GR101_LYMST
ID GR101_LYMST Reviewed; 1115 AA.
AC P46023;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=G-protein coupled receptor GRL101;
DE Flags: Precursor;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=CNS;
RX PubMed=8197140; DOI=10.1073/pnas.91.11.4816;
RA Tensen C.P., van Kesteren E.R., Planta R.J., Cox K.J.A., Burke J.F.,
RA van Heerikhuizen H., Vreugdenhil E.;
RT "A G protein-coupled receptor with low density lipoprotein-binding motifs
RT suggests a role for lipoproteins in G-linked signal transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4816-4820(1994).
CC -!- FUNCTION: Might directly transduce signals carried by large
CC extracellular lipoprotein complexes into neuronal events.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in a small number of
CC neurons within the central nervous system and to a lesser extent in the
CC heart.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z23104; CAA80651.1; -; mRNA.
DR PIR; S40241; S40241.
DR AlphaFoldDB; P46023; -.
DR SMR; P46023; -.
DR PRIDE; P46023; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 10.
DR Gene3D; 3.80.10.10; -; 1.
DR Gene3D; 4.10.400.10; -; 12.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 12.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF57424; SSF57424; 9.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS01209; LDLRA_1; 7.
DR PROSITE; PS50068; LDLRA_2; 11.
DR PROSITE; PS51450; LRR; 6.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Leucine-rich repeat; Membrane; Receptor; Repeat; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1115
FT /note="G-protein coupled receptor GRL101"
FT /id="PRO_0000012791"
FT TOPO_DOM 25..767
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..857
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..878
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 879..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 888..908
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 909..941
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..962
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 963..988
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 989..1009
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1010..1017
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1018..1038
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1039..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..79
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 77..115
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 116..155
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 156..196
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 195..232
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 231..269
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 272..318
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 320..363
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 365..403
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 404..442
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 444..485
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 486..525
FT /note="LDL-receptor class A 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 518..562
FT /note="LRRNT"
FT REPEAT 584..605
FT /note="LRR 1"
FT REPEAT 608..629
FT /note="LRR 2"
FT REPEAT 632..653
FT /note="LRR 3"
FT REPEAT 656..677
FT /note="LRR 4"
FT REPEAT 680..701
FT /note="LRR 5"
FT REPEAT 704..725
FT /note="LRR 6"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..53
FT /evidence="ECO:0000250"
FT DISULFID 46..66
FT /evidence="ECO:0000250"
FT DISULFID 60..77
FT /evidence="ECO:0000250"
FT DISULFID 79..91
FT /evidence="ECO:0000250"
FT DISULFID 86..104
FT /evidence="ECO:0000250"
FT DISULFID 98..113
FT /evidence="ECO:0000250"
FT DISULFID 118..131
FT /evidence="ECO:0000250"
FT DISULFID 138..153
FT /evidence="ECO:0000250"
FT DISULFID 158..170
FT /evidence="ECO:0000250"
FT DISULFID 165..183
FT /evidence="ECO:0000250"
FT DISULFID 177..194
FT /evidence="ECO:0000250"
FT DISULFID 202..220
FT /evidence="ECO:0000250"
FT DISULFID 214..230
FT /evidence="ECO:0000250"
FT DISULFID 233..245
FT /evidence="ECO:0000250"
FT DISULFID 240..258
FT /evidence="ECO:0000250"
FT DISULFID 252..267
FT /evidence="ECO:0000250"
FT DISULFID 274..291
FT /evidence="ECO:0000250"
FT DISULFID 282..304
FT /evidence="ECO:0000250"
FT DISULFID 298..316
FT /evidence="ECO:0000250"
FT DISULFID 322..339
FT /evidence="ECO:0000250"
FT DISULFID 334..352
FT /evidence="ECO:0000250"
FT DISULFID 346..361
FT /evidence="ECO:0000250"
FT DISULFID 367..379
FT /evidence="ECO:0000250"
FT DISULFID 374..392
FT /evidence="ECO:0000250"
FT DISULFID 386..401
FT /evidence="ECO:0000250"
FT DISULFID 406..418
FT /evidence="ECO:0000250"
FT DISULFID 413..431
FT /evidence="ECO:0000250"
FT DISULFID 425..440
FT /evidence="ECO:0000250"
FT DISULFID 446..458
FT /evidence="ECO:0000250"
FT DISULFID 453..474
FT /evidence="ECO:0000250"
FT DISULFID 465..483
FT /evidence="ECO:0000250"
FT DISULFID 488..500
FT /evidence="ECO:0000250"
FT DISULFID 495..513
FT /evidence="ECO:0000250"
FT DISULFID 507..523
FT /evidence="ECO:0000250"
SQ SEQUENCE 1115 AA; 125866 MW; E9BB01297ECE356C CRC64;
MATMSGTTIV CLIYLTTMLG NSQGVNLKIE SPSPPTLCSV EGTFHCDDGM LQCVLMGSKC
DGVSDCENGM DESVETCGCL QSEFQCNHTT CIDKILRCDR NDDCSNGLDE RECDIYICPL
GTHVKWHNHF CVPRDKQCDF LDDCGDNSDE KICERRECVA TEFKCNNSQC VAFGNLCDGL
VDCVDGSDED QVACDSDKYF QCAEGSLIKK EFVCDGWVDC KLTFADELNC KLCDEDDFRC
SDTRCIQKSN VCDGYCDCKT CDDEEVCANN TYGCPMDTKY MCRSIYGEPR CIDKDNVCNM
INDCRDGNVG TDEYYCSNDS ECKNFQAAMG FFYCPEERCL AKHLYCDLHP DCINGEDEQS
CLAPPKCSQD EFQCHHGKCI PISKRCDSVH DCVDWSDEMN CENHQCAANM KSCLSGHCIE
EHKWCNFHRE CPDGSDEKDC DPRPVCEANQ FRCKNGQCID PLQVCVKGDK YDGCADQSHL
INCSQHICLE GQFRCRKSFC INQTKVCDGT VDCLQGMWDE NNCRYWCPHG QAICQCEGVT
MDCTGQKLKE MPVQQMEEDL SKLMIGDNLL NLTSTTFSAT YYDKVTYLDL SRNHLTEIPI
YSFQNMWKLT HLNLADNNIT SLKNGSLLGL SNLKQLHING NKIETIEEDT FSSMIHLTVL
DLSNQRLTHV YKNMFKGLKQ ITVLNISRNQ INSIDNGAFN NLANVRLIDL SGNVIKDIGQ
KVFMGLPRLV ELKTDSYRFC CLAPEGVKCS PKQDEFSSCE DLMSNHVLRV SIWVLGVIAL
VGNFVVIFWR VRDFRGGKVH SFLITNLAIG DFLMGVYLLI IATADTYYRG VYISHDENWK
QSGLCQFAGF VSTFSSELSV LTLSTITLDR LICILFPLRR TRLGLRQAII VMSCIWVLVF
LLAVLPLLGF SYFENFYGRS GVCLALHVTP DRRPGWEYSV GVFILLNLLS FVLIASSYLW
MFSVAKKTRS AVRTAESKND NAMARRMTLI VMTDFCCWVP IIVLGFVSLA GARADDQVYA
WIAVFVLPLN SATNPVIYTL STAPFLGNVR KRANRFRKSF IHSFTGDTKH SYVDDGTTHS
YCEKKSPYRQ LELKRLRSLN SSPPMYYNTE LHSDS
