ID RXFP1_PONAB Reviewed; 757 AA.
AC Q5R5V8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 22-FEB-2023, entry version 91.
DE RecName: Full=Relaxin receptor 1;
DE AltName: Full=Relaxin family peptide receptor 1;
GN Name=RXFP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for relaxins. The activity of this receptor is
CC mediated by G proteins leading to stimulation of adenylate cyclase and
CC an increase of cAMP. Binding of the ligand may also activate a tyrosine
CC kinase pathway that inhibits the activity of a phosphodiesterase that
CC degrades cAMP (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with C1QTNF8. {ECO:0000250|UniProtKB:Q9HBX9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR860744; CAH92858.1; -; mRNA.
DR RefSeq; NP_001126672.1; NM_001133200.1.
DR AlphaFoldDB; Q5R5V8; -.
DR SMR; Q5R5V8; -.
DR STRING; 9601.ENSPPYP00000016938; -.
DR GlyCosmos; Q5R5V8; 6 sites, No reported glycans.
DR GeneID; 100173672; -.
DR KEGG; pon:100173672; -.
DR CTD; 59350; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; Q5R5V8; -.
DR OrthoDB; 2913881at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15965; 7tmA_RXFP1_LGR7; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR008112; Relaxin_rcpt.
DR PANTHER; PTHR24372; GLYCOPROTEIN HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24372:SF68; RELAXIN RECEPTOR 1; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF13855; LRR_8; 2.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01739; RELAXINR.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 9.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS51450; LRR; 10.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Leucine-rich repeat; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..757
FT /note="Relaxin receptor 1"
FT /id="PRO_0000312668"
FT TOPO_DOM 1..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..577
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..660
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..63
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 91..127
FT /note="LRRNT"
FT REPEAT 151..172
FT /note="LRR 1"
FT REPEAT 175..196
FT /note="LRR 2"
FT REPEAT 199..220
FT /note="LRR 3"
FT REPEAT 223..244
FT /note="LRR 4"
FT REPEAT 248..269
FT /note="LRR 5"
FT REPEAT 272..293
FT /note="LRR 6"
FT REPEAT 296..317
FT /note="LRR 7"
FT REPEAT 320..341
FT /note="LRR 8"
FT REPEAT 344..365
FT /note="LRR 9"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..40
FT /evidence="ECO:0000250"
FT DISULFID 34..53
FT /evidence="ECO:0000250"
FT DISULFID 47..62
FT /evidence="ECO:0000250"
FT DISULFID 485..563
FT /evidence="ECO:0000250"
SQ SEQUENCE 757 AA; 86703 MW; 140A8E16F8A6ACDB CRC64;
MTSGSVFFYI LIIGKYFSHG GGQDVKCSLG YFPCGNITKC LPQLLHCNGV DDCGNQADED
NCGDNNGWSL QFDKYFASYY KMTSQYPFEA ETPECLVGSV PVQCLCRGLE LDCDETNLRA
VPSVSSNVTA MSLQWNLIRK LPPDCFKNYH DLQKLYLQNN KITSISIYAF RGLNSLTKLY
LSHNRITFLK PGVFEDLHRL EWLIIEDNHL SRISPPTFYG LNSLILLVLM NNVLTRLPDK
PLCQHMPRLH WLDLEGNHIH NLRNLTLISC SNLTVLVMGK NKINHLNENT FAPLQKLDEL
DLGSNKIENL PPLIFKDLKE LSQLNLSYNP IQKIQANQFD YLVKLKSLSL EGIEISNIQQ
RMFRPLMNLS HIYFKKFQYC GYAPHVRSGK PNTDGISSLE NLLASIIQRV FVWVVSAVTC
FGNVFVICMR PYIRSENKLY AMSIISLCCA DCLMGIYLFV IGGFDLKFRG EYNKHAQLWM
ESTHCQLVGS LAILSTEVSV LLLTFLTLEK YICIVYPFRC VRPGKCRTIT VLILIWITGF
IVAFIPLSNK EFFKNYYGTN GVCFPLHSED TESIGAQVYS VAIFLGINLA AFIIIVFSYG
SMFYSVHQSA ITATEIRNQV KKEMILAKRF FFIVFTDALC WIPIFVVKFL SLLQVEIPGT
ITSWVVIFIL PINSALNPIL YTLTTRPFKE MIHRFWYNYR QRKSMDSKGQ KTYAPSFIWV
EMWPLQEMPP ELMKPGLFTY PCEMSLISQS TRLNSYS
//
