ID F1MGL8_BOVIN Unreviewed; 1575 AA.
AC F1MGL8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000313|Ensembl:ENSBTAP00000039471.4};
GN Name=ADGRL3 {ECO:0000313|Ensembl:ENSBTAP00000039471.4,
GN ECO:0000313|VGNC:VGNC:53686};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000039471.4, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000039471.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000039471.4,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000039471.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000039471.4};
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 RefSeq; XP_005208060.1; XM_005208003.3.
DR Ensembl; ENSBTAT00000039682.4; ENSBTAP00000039471.4; ENSBTAG00000013918.6.
DR VEuPathDB; HostDB:ENSBTAG00000013918; -.
DR VGNC; VGNC:53686; ADGRL3.
DR GeneTree; ENSGT00940000155527; -.
DR HOGENOM; CLU_002753_0_2_1; -.
DR TreeFam; TF351999; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000013918; Expressed in semen and 84 other cell types or tissues.
DR ExpressionAtlas; F1MGL8; baseline and differential.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd16005; 7tmB2_Latrophilin-3; 1.
DR CDD; cd22846; Gal_Rha_Lectin_LPHN3; 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:SF60; ADHESION G PROTEIN-COUPLED RECEPTOR L3; 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 Reference proteome {ECO:0000313|Proteomes:UP000009136};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1575
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018525244"
FT TRANSMEM 942..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1001..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1044..1064
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1084..1107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1166..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 103..192
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 197..456
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 561..617
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 940..1190
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 23..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 198..380
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1575 AA; 175452 MW; 565BA8AB310D0386 CRC64;
MWPSQLLVFM MLLAPIIHGG KHSERHPALA SPLRHAERGP GGALPPRHLL QQPAAERATA
HRGPGPRGAT RGVRGPGAHG AQISAQAFSR APIPMAVVRR ELSCESYPIE LRCPGTDVIM
IESANYGRTD DKICDSDPAQ MENIRCYLPD AYKIMSQRCN NRTQCAVVAG PDVFPDPCPG
TYKYLEVQYE CVPYIFLCPG LLKGVYQSEH LFESDHQSGA WCKDPLQASD KIYYMPWTPY
RTDTLTEYSS KDDFIAGRPT TTYKLPHRVD GTGFVVYDGA LFFNKERTRN IVKFDLRTRI
KSGEAIIANA NYHDTSPYRW GGKSDIDLAV DENGLWVIYA TEQNNGKIVI SQLNPYTLRI
EGTWDTAYDK RSASNAFMIC GILYVVKSVY EDDDNEATGN KIDYIYNTDQ SKDSLVDVPF
PNSYQYIAAV DYNPRDNLLY VWNNYHVVKY SLDFGPLDSR SGQAHHGQVS YISPPIHLDS
DLERPPVREI STTGPLGTGS TTTSTTLRTT TWSPGRSTTP SVSGRRNRST STPSPAIEVL
NDITTHVPSA SPQIPALEES CEAVEAREIM WFKTRQGQMA KQPCPAGTIG VSTYLCLAPD
GIWDPQGPDL SNCSSPWVNH ITQKLKSGET AANIARELAE QTRNHLNAGD ITYSVRAMDQ
LVGLLDVQLR NLTPGGKDSA ARSLNKLQKR ERSCRAYVQA MVETVNNLLQ PQALNAWRDL
TTSDQLRAAT MLLDTVEESA FVLADNLLKT DIVRENTDNI QLEVARLSTE GNLEDLKFPE
NTGHGSTIQL SANTLKQNGR NGEIRVAFVL YNNLGPYLST ENASMKLGTE AMSTNHSVIV
NSPVITAAIN KEFSNKVYLA DPVVFTVKHI KQSEENFNPN CSFWSYSKRT MTGYWSTQGC
RLLTTNKTHT TCSCNHLTNF AVLMAHVEVK HSDAVHDLLL DVITWVGILL SLVCLLICIF
TFCFFRGLQS DRNTIHKNLC ISLFVAELLF LIGINRTDQP IACAVFAALL HFFFLAAFTW
MFLEGVQLYI MLVEVFESEH SRRKYFYLVG YGMPALIVAV SAAVDYRSYG TDKVCWLRLD
TYFIWSFIGP ATLIIMLNVI FLGIALYKMF HHTAILKPES GCLDNINYED NRPFIKSWVI
GAIALLCLLG LTWAFGLMYI NESTVIMAYL FTIFNSLQGM FIFIFHCVLQ KKVRKEYGKC
LRTHCCSGRS TESSIGSGKT SGSRTPGRYS TGSQSRIRRM WNDTVRKQSE SSFITGDINS
SASLNRGAMA NHLISNALLR PHGTNNPYNT LLGEPAVCNN PSVSMYNAQE GLLNNARDTS
VMDTLPLNGN HGNSYSIASG EYLSNCVQII DRGYNHNETA LEKKILKELT SNYIPSYLNN
HERSSEQNRN LMNKLVNNLG SGSEDDAIVL DDATSFNHEE SLGLELIHEE SDAPLLPPRV
YSTENHQLHH YTRRRIPQDH SESFFPLLTN EHTEDLQSPH RDSLYTSMPA LAGVPTAESV
TTSTQTEPPP AKCGDAEDVY YKSMPNLGSR NHVHQLHTYY QLGRGSSDGF IVPPNKDGTP
PEGSSKGPAH LVTSL
//
