ID A0A3P8VH55_CYNSE Unreviewed; 1531 AA.
AC A0A3P8VH55;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSCSEP00000013682.1};
GN Name=ADGRL2 {ECO:0000313|Ensembl:ENSCSEP00000013682.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000013682.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000013682.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000013682.1}
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 RefSeq; XP_016898286.1; XM_017042797.1.
DR Ensembl; ENSCSET00000013842.1; ENSCSEP00000013682.1; ENSCSEG00000008720.1.
DR GeneTree; ENSGT00940000156348; -.
DR InParanoid; A0A3P8VH55; -.
DR Proteomes; UP000265120; Chromosome 2.
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:InterPro.
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; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000265120};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1531
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018220400"
FT TRANSMEM 860..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 893..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 998..1021
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1067..1089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..131
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 141..400
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 476..533
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 854..1119
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 405..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 142..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1531 AA; 172318 MW; 9B3FF89A0A88E2F3 CRC64;
MARSLWNLHT VCWFLLTLTH VHSTEGFSRA ALPFGLVRRE LSCEGYPIDL RCPGSDVIMI
ESANYGRTDD KICDADPFQM ENINCYLPDA YKIMSQRCNN RTQCIVITGS DVFPDPCPGT
YKYLEVQYEC VPYKVEQKVF LCPGTLKSVG EPSFVYEAEQ QAGAWCKDPL QAGDKIYFMP
WTPYRTDTLI EYSSLDDFQN ARQTITYKLP HRVDGTGFVV YDGAVFFNKE RTRNIVKFDL
RTRIKSGEAI INNANYHDTS PYKWGGKTDI DLAVDENGLW VIYATEHNNG MMVISQLNPY
TLRFEATWDT AYDKRSASNA FMVCGVLYVV RSTYEDNESE VSKSLIDYVY NTKQNRGEYV
DIHFPNQYQY IASVDYNPRD NQLYVWNNFY ILRYNLEFGP PDPAHAPPLS EVTSSPPSQR
TTSTTTTTTT AHRGVANTTA TTGLREGSRG APGAPPLTPH TTSPPPLESF PLPERYCEAA
ERRDIMWPQT QRGMLVERPC PKGTRGTASY LCVLSTGAWN PRGPDLSNCT SHWVNQVAQK
IRSGENAANL ANELAKHTKG PIYAGDVSSS VRLMEQLVDI LDAQLQELRP SEKDSAGRSF
NKLQKRERTC RAYMKAIVDT VDNLLRPEAL KSWRDMNSTE QTHAATMLLD TLEEGAFVLA
DNLMEPAFVK VPADNIILDV YVLSTDGQVQ DFKFPQSSKS GISIQLSANT VKLNSRNGVA
KLVFVLYKNL GQFLSTENAT IKMENEAYGR NMSVAVNSDI IAASINKESS RVFINDPVIF
TLEHIDMEHY FNSNCSFWNY SERSMMGYWS TQGCKLLESN KTHSTCSCSH LTNFAILMAH
REISVNDRVH ELLLTVITRV GIVVSLVCLT ISIFTFCFFR GLQSDRNTIH KNLCINLFIA
ELIFLIGIDM TEPRVGCAII AGILHFFFLA SFSWMCLEGV QLYLMLVEVF ESEYSRKKYY
YVSGYLFPAI VVAVSAAIDY QSYGTKTACW LSVDNHFIWS FIGPVTFVIM LNLIFLVITM
YKMVKHSTTL KPDSSRLENI NNYRVCDGYY NTDLPGYEDN KRFIKSWVMG AFALLFLLGL
TWSFGLFFIS EASVVMAYLF TIFNTFQGMF IFVFHCLLQK KVRKEYSKCF RHTSCCGGLP
TESSHSSAKT STTRTSARYS SGTQSRIRRM WNDTVRKQTE SSFISGDINS TSTLNQGMTG
NYLLTNPLLR PQGTNNPYNT LLAETVVCNT PTAPVFNSPV TYRETRHSLN KAVRDTSAMD
TLPLNGNFNN SYSLRNGNFG DSVQVVDCGL SLDDAAFEKM IISELVHNNL RACNKSIQQQ
QQQQQHHLHH SLHHPPNHQH QQPPQYHHHH HVERAPPKVT VIGGGEDGAI VADASSLARM
SNTVGLKVHH QQELEAPLIP QRTHSLLYTP QKKVRTDGGV DSFVSQLTPS NPDDSLQSPN
RDSLYTSMPD LRDSPCAESS PDVVEDVSSS KSESEDIYYK SMPNLGSGHQ LQAYYQIGRG
GSDGYILPVT KEGCSPEGDV REGQMQLVTS L
//