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Database: UniProt
Entry: W5ND92_LEPOC
LinkDB: W5ND92_LEPOC
Original site: W5ND92_LEPOC 
ID   W5ND92_LEPOC            Unreviewed;      1254 AA.
AC   W5ND92;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=G-protein coupled receptors family 2 profile 2 domain-containing protein {ECO:0000259|PROSITE:PS50261};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000018601.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000018601.1}
RP   IDENTIFICATION.
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}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       Adhesion G-protein coupled receptor (ADGR) subfamily.
CC       {ECO:0000256|ARBA:ARBA00007343}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01172}.
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DR   EMBL; AHAT01016976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01016977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01016978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5ND92; -.
DR   STRING; 7918.ENSLOCP00000018601; -.
DR   Ensembl; ENSLOCT00000018633.1; ENSLOCP00000018601.1; ENSLOCG00000015115.1.
DR   eggNOG; KOG4193; Eukaryota.
DR   GeneTree; ENSGT00940000156341; -.
DR   HOGENOM; CLU_002753_3_3_1; -.
DR   InParanoid; W5ND92; -.
DR   OMA; EIDITHD; -.
DR   Proteomes; UP000018468; Linkage group LG7.
DR   Bgee; ENSLOCG00000015115; Expressed in intestine.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled 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:0048731; P:system development; IEA:UniProt.
DR   CDD; cd15997; 7tmB2_GPR112; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR001759; Pentraxin-related.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR12011:SF277; ADHESION G-PROTEIN COUPLED RECEPTOR G4; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS51828; PTX_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1254
FT                   /note="G-protein coupled receptors family 2 profile 2
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004867591"
FT   TRANSMEM        881..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        919..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        954..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        989..1010
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1041..1067
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1088..1110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1116..1137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          882..1139
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          1166..1206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1166..1204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1254 AA;  138856 MW;  3717CBE75D026037 CRC64;
     SIMQPSSCKV LLCCWVLSTV FILRSGAPSL RGQKVVLFGR QCSYWELRGS VSLPALDEFT
     VCVDLCRKIN TRQWTAFTYN RPPQRLSEGA PELGLAGHGQ ALRLWLFGRA LDAPVDLRPF
     AWHSVCLAWS GVEQKVWLYV NGSGVFSAAV PDRRPLAPHG TLTLGVAHGL IGGEIVTEDG
     NNLIGEIYFF RMWDKQRSAQ QVSSQICAEG NVIRWTSEYW HNHSCSPVPD LSLPCASSFY
     SINMSIYIMR RDGQSADETI AKDLVCLWLT TYFPANITVL AIAVFSLQQG WEITFPKMQI
     VITAPASYGC FVSVKVIPSS EVLLTKEEVT RLLRGSVAHV ADSCCVVLPL HLLLCSCVLT
     ASRPSTPTTQ DTTMSVSTAV MSTSTPVCGA QKWTSVCVKV ENTKQSEAKA SHFTAEAKVQ
     KGFKLTFYTV SLNATLKDSS DNPEPFIYEW LLKILPGDEM TAFNLNASLA PVRQTRFQLQ
     VNSTANVNDT KTQIEHLLQK NYTNGTGSVE PEPNSINVYP IEPGRCPEQT QLMHQGQYLW
     PETQARFTAK LQCERDPENQ ATRNCMVNAL TNRAQWDKPD LMSCPTLHKT IADLSNITVT
     ANNSEDLAEL IKNLTSDQLF LSHNELIIVF SKMAEILDAG SVTPPLGQTI IDILNKLLGT
     ESNLQPFTND ILNVMESLGN RIAFPGNLFS LTSPNLALSV VGVDPRNFSG LAFGVSSFSQ
     GVNPQLFLQV FINQGPSSHT IAFISLPSAL ENHFPQHTEL ARSRVQFQFY GKTELFQDSM
     KEKSLLTYVI SGSVTNATIR NLRDPVTVTL HHLKPNRLGQ QVQCVFWDLQ KNGGQGGWSP
     EGCEVYGTSV NHTTCVCDHL THFGVLLVPS RSPVNSVDNR ILTLITYVGC GLSALFLGIS
     LLTYTAFEKL RRDYPSKILM NLSAALLGLN LVFLVDSWLA SFNRRGLCIS VAVILHYFLL
     ASFTWMGLEA VHMYFALVKV FNIYVPCYIL KFCSAGWGIP LLVIALVLAI NKDAYGSGLY
     AKSLSPSEDS EELFCWVQSD VAFYVSVVAF FLLVLLCNVA VFVVVLLQIR NVKAKQPAGC
     RGGLLHDLKS VASITFLLGL TWALAFLAWG PARVPLLYLF SIFNSLQGFF IFVFHCLMKD
     SVRKQWRIHL CCGRFRLATT SEWSQSGTKS REKQLAHSPS VKSAKSDKSN STSSTSNESD
     SGGRLVSTPD LVYENTLTVP QAHSPSFHDV LRVGPREMEG TYQVCSWLPR ERSY
//
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