ID G1KGY4_ANOCA Unreviewed; 3155 AA.
AC G1KGY4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 1 {ECO:0008006|Google:ProtNLM};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000007545.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000007545.4, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000007545.4,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000007545.4}
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.
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 STRING; 28377.ENSACAP00000007545; -.
DR Ensembl; ENSACAT00000007706.4; ENSACAP00000007545.4; ENSACAG00000007375.4.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000159839; -.
DR HOGENOM; CLU_000158_1_0_1; -.
DR InParanoid; G1KGY4; -.
DR TreeFam; TF323983; -.
DR Proteomes; UP000001646; Chromosome 5.
DR Bgee; ENSACAG00000007375; Expressed in embryonic post-anal tail and 11 other cell types or tissues.
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:0098609; P:cell-cell adhesion; IBA:GO_Central.
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; 6.
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; 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; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000001646};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..3155
FT /note="Cadherin EGF LAG seven-pass G-type receptor 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032325370"
FT TRANSMEM 2598..2621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2633..2651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2657..2679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2700..2720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2740..2761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2781..2803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2809..2832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 381..489
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 490..597
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 598..703
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 704..819
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 820..921
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 922..1024
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1025..1130
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1131..1232
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1255..1355
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1434..1492
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1494..1530
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1534..1572
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1573..1777
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1780..1816
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1820..2001
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2003..2039
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2040..2077
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2134..2181
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2166..2239
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2596..2833
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 354..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2899..3083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2899..2914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2916..2941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2955..2971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3010..3024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3050..3064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1482..1491
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1520..1529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1806..1815
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2029..2038
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2067..2076
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2134..2146
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2136..2153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2155..2164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3155 AA; 350459 MW; 6E47E4A857E58342 CRC64;
MALAALPLLL LLPWLAAGEW ELRLGRCPEG GALLLDLSLG PEWRCDVDEA RTSPPLRGAL
ELGRGGRLRV AKGGREECGE AWANGPLALH LRLSSPSAGG ALFWLRLPAF QHGCPPIRRR
KRTPRLFVGL TPPLANWLCS PAASLHPQAA LRAWTSFPRC RCSNGVSFSC NGETRNGSTC
QPPSGPHSHL QLLCRLRKTS GVVLLDLKEG PEGNKREVAV SAEVSFPQKW DSWHRDLQRI
RSVITPSQFK LSNYKVSITE KQPTGTLVSS PRRWDSRHQG LRRIRSVNTP LQFRLTNDQV
SIAKNEPART LVSPQGWGFW HRGLQGMQTV NTLPQFKLTN YQVSIAENEP AGTVVSSPQR
WDSRHQGPRW MRSVNTPPQF KLTNYQVSIP ENQPSGTVVI ALEAHDPDEG EAGHLVYSIE
AFFDKRSNDY FSINAGTGVV TTTRSLDRET KDTHVLQVTA TDQGAPRHRS ATTFLTVTVS
DTNDHGPVFE QPEYRENIRE NLEVGYEVLT IRATDKDAPD NANLLYRILE PGAGEGVFEI
DPHSGVVRTC APVDREEVSE YHLVVEANDQ GKDPGPRSAT VTVHISVEDE NDNSPQFSEK
RYQVQIPEDT PINNQVLQVQ ATDRDRGSNA QVHYSIVSGN LKGQFYIHSF SGSIDLINPL
DYETIREYTL RIKAQDGGRP PQINSSGMVS IQVLDVNDNA PIFVSTPFQA TVLENVPVGY
SVLHIQAVDA DSGDNARLEY KLIEVAHPSS LVATVGDMSF PFQINNSTGW ITVSVELDRE
TVENYHFGVE ARDHGIPVMT SSASVSITVL DVNDNSPTFT EKVYQLRLNE DAVVGSSVLT
LTAVDKDVNS VVTYQITSGN TRNRFAITSQ SAGGLITLAL PLDYKQERQY VLTVTASDGT
LFDTVQVHIN VTDANTHRPV FQSSHYTVSV SEDKPVGTSI VTIVATDEDT GENARITYVL
EDNIPQFRID PDTGTITTLM ELDYEDQASY TLAITAQDNG IPQKSDTTYV EILILDANDN
VPRFLRDRYQ GAVFEDVPLS TSVLQVSAVD RDSGPNGRLL YTFQGGDDGD GDFYIEATSG
VIRTLRKLDR ENVAVYSLRA FAVDRGSPPL KASVDIQVTV LDINDNPPVF EQDEFDIYVE
ENSPVGSIVA RISAVDPDEG TNAQIMYQIV EGNIPEVFQL DLLNGDLTAL MDLDYESQTE
YVIVVQATSA PLVSRATVHI RLRDQNDNPP VLQDFQILFN NYVTNKSNSF PSGVIGKIPA
HDPDISDHLD YTFVQGNELN LLLLDSATGE LKLSRDLDNN RPLEAIMKVS VSDGIHNVTA
LCTLRVTIIT DDMLTNSITV RLENMSQEKF LSPLLALFVE GVATVLSTTK EGIFVFNIQN
DTDVSSNILN VTFSALLPGG IRNEFFPSED LQEQIYLNRT LLTLISTQRV LPFDDNICLR
EPCENYMKCV SVLKFDSSAP FISSNSVLFR PIHPINGLRC RCPPGFTGDY CETEIDLCYS
NPCGNNGLCR SREGGYTCEC YEDYTGEYCE VNARSGRCAP GVCKNGGTCI NLLIGGFKCE
CPPGEYERPY CEMTTRSFPP LSFVTFKGLR QRFHFTVSLM FATRERNALL LYNGRFNEKH
DFIALEIIEE QIQLTFSAGE TTTTVAPFVP GGVSDGQWHS VQVQYYNKPN IGRLGIPHGP
SGEKVAVVTV DDCDTAVAVR FGSLIGNYSC AAQGTQTGSK KSLDLTGPLL LGGVPNLPED
FPVHNRQFVG CMRNLSIDSK QVDMASYIAN NGTLAGCLAQ KNYCTSNWCQ NGGSCVNKWN
TYSCDCPLQY GGKNCEQVMT FPYRFTGESI IIWSDLDITI SVPWYIGLMF RTRKVNGMLM
QANAGLSSKI NIQILNKHVV FEVYDGLNKI ANLTMAQSRV SDGEWHHLLI ELKSAKDGKD
IKYLAVVTLD YGMYQSTVQI GNQLPGLKMK SIIVGGVSGD HVSVQQGFYG CLQGVRMGET
PTNVATLNTE QATKIHVTEG CEVDNPCDSN PCPLHSYCSD DWDSYSCICD PGFFGTDCVD
VCSLNPCQHV SACVHKPSSS HGYTCECGQS YYGQYCESKI DLPCPRGWWG NPICGPCNCE
ISKGFDPDCN KTNGECRCMA NHYRPQNSDT CYPCDCLPSG SQNRTCDNET GQCPCKAGVI
GRQCNRCDNP FAEVTVHGCE VVYNGCPKAF EAGIWWPQTK FGQPAAVPCP KGSVGNAVRH
CNSEKGWLPP ELFNCTTVGF MDLKIMNEKL LRNETNMDGD KSVQIAKVLH SATNHTGSFY
GNDVRTAYQM MIRVLQYESQ QQGFDLAATR DVDFNENIIR AGSALLEPST KEHWEHIQRT
EGGTAHLLKH YEEYFNTVAK NMQKTYMKPF IIVAANMIIA VDIFEKSNFT GAKVPRFDAI
KEDYPRDLES SVLFPDTLFK ASNRKAVPTM KPANYIFPSK KGDEIFKKVL TKRKRRHPEE
SNQHATAIVI IYRTLGRFLP ESYDPDRRSL RLPNRPIINT PIISTIVYRD GESLPNLLES
PITLEHVMME TEERTKPVCV FWNHSTTIGE TGGWSSKGCE MFSRSQSHVI CQCNHLTSFA
VLMDISKREN GEALPLKIIT YTTVSISLAA LLLTFILLVL IRTLRSNLHS IHKNLVAALF
FSELVFLIGI NQTENPFVCT VIAILLHYFY MSTFAWMFVE QLHIYRMLTE VRNINFGHMR
FYYVMGWGIP AIITGLAVGL DPQGYGNPDF CWLSVHDTLI WSFAGPIVIV VVINIIIFIL
AVKASCRRRQ RSLEKTGIIS VLRTAFLLLL LISATWLLGL MAVNSDVMTF HYLFAVFSCL
QGLFIFFFHC IFNKEVRKHL KNTFTGKKPL PDDSTTTRAT LLTRSLNCND TYIEEPNMYR
TTIGESTVSL ESTVRDEAAQ KLSVSSSQAR AGHTEGDSSI FRRKPSKSHE HDSDSDSELS
LDEHSSSYAS SHSSDSEEDA IDAEKKWNAA TSKSNDRGPL HSTPKVDSLP NHVKSYWPSE
SIAASDGEEP SAKQKLKVET KVNVELHQEN QANHSSEIPP DKENEVQQKE NKPFSQQNHQ
QPEQRKGILK NKVTYPPPLV DKNIKNRLRE KLSDYNQTTI SSRMTAIGTN NGIRSNSDSG
VTVKNPRRDQ LPEQINGLAM NLHVGTGTAE TSDSE
//
