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Database: UniProt
Entry: A0A3B5RBI3_XIPMA
LinkDB: A0A3B5RBI3_XIPMA
Original site: A0A3B5RBI3_XIPMA 
ID   A0A3B5RBI3_XIPMA        Unreviewed;      1553 AA.
AC   A0A3B5RBI3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSXMAP00000039231.1};
GN   Name=ADGRL2 {ECO:0000313|Ensembl:ENSXMAP00000039231.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000039231.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000039231.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000039231.1};
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   STRING; 8083.ENSXMAP00000039231; -.
DR   Ensembl; ENSXMAT00000032931.1; ENSXMAP00000039231.1; ENSXMAG00000017908.2.
DR   GeneTree; ENSGT00940000156348; -.
DR   InParanoid; A0A3B5RBI3; -.
DR   OMA; XTASYLC; -.
DR   OrthoDB; 1114672at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0071603; P:endothelial cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0035331; P:negative regulation of hippo signaling; IEA:Ensembl.
DR   GO; GO:0043114; P:regulation of vascular permeability; IEA:Ensembl.
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   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:UP000002852};
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..1553
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017326334"
FT   TRANSMEM        879..900
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        912..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        942..966
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        978..997
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1017..1040
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1086..1108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1114..1137
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          161..420
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51132"
FT   DOMAIN          494..551
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          873..1138
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          461..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1341..1384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1440..1487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..489
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        162..344
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ   SEQUENCE   1553 AA;  174809 MW;  1691DAA75B52D67A CRC64;
     MACSLRTLHT FCWFLITLNQ VHSTEGFSRA ALPFGLVRRE LSCEGYPIDL RCPGSDVIMI
     ESANYGRTDD KICDADPFQM ENINCYLPDA YKIMSQRCNN RTQCIVITGS DVFPDPCPGT
     YKYLEVQYEC VPYSPCPTRI GSRAQNVSYH NCPEVEQKVF LCPGTLKAVG DPSFRFEVEQ
     QAGAWCKDPL QAGDKIYFMP WTPYRTDTLI EYSSLDDVQN ARQTITYKLP HRVDGTGFVV
     YDGAVFFNKE RTRNIVKFDL RTRIKSGEAI INNANYHDTS PYKWGGKTDI DLAVDENGLW
     VIYATEQNNG MMVISQLNPY TLRFEATWET AYDKRSASNA FMVCGVLYVV RSTYEDNESE
     VSKSLIDYIY NTKQNHGEFV DIHFPNQYQY IAAVDYNPRD NQLYVWDNFY VLRYNLEFGP
     PDPAHAPPLS EVTTATQPQR TTTVTTTTTA HWGAANTTTT VLKEGSRRAP KPPPVIPQTT
     SPPPLESFPL PERFCKATEK RDIMWPQTQR GMLVERPCPK GTRGTASYLC LLSTGDWHPK
     GPDLSNCTSH WVNQLAQKIR SGENAANLAN ELAKHTKGPI FAGDVSSSVR LMEQLVDILD
     AQLQEYRPSE KDSAGRSFNK LQKRERTCRA YMKAMVDTVD NLLRPEALKS WHDMNSTEQT
     HAATMLLDTL EEGAFVLADN LMEPAIVKVP ADNIILDVYV LSTDGQVQDF KFPQSSKSGI
     SIQLSANTVK LNSRNGVAKL VFVLYKNLSQ FLGTENATIK MANEAYGRNV TVAVNSDIIA
     ASINKESSRV FINDPVIFTL QHIDMEHYFN SNCSFWNYSE RSMMGYWSTQ GCKLLDSNKT
     HTTCACSHLT NFAILMAHRE ISGSVRDHHE LLLTVITRVG IVVSLVCLTI CIFTFCFFRG
     LQSDRNTIHK NLCINLFIAE LIFLIGIDMT EPRIGCAIIA GILHFFFLAS FSWMCLEGVQ
     LYLMLVEVFE SEYSRKKYYY VSGYLFPAIV VGVSAAIDYG SYGTHKACWL SVDNHFIWSF
     IGPVTFIIML NLIFLVITMY KMVKHSTTLK PDSSRLENIN NYRVCDGYYN TDLPGYEDNK
     HFIKSWVMGA FALLCLLGLT WSFGLFFISE ASIVMAYLFT IFNTFQGMFI FIFHCLLQKK
     VRKEYSKCFR HTYCCRGLPT ESSHGSTKTS TTRTSARYSS GTQVDQQLYT SRIRRMWNDT
     VRKQSESSFI SGDINSTSTL NQGMTGNYLL TNPLLRPQGT NNPYNTLLAE TVVCNTPTAP
     VFNSPVTFRE TRHSLNSAVR DTSAMDTLPL NGNFNNSYSL RNGDFGDSVQ VVDCGLSLDD
     AAFEKMIISE LVHNNLRACN KSHQQQQHSS LRHPPHRQQL PPPQYHHHHH TERAPPKVTV
     VGGSSSEDDA IVADTSSLVH MGNAVGLELH HQQELEAPLI PQRTHSLLYA PQKKVRTDGG
     VDTFVSPLTP TNPDDSAQSP NRDSLYTSMP NITDSPCPES SPDVVEDVSP IKGSENEDVY
     YKSMPNLGAG HQLQAYYQIG RGSSDGYIIP VTKEDCIPEG DVQEGQMQLV TSL
//
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