ID   RAMP2_CAVPO             Reviewed;         157 AA.
AC   Q8R4C5;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Receptor activity-modifying protein 2;
DE   Flags: Precursor;
GN   Name=RAMP2;
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       adrenomedullin (AM) together with CALCRL (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of CALCRL and RAMP2.
CC       {ECO:0000250|UniProtKB:O60895}.
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; AF484220; AAL91559.1; -; mRNA.
DR   RefSeq; NP_001166481.1; NM_001173010.1.
DR   AlphaFoldDB; Q8R4C5; -.
DR   SMR; Q8R4C5; -.
DR   STRING; 10141.ENSCPOP00000017305; -.
DR   GeneID; 100135611; -.
DR   KEGG; cpoc:100135611; -.
DR   CTD; 10266; -.
DR   eggNOG; ENOG502S5WC; Eukaryota.
DR   InParanoid; Q8R4C5; -.
DR   OrthoDB; 1482534at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR   GO; GO:0015026; F:coreceptor activity; ISS:UniProtKB.
DR   GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0070831; P:basement membrane assembly; ISS:UniProtKB.
DR   GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0043116; P:negative regulation of vascular permeability; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR   GO; GO:0097084; P:vascular associated smooth muscle cell development; ISS:UniProtKB.
DR   GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
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; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000305"
FT   CHAIN           25..157
FT                   /note="Receptor activity-modifying protein 2"
FT                   /id="PRO_0000030171"
FT   TOPO_DOM        25..127
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..113
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  17749 MW;  FCFA49570000DB19 CRC64;
     MAARLRPLLA LLALAALCPQ ETLAQPLPTT DTWKSEGQVV DSYEASAQLC WADYREHMDL
     LEKDWCNWTV ISRPYSALRD CLEVEAEVFS LGFPNPLAER VIFETHQLHF SNCSLEQPTL
     CDPPEDVLLA MIIAPICLIP FFVTLVVWRS KGTELKT