ensembl; ENSLACT00000019883.1; ENSLACP00000019745.1; ENSLACG00000017360.1.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000157493; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; H3BCX4; -.
DR OMA; FTLYIVE; -.
DR TreeFam; TF323983; -.
DR Proteomes; UP000008672; 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; cd15992; 7tmB2_CELSR2; 1.
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; 1.25.40.610; -; 1.
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; IPR013032; EGF-like_CS.
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; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026:SF32; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 2; 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; PF12661; hEGF; 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; 5.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 9.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 6.
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:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2952
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003580389"
FT TRANSMEM 2437..2459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2471..2489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2495..2517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2538..2558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2578..2599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2620..2642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2648..2671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..363
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 364..471
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 472..577
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 578..682
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 683..784
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 785..887
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 888..993
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 994..1095
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1118..1218
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1297..1355
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1357..1393
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1397..1435
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1436..1644
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1640..1676
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1680..1863
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1865..1901
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1902..1939
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1996..2043
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2028..2101
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2434..2672
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 239..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1575..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2774..2849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1345..1354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1383..1392
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1666..1675
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1891..1900
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1929..1938
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1996..2008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1998..2015
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2017..2026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2952 AA; 326663 MW; F0F704358495D2FE CRC64;
VLFFFGCLGL CSLLHAIAVH LGADAQPGTL IAEVGGNRTC TLDQVVAPSF AKRFLGSQPT
GGRVFVSQRL DCARLASNPF SLYLTQDCRP QLPGFASFLT ARLDVHVHGG NCFPKRRRRA
RLDLQVLSLL MGSKKRPAPC FGAGEPLFSL SDLLPESLSG CKLHCQPTRA SHLAFQKGGI
LALENLCLKR DALLELDLHC NRCVDGAGVH LRVGLGSLEE EEEEDHWVKL LKKAARSEKV
KSSRRKRNVN ASPQFQPPTY QVSVPENKPA GTAIILLKAV DPDEGEAGRL DYSMDALFDS
RSNSLFAIDP QSGAVITAEE LDRETKATHV FRVTAVDHGT PRRTAMATLT VTVTDTNDHD
PVFEQPEYKE SVRENLEIGY EVLTVRATDG DGPANNNILY RILNDDGVNA VFEIDPRSGV
VRTKGPVDRE TVEYYQLVVE ANDQGRDPGP HSSTATVYIT VEDDNDNSPQ FSEKRYIVQV
PEDVSPNTQI LQVMASDKDK ANNALVHYSI MSGNTRGQFY IDAQSGDIDV VSQLDYEMNK
EYTLRIRAQD GGRPPLSNIS GLVTVQVLDV NDNAPIFVST PFQSTVLENV PIGYSVIHIQ
AIDADYGENS RLEYKLLDTS PNFPFAINNN TGWIVVATEL DRETVDCYNF GVEAKDHGSP
SMTSSASVSI TVLDVNDNNP EFTEKMYYMR LNEDAAVGTS VLTVLAVDRD GNSVVTYQIS
NGNTRNRFSI TSQSGGGLIT LALPLDYKLE RQYILTITAS DGTRFDTAQV YVNVTDANTH
RPVFQSSHYT VTINEDKPVG TTVVIISATD EDTGENSRIT YFMEDSIPQF KIDPDTGAVT
TQMELDYEDQ VSYTLAITAK DNGIPQKSDT TYLEILVNDV NDNAPQFVRD DYQGSVYEDV
PTFTSVLQIS ATDRDSGLNG RVFYTFQGGD DGDGDFIIES TSGIVRTLRR LDRENVPVYN
LKAFAVDKGV QALKTPIDIQ VTVLDVNDNP PVFEKDEFDI FVEENSPIGL AVARITATDP
DEGTNAQIMY QIVEGNIPEV FQLDIFSGEL TALMDLDYET KSEYIIVVQA TSAPLVSRAT
IHIRLLDKND NVPILKNFKI IFNNYVTNKS SSFPTGVIGR IPAYDPDVSD TLIYSFEEGN
ELDLVILNQT TGELRLSRAL DNNRPLEATM RVSVSDGIHS VTAQCTLQVT IITDEMLTNS
ITLRLENMSQ EKFLSPLLSL FVEGVAAVLS ATKEDIVIFN IQNDTDVSAN ILNVSLSVLL
PGGAQNQFFS SEDLQEQIYL NRTLLTAIST QRVLPFDDNI CLREPCENYM KCVSVLKFDS
SAPFITSDTI LFRPIHPING LRCRCPAGFT GDYCETEIDL CYSNPCGNNG VCRSREGGYT
CECHEDFTGD HCEVNSRIGR CAPGVCRNGG TCVNLLVGGF KCDCPSGEYE KPYCEMTTRS
FPPQSFITFK GLRQRFHFTI SLTFATKEKN GLLLYNGRFN EKHDFIALEI VNEQIQLTFS
AGESTTTVSP FIPGGVSDGQ WHTVQLQYYN KPIIGKSGVP QGPSDQKVAV VTVDDCDTSV
ALRFGSEIGN YTCSAQGTQS GSKNKSPPSP PHWRGGGVSK LKMDSVLITR VFAPELWNSL
QLDIRLLTFP QFLTSGCSAK RNFCDSNTCK NGGTCANKWD TFSCECPLGF GGKNCEQVMA
SPQRFLDNSL VSWNNLATTI TLPWYIGLMF RTRQANGILL RAVASQSSAI TIQLREGHVL
LEVLPATGPI SALKLDQVKV NDGDWHHLQV EMRSNKGSQQ PRYLALMSFD YGLHQTLSTV
DIGNEMQGVK MRNLSVGGIA GSGGRVQQGF RGCIQGVRIG ETSASAIALN MNHAEKVNVE
RGCSIPDPCD SSPCPSNSYC NDDWDSFSCS CDPGYYGNGC MDVCSLNPCE HQSICARKPS
SSHGYTCSCS DNYFGQYCES KIDQPCPRGW WGHPMCGPCN CDVNRGFDPD CNKTTGECRC
KENHYRPSGS DTCFPCDCYP TGSLSRTCDL ETGQCQCKPG VIGRKCDRCD NPFAEVGPNG
CEVIYDSCPR AMDSDIWWPR TKFALPAAVP CPKGSIGTAI RHCDEHRGWL APNLFNCTSV
SFIELKAFVD KLIRNESLLD TSRSRKMAVL LRNATKHTGT YFGSDVRVAY HLTDKILEYE
NLQHGFNLAA TQDVHFTENL IKVGSTILDE SNKHHWDLIQ QVEGGTAHLL KRYEDYASVL
AQNMRKTYLS PFTIVTPNIV ISVDRLEKMN FAGAKLPRYE TFRGEKPQDL ETTVILPESV
FKPAENKCES LLEAHVSKIV NQITWHLLIN EFCFVITTVL WMTGCSLLRV PKRPVINTPV
VSVTVHDNDE PLQHTLDKPI IVQFRLFETE ERSKPICVFW NHSIPVSKVG GWSAKGCEVI
FRNETHISCQ CNHMTSFAVL MDISRRENGE ILPLKTITYA TMAVSLAGLF LTFLVFLVLR
SLRSNQHSIS KNMAVALFFS ELIFLLGINQ ADNPFLCTVI AILLHFFYMC TFAWMFLEGL
HIYRMLTEVR DINYGPMRFY YMIGWGVPAF ITGLAVGLDP EGYGNPDFCW LSIYDTLIWS
FAGPISLAVS MNVFLYILAA RASCVPRHQG FENKTVPSSG VRTAFVILLL VTTSWLVALL
AVNSDTIIFH YVFAGFNCVQ GPFIFFFRIV FNKEVRKGFK YAFSKKHIDD TVGAVKSTGA
SSYNCNNTYV DGRLYHPPFG DSTGSLHSTV RSGKSYHSYI PFVLREDSGL NNSSSQTHIA
LTDHNSTLFH EVKGLPDEHD TDSDSDLSLE DDQSGSYAST HSSDSEEDEE YAGAPCWENL
VSPNNEKLPV QSTPKDKMNH LEDKPKENGD GIYKENMLVS LPFPATQPQK GILKKKMLPT
ITEKNSINRI HNELCNHKPG TVSSQASSLS DVSRTGGIQR TKQTLQEQLN GVMPIAMSIK
TGTVDEDSSG SE
//
