ID A0A3B3X647_9TELE Unreviewed; 1071 AA.
AC A0A3B3X647;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Adhesion G protein-coupled receptor L3.1 {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000010526.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000010526.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3X647; -.
DR Ensembl; ENSPMET00000017401.1; ENSPMEP00000010526.1; ENSPMEG00000012638.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.25.40.610; -; 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 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; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02354; Latrophilin; 2.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01444; LATROPHILIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 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.
PE 4: Predicted;
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 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 482..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 624..647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..159
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 480..721
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..952
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 118626 MW; 8E47B9AA054C2EF2 CRC64;
MLPPNRGGAG GGGGGSSSSS TSRATTTRSP PYYTTPRPLL TTSPGQRYRT TTTVRQPILV
PAGGASSDSN HIPDTNQKAG RSPPVQVPPA APQPPALPPQ DFCTPRVTAD ISWPRTQQGQ
TAKQPCPVGT LGVATYVCLP RLGYWAPQGP DLSNCTSPWV NHIMQKLRSG ETAAIVAKEL
AEQTKGLLRP GDVPSTVRAM AQLVELLDVQ LRNLTPGGKD SAARSLTKLQ KRERSCRFFT
QAMVETVNNL LHPRAQAAWK ELPTSEQLHS ATLLLDTVET GAFMLADNLL KTDTVQETTD
YIQLEVARLS TDGNLADLTF PQSEQHGNAI QLSASTLKQH GRNGEIRMAF VLYRNLGSYL
PTENASVRLS SEAVYPNYSV IVNSPVITAS INKESNKVYL SEPVVFTVQH LQQSEKNFNP
NCSFWSYSKR TMTGFWSTQD CRLLATNRTH TSCSCTHLTS FAVLMAHVEV KVHSMHDMLL
DVITWVGILL SLVCLLICIF TFCFFRGLQS DRNTIHKNLC ISLFIAESLF LVGINKADQP
IVCAVFAALL HFFFLAAFTW MFLEGVQLYI MLVEVFESEH SRTKYFYLAG YGVPAVIVAV
SAAVDYRSYG TDRVCWLRLD TYFIWSFIGP ATLIIMLNVI FLGIALYKMF HHTAILKPDS
GCLDNIKSWV IGAIALLCLL GLTWAFGLMY INESTVIMAY LFTIFNSLQG MFIFIFHCIL
QKKVRKEYGK CLRTHCCSGK SVETSISSSS KTTTSRTPGR YSTGSQSRIR RMWNDTVRKQ
ESSFITGDIN SSATLNREGI LNNARDASVM DTLPLNGNHP NNFSMASSEY LSDCVQILDR
SGGYGTHSNH KETTLEKKIL KELTSNYIPP YLNNHERATT ERSHNLMNKL VNSNMANGED
NSPIVLDNPA AFPHEENLGL EIIREESNAP LLPPRPPPPD SHPPPPPPPH SFSRQRRIAQ
EPSESFFPLL TNEHTDEHTH SPNHRDSLYT SMPDSSGELQ PCKSATAPEL DDVYYKSMPN
LGSRNHLHEL QNYYHMGRGG SDGYMVSGSK EESDSSPEEP PVDPSHLVTS L
//
