ID   RAMP1_CAVPO             Reviewed;         148 AA.
AC   Q8R4C6;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Receptor activity-modifying protein 1;
DE   Flags: Precursor;
GN   Name=RAMP1;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Derst C., Preisig-Mueller R., Daut J.;
RT   "Cloning and sequencing of guinea pig amylin, calcitonin, CGRP and
RT   adrenomedullin receptor subunits.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transports the calcitonin gene-related peptide type 1
CC       receptor (CALCRL) to the plasma membrane. Acts as a receptor for
CC       calcitonin-gene-related peptide (CGRP) together with CALCRL (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of CALCRL and RAMP1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RAMP family. {ECO:0000305}.
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DR   EMBL; AF484219; AAL91558.1; -; mRNA.
DR   RefSeq; NP_001166480.1; NM_001173009.1.
DR   AlphaFoldDB; Q8R4C6; -.
DR   SMR; Q8R4C6; -.
DR   STRING; 10141.ENSCPOP00000020178; -.
DR   Ensembl; ENSCPOT00000020782; ENSCPOP00000020178; ENSCPOG00000026974.
DR   GeneID; 100135610; -.
DR   KEGG; cpoc:100135610; -.
DR   CTD; 10267; -.
DR   eggNOG; ENOG502S0TC; Eukaryota.
DR   GeneTree; ENSGT00940000159224; -.
DR   HOGENOM; CLU_116349_3_0_1; -.
DR   InParanoid; Q8R4C6; -.
DR   OMA; CYWPNRM; -.
DR   OrthoDB; 1432933at2759; -.
DR   TreeFam; TF333286; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000026974; Expressed in hypothalamus and 13 other tissues.
DR   GO; GO:0150056; C:amylin receptor complex 1; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:1990406; C:CGRP receptor complex; IEA:Ensembl.
DR   GO; GO:0097643; F:amylin receptor activity; IEA:Ensembl.
DR   GO; GO:1990407; F:calcitonin gene-related peptide binding; IEA:Ensembl.
DR   GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IEA:Ensembl.
DR   GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0097647; P:amylin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:1990408; P:calcitonin gene-related peptide receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0060050; P:positive regulation of protein glycosylation; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 1.10.150.510; -; 1.
DR   InterPro; IPR006985; RAMP.
DR   InterPro; IPR038126; RAMP_sf.
DR   PANTHER; PTHR14076; PTHR14076; 1.
DR   Pfam; PF04901; RAMP; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Membrane; Receptor; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..148
FT                   /note="Receptor activity-modifying protein 1"
FT                   /id="PRO_0000030167"
FT   TOPO_DOM        27..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..104
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   148 AA;  16942 MW;  6CE8486CD5B44856 CRC64;
     MVRVLRGLPW RGLWLLLAHQ LFLVTACQDA HYGTLMQELC LSRFQKDMEA MERTLWCDWG
     KTIGSYGELT DCTRNLAERL GCFWPNVEVD RFFVAVHRHY FRSCPASGRA LGDPPSTILC
     PFVVLPITVT LLVTALVVWR SKRAESIV