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