ID A0A2K6SCQ0_SAIBB Unreviewed; 1011 AA.
AC A0A2K6SCQ0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Adhesion G protein-coupled receptor G6 {ECO:0000313|Ensembl:ENSSBOP00000005156.1};
GN Name=ADGRG6 {ECO:0000313|Ensembl:ENSSBOP00000005156.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000005156.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000005156.1}
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}.
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:PRU00059}.
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DR AlphaFoldDB; A0A2K6SCQ0; -.
DR Ensembl; ENSSBOT00000021735.1; ENSSBOP00000005156.1; ENSSBOG00000019284.1.
DR GeneTree; ENSGT00940000155621; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd00041; CUB; 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 Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001759; Pentraxin-related.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR12011:SF290; ADHESION G-PROTEIN COUPLED RECEPTOR G6; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00354; Pentaxin; 1.
DR SMART; SM00042; CUB; 1.
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 SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS01180; CUB; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00059};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Signal {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..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..1011
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014417238"
FT TRANSMEM 865..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 900..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 927..949
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 969..990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..148
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 863..1011
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DISULFID 93..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 1011 AA; 112940 MW; EE8131D2073F113F CRC64;
MFHSDRMWSC HWKWKPNPLL FLLALYIMCV PRSVSGCANC RVVLSNPSGT FTSPCYPNDY
PNSQACMWTL RAPTGYIIQI TFNDFDIEEA PNCIYDSLSL DNGESQTKFC GATAKGLSFN
SSVNEMHVSF SSDFSIQKKG FNASYIRVAV SLRNQKVILP QTSDAYQVSI AKSVSIPELS
AFTLCFEATK VGHEDNDWTA FSYSNASFTQ LLSFGKAKSG YFLSISDSKC LLNNALPIKE
KEDIFAESFE QLCLVWNNSL GSVGVNFKRN YEIVQCDSTI SKVIPGNGKL FLGSNQNEIA
SLKGDIYNFR LWNFTMNSKI LSNLSCNVKG NVVDWQNDFW NIPNLALKAE SNLSCGSYLI
PLPAAELASC ADLGTLCQAT VNSPSTTPRT VTTNMPVTNR IDKQMNDGIL YRISVVIQNI
LRHPEVKIQS KVAEWLNSTF QNWNYTVYVI NISFHLSSGE DKIKVKRSTE NDSRLVLWAL
LVYNATNNTN LEGKIIQQKL LKSNESLDEG LRLHRVNVRQ LYLCPAVEEP EGFKWPSIVP
SEYTLPCPEK PGFNVTRICF YNASNFSETY WGPVDISNCL KEANEVATQI LNYTADGQNL
TSANIIDIVE QVKRIVNKEE NIDITLGSTL MSIFSNILSS SDSDLLESSS EALKTIDELA
FKIDLNNISH VNITTQNLAL GVSSLLPGTN AISNFSIGLP SNNESYFQMD FESGQVDPLA
SVILPPNLLE NLSQEDAALV RRAQFTFFNK TGLFQDVGPQ RNPLVSYVMA CSIGNITIQN
LKDPVQIKIK HMSTQEVHHP ICAFWDLNKN KSFGGWNTSG CVAHRDSDAS ETVCLCNHFT
HFGVLMDLSR STSQLDARNT KVLTFITYIG CGISAIFSAV TLLTYVAFEK LRRDYPSKIL
MNLSTALLFL NLLFLLDGWI TSFNVDGLCI AIAALLHFFL LATFTWMGLE AIHMYIALVK
VFNTYIRRYI LKFCIIGWGL PALVVSVILV SRNKNEVYGK ESYGKEKSDE L
//
