ID F1Q9V2_DANRE Unreviewed; 1519 AA.
AC F1Q9V2; A0A8M9Q5J0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 3.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Adhesion G protein-coupled receptor L1 isoform X2 {ECO:0000313|RefSeq:XP_021330396.1};
DE SubName: Full=Adhesion G protein-coupled receptor L1a {ECO:0000313|Ensembl:ENSDARP00000106818};
GN Name=adgrl1a {ECO:0000313|Ensembl:ENSDARP00000106818,
GN ECO:0000313|RefSeq:XP_021330396.1,
GN ECO:0000313|ZFIN:ZDB-GENE-131127-267};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000106818};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000106818}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000106818};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000106818, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000106818};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_021330396.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021330396.1};
RG RefSeq;
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 EMBL; AL928740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX908755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01042923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01042924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01066899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01066900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO904949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LO018428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LO018532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_021330396.1; XM_021474721.1.
DR PaxDb; 7955-ENSDARP00000106818; -.
DR Ensembl; ENSDART00000124480; ENSDARP00000106818; ENSDARG00000089292.
DR Ensembl; ENSDART00000124480.3; ENSDARP00000106818.3; ENSDARG00000089292.4.
DR AGR; ZFIN:ZDB-GENE-131127-267; -.
DR ZFIN; ZDB-GENE-131127-267; adgrl1a.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_002753_0_2_1; -.
DR TreeFam; TF351999; -.
DR Proteomes; UP000000437; Chromosome 3.
DR Bgee; ENSDARG00000089292; Expressed in retina and 3 other cell types or tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0016524; F:latrotoxin receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd16007; 7tmB2_Latrophilin-1; 1.
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; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR031234; Latrophilin-1_TM.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
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; SSF81321; Family A G protein-coupled receptor-like; 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 ECO:0000313|RefSeq:XP_021330396.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1519
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041116746"
FT TRANSMEM 845..872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 913..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 952..971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1014
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1035..1058
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1064..1087
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..129
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 134..393
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 471..527
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 847..1088
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 398..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1519 AA; 168617 MW; 56B6C6559072D9C1 CRC64;
MALALWILFT CTIALSHVRP SAQALSRSAM PFGLMRRELA CEGYPIELRC PGSDVIMIET
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDV FPDPCPGTYK
YLEIQYECVP YIFVCPGTLL RVQAASLLQE AEHQSGAWCK DPLQSGDRLY VMPWTPYRTD
MLYEYASWED FKQNRATTTY KLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG
EAIVNNANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATEA NNGRLVVSQV NPYTLRFEGT
WETSFDKRLA SNAFMACGVL YAVRSVYQDD DSEAGGDLVL YAYNTNRARE EPVHIPFPNP
YQYVSSVDYN PRDNQLYVWN NYNVLRYPLE FGPPDPTAGP PVTTQMSSST TTAARPITST
SLPSTIRPLP PTAHPIGAIN KAPDLRPITA TVPVTRRPLR VPPQGPEIEV CESRVARGVQ
WPATQKGETV DRPCPKGSLG IASFQCLSSP VLWNPRGPDL SNCTSPWVNQ VAQKIKSGEN
AANIAAELVN HTQGRIHAGD VSSSVRLIEQ LLDILDAQLQ ALRPGNKESA ARNYNKWQKR
ERTCRAYVQA VVQTVDNLLR AEALESWQDM NSTEQAHTAT MLLDVMEKGA FLLANNMYNN
HFSDHAANVD LEVRVLNTET DSQDLSFPQS GPSDSSIQLS ASTFKQYSRN GQVKVVFVLY
KNLGSFLSTE NATVKMEMEA GIGGRGLAVN SHVIAASINK ESSRVFLTEP VVFTLRHLQL
ENHFSPNCSF WNYSERSMTG QWSSQGCRLI ETNSTHTTCS CSHLTNFAVL MVHHEPDYPG
RMHELILFVI TWVGIVISLV CLAICISTFC FLRGLQTDRN TIHKNLCINL FIAELLFLIG
IDKTQYHIAC PIFAGLLHFF FLAAFSWMCL EGIQLYLMLV EVFESEYSRK KYYYLCGYCF
PALVVGISAA IDYRSYGTKK ACWLRVDNYF IWSFIGPVSF IIMLNLVFLM ITLHKMIRNS
SALKPDSSRL DNIKSWALGA IALLFLLGLT WAFGLLFINE NTVIMAYLFT TFNAFQGMFI
FIFHCALQKK VHKEYSKCLR HSYCCSRTST TSSHGSLKNS ALRTNNRYYT GSQTRHAAVH
RQSRIRRMWN DTVRKQTESS FMAGDINSTP TLNRGTMGNH LLTNPVLQTR TGSSPYNTLL
AETFTPPSPG VFNSTGTFRD PKSTLSKNRD HGGMETLPLN GNFNNSYSLR SVGGSGAPGG
SCDFLGGGGG DSPPPLLNPR GSETLGGIRR NLSDAAAFEK MIISELVHNN LRGGGGVGGG
DRTCGSLARG HGHLGMGRAG GGVEPVIGME DDEDFRSREA RQRTPQDVEL LYKALEEPLL
LQRAQSVLYQ SDPDESESYT ADLTESLGHS GHSAQSAAGQ GHSGPPDSPA RDSLYTSITN
LRDSPYPDSS PEPLEVVPRS AQPPEELYYS SGRPAIGSRG APMQTFYQAP PRRPSTEAHP
APEAPHSEGD GQMQLVTSL
//
