ID H3CIS6_TETNG Unreviewed; 1221 AA.
AC H3CIS6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Adhesion G protein-coupled receptor L1a {ECO:0008006|Google:ProtNLM};
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:ENSTNIP00000008154.1, 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:ENSTNIP00000008154.1}
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 AlphaFoldDB; H3CIS6; -.
DR Ensembl; ENSTNIT00000008319.1; ENSTNIP00000008154.1; ENSTNIG00000014104.1.
DR GeneTree; ENSGT00940000167471; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd22844; Gal_Rha_Lectin_LPHN1; 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; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR12011:SF62; ADHESION G PROTEIN-COUPLED RECEPTOR L1; 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; 1.
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; SSF111418; Hormone receptor domain; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..915
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..945
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1006..1028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1064..1087
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1093..1116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..138
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 143..406
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 481..537
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 861..1117
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DISULFID 144..326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1221 AA; 135006 MW; C9F05C1ABB934B59 CRC64;
IVNSGCLFTM AVSLWFLGVC ALLLSYVDPS SQAMSRAAMP FGLLRRELAC EGYPIELRCP
GSDVVMVETA NYGRTDDKIC DADPFQMENT QCYLPDALKI MAQRCNNRTQ CVVVAGVDVF
PDPCPGTYKY LEIQYECVPY IFVCPGSLLS IQPASSLLEA EHQSGAWCKD PLQAGDRLYV
MPWTPYRTEM LYEYASWDDY RQNRATTTYK CPAGVDGTGF VVYDGAVLYN KERTRNLVKY
DLRTRIKSGE AVVVNANYHD TSPYRWGGKS DIDLAVDENG LWVIYSTEAN NGRIVVSQVN
PYTLRFEGTW ATGFDKRGAS NAFMACGVLY AVRSVFQDDE GQTEGRAGSD MVVYAYDTSR
GQELPVQIPF PNPYQYISSI DYNPRDNQLY VWNNYYVLRY PLQFTPPPPT KGPLSSLMTT
VRSYTATVAL SPARPSASHP IGVINRGPFD QRPITAMVPL TPRPPLRVPL DPGGSGQVGG
CEGRVARGVQ WPPTLMGETV ERPCPKGSLG IASYQCMQSP VGWSSRGPDL SNCTSPWVSQ
IAQKIKSGEN AANIAGELVN LTRGLIYAGD VSMSVRLVEQ LLDVLDSQLQ ALRPANRESA
ARNYNKLQKR ERTCKAYVQA VVQTVDNLLG PEALVSWADM NSVDQSRSAS LLLDAVEKGA
FLLANNLYEG RFSDRAPNPD LEVYVLNTEA DMQDLTFPHS YDSDSILQIS ALALQQYSSN
GQVKLVLTLY KNLGSFLTTQ NSTLRLGLGL GQGSDTRRRT LVVNSHVISA SVHRGSNRVY
LSEPVIFTLR HLQLDNHFGP NCSFWNSSGV SGNGRWSTQG CRLLHTNNTH TTCACNHLSS
YAVLMTYEQP AFGAGVEELL VFVVCWVGIS VALVCLLTCL TTLCCQGALW HTDHSTIHCN
LWANLVITEL LFILGANRTQ YTVVCSITAG LLHFSLLSVF CWLCLEGVEL CLLQREVFEG
HNSRRKYFYL CGYSIPGLVV AVSAAIDFRG YGSKTACWLR SDNYFIWSFL GPVGAVITLN
LVVLVMTLHR MHSTADLKPD SGRHDNLRLN RRCIAAFTED INRAWAVGSL TLLFLQSVTW
SSGLMFLSAP SLLLAYLFSS LNTAQALLIT ILHCTLARKG QKDYSRCLRL SQCCITSSSS
SPDSVKGAAL RSNSRYTSSQ SSRIRRMWND TVRRQTESSF IAADVNNTPT LNRAPLGNHF
LTNPVLQTHA GASPYDTMLA Q
//
