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RAMP3_PIG
ID   RAMP3_PIG               Reviewed;         151 AA.
AC   Q7YS88; Q7YS89; Q867B8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Receptor activity-modifying protein 3;
DE   Flags: Precursor;
GN   Name=RAMP3;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=12759187; DOI=10.1016/s0167-4781(03)00051-4;
RA   Rival-Gervier S., Thepot D., Jolivet G., Houdebine L.-M.;
RT   "Pig whey acidic protein gene is surrounded by two ubiquitously expressed
RT   genes.";
RL   Biochim. Biophys. Acta 1627:7-14(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kikumoto K., Katafuchi T., Minamino N.;
RT   "Specificity of porcine calcitonin receptor and calcitonin receptor-like
RT   receptor in the presence of receptor-activity-modifying proteins.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in cardioprotection by reducing cardiac
CC       hypertrophy and perivascular fibrosis in a GPER1-dependent manner.
CC       Transports the calcitonin gene-related peptide type 1 receptor (CALCRL)
CC       and GPER1 to the plasma membrane. Acts as a receptor for adrenomedullin
CC       (AM) together with CALCRL (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of CALCRL and RAMP3. Interacts with GPER1.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}. Note=Moves from intracellular
CC       puncta to the plasma membrane in a RAMP3-dependent manner.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RAMP family. {ECO:0000305}.
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DR   EMBL; AY236155; AAP37948.1; -; Genomic_DNA.
DR   EMBL; AY236153; AAP37948.1; JOINED; Genomic_DNA.
DR   EMBL; AY236154; AAP37948.1; JOINED; Genomic_DNA.
DR   EMBL; AY236156; AAP37949.1; -; mRNA.
DR   EMBL; AB090165; BAC54963.1; -; mRNA.
DR   RefSeq; NP_999254.1; NM_214089.1.
DR   AlphaFoldDB; Q7YS88; -.
DR   SMR; Q7YS88; -.
DR   PRIDE; Q7YS88; -.
DR   GeneID; 397163; -.
DR   KEGG; ssc:397163; -.
DR   CTD; 10268; -.
DR   InParanoid; Q7YS88; -.
DR   OrthoDB; 1432933at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IPI:UniProtKB.
DR   GO; GO:1990410; P:adrenomedullin receptor signaling pathway; IPI:UniProtKB.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR   GO; GO:0086103; P:G protein-coupled receptor signaling pathway involved in heart process; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
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   Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..151
FT                   /note="Receptor activity-modifying protein 3"
FT                   /id="PRO_0000250475"
FT   TOPO_DOM        31..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..107
FT                   /evidence="ECO:0000250"
FT   CONFLICT        103
FT                   /note="H -> Y (in Ref. 2; BAC54963)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  17368 MW;  8486F8BE564AFCF4 CRC64;
     MEATAPRRRH LLPLLLLLLL LCGECPPVSG CNEKRMLAML PRCGKTFAEM MKKVEVWKWC
     NLSEFIVYYE SFTNCTEVET NVVGCYWPNP LAQSFITGVH RRHFHNCSVD RQQWQDPPDE
     ILIPLIVVPI LLTLAMTGLV VWRSKRAAQV V
 
 
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