ID H3CKW2_TETNG Unreviewed; 1364 AA.
AC H3CKW2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Adhesion G protein-coupled receptor L2a {ECO:0000313|Ensembl:ENSTNIP00000008891.1};
GN Name=ADGRL2 {ECO:0000313|Ensembl:ENSTNIP00000008891.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000008891.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000008891.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR Ensembl; ENSTNIT00000009062.1; ENSTNIP00000008891.1; ENSTNIG00000006144.1.
DR GeneTree; ENSGT00940000156348; -.
DR HOGENOM; CLU_002753_1_0_1; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd22845; Gal_Rha_Lectin_LPHN2; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; IPR003924; GPCR_2_latrophilin.
DR InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF61; ADHESION G PROTEIN-COUPLED RECEPTOR L2; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02354; Latrophilin; 2.
DR Pfam; PF02191; OLF; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01444; LATROPHILIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF111418; Hormone receptor domain; 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; PS51132; OLF; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00446};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000007303};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 TRANSMEM 794..816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 828..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 931..957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1006..1029
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..133
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 143..402
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 410..467
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 788..1030
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1258..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 144..326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1364 AA; 153783 MW; 39579322CDD3BD83 CRC64;
KISFLCRVDS LWLRYLLHLS PPSPLFLGFS RAALPFGLVR RELSCEGYPI DLRCPGSDVI
MIESANYGRT DDKICDADPF QMENINCYLP DAYKIMSQRC NNRTQCIVIT GSDVFPDPCP
GTYKYLEVQY ECVPYKVEQK VFLCPGTLKA VGDPSFLFEA EQQAGAWCKD PLQAGDKIYF
MPWTPYRTDT LIEYSSLDDF QNGRQTITYK LPHRVDGTGF VVYDGAVFFN KERTRNIVKF
DLRTRIKSGE AIINNANYHD TSPYKWGGKT DIDLAVDENG LWVIYATEQN NGMMVISQLN
PYTLRFEATW DTAYDKRSAS NAFMVCGVLY VVRSTYEDNE SEVSKSLIDY IYNTKLSRGE
YVDIHFPNQY QYITAVDYNP RDNQLYVWNN FYILKYNLDF GPPDPAHERF CKATEERDIM
WPQTPRGMLV ERPCPKGTRG TASYLCVLSS GTWNPKGPDL SNCTSHWVNQ VAQKIRSGEN
AANLANELAK HTKGPIFAGD VSSSVRLMEQ LVDILDAQLQ ELRPSEKDSA GRSFNKLQKR
ERTCRAYMKA IVDTVDNLLR PEALKSWQDM NSTEQTHAAT MLLDTLEEGA FVLADNLMEP
AIVKVPAENI ILDVYVLSTD GQVQDFKFPQ SNEDGISIHL SANTVKLNSR NGVAKLVFVL
YKNLSQFLTA ENATIKMANE AYGRNVSVAV NSDIIAASIN KESSRVFIND PVIFTLKHIN
MEHYFNSNCS FWNYSERSMM GYWSTQGCKL LESNKTHTTC SCNHLTNFAV LMAQREISGN
NIGHELLLTI ITRVGIVVSL VCLTISIFTF CFFRGLQSDR NTIHKNLCIN LFIAELIFLI
GIDMTEPTIG CAIIAGILHF SSWHLFWMCL EGVQLYLMLV EVFESEYSRK KYYYVSGYLF
PAIVVAVSTA IDYKSYGTKK ACWLSVDNHF IWSFIGPVTF IIMLNLIFLV ITMYKMVKHS
TTLKPDSSRL ENINKVLWSW APFALLCLLG LTWSFGLFFI NEASIVMAYL FTIFNTFQGM
FIFIFHCLLQ KKVRKEYSKC FRHTYCCGGL PAESSHGSVK TSTTRTSARY SSGTQSRIRR
MWNDTVRKQS ESSFISGDIN STSTLNQGHS LNSVMRDTSA MDTLPLNGNF NNSYSLRNGD
FGDSVQVVDC GLSLDDAAFE KMIISELVHN NLRACNKSSQ TERAPPKVTI LGGSSSEDNG
IVANTSSLVH VGDAVGIELH HQQELEAPLI PQRTHSLLYP PQRKVRTSGG VEAFVEELTS
TTNPEDSSQS PNRDSLYTSM PNLRDSPSPE SNSEVVEDLS PSKRSESEDI YYKSMPNLGG
GNQLQAYYQI GRGTSDGYII PILTEGCIPE GDVREGQMQL VTSL
//
