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RAMP3_MOUSE
ID   RAMP3_MOUSE             Reviewed;         147 AA.
AC   Q9WUP1; Q5SWP4;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Receptor activity-modifying protein 3;
DE   Flags: Precursor;
GN   Name=Ramp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Derst C., Preisig-Mueller R., Gerhardus J., Daut J.;
RT   "Cloning and sequencing of mouse CGRP/adrenomedullin receptor subunits.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10854696; DOI=10.1016/s0303-7207(00)00212-4;
RA   Husmann K., Sexton P.M., Fischer J.A., Born W.;
RT   "Mouse receptor-activity-modifying proteins 1, -2 and -3: amino acid
RT   sequence, expression and function.";
RL   Mol. Cell. Endocrinol. 162:35-43(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=10777702; DOI=10.1006/bbrc.2000.2606;
RA   Ono Y., Okano I., Kojima M., Okada K., Kangawa K.;
RT   "Decreased gene expression of adrenomedullin receptor in mouse lungs during
RT   sepsis.";
RL   Biochem. Biophys. Res. Commun. 271:197-202(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23674134; DOI=10.1530/jme-13-0021;
RA   Lenhart P.M., Broselid S., Barrick C.J., Leeb-Lundberg L.M., Caron K.M.;
RT   "G-protein-coupled receptor 30 interacts with receptor activity-modifying
RT   protein 3 and confers sex-dependent cardioprotection.";
RL   J. Mol. Endocrinol. 51:191-202(2013).
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       to the plasma membrane. Acts as a receptor for adrenomedullin (AM)
CC       together with CALCRL. {ECO:0000269|PubMed:10854696,
CC       ECO:0000269|PubMed:23674134}.
CC   -!- SUBUNIT: Interacts with GPER1 (By similarity). Heterodimer of CALCRL
CC       and RAMP3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23674134};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:23674134}.
CC       Membrane {ECO:0000250}; Single-pass type I membrane protein
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the testis, embryonic
CC       and adult brain and in kidney. {ECO:0000269|PubMed:10777702,
CC       ECO:0000269|PubMed:10854696}.
CC   -!- SIMILARITY: Belongs to the RAMP family. {ECO:0000305}.
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DR   EMBL; AF146524; AAD35020.1; -; mRNA.
DR   EMBL; AJ250491; CAB59513.1; -; mRNA.
DR   EMBL; AF209907; AAF21039.1; -; mRNA.
DR   EMBL; AL603787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC024765; AAH24765.1; -; mRNA.
DR   CCDS; CCDS24425.1; -.
DR   PIR; JC7263; JC7263.
DR   RefSeq; NP_062384.1; NM_019511.3.
DR   AlphaFoldDB; Q9WUP1; -.
DR   SMR; Q9WUP1; -.
DR   ComplexPortal; CPX-3151; Adrenomedullin receptor AM2 complex.
DR   ComplexPortal; CPX-3237; Amylin receptor 3 complex.
DR   STRING; 10090.ENSMUSP00000047518; -.
DR   GuidetoPHARMACOLOGY; 53; -.
DR   GlyGen; Q9WUP1; 4 sites.
DR   PhosphoSitePlus; Q9WUP1; -.
DR   PaxDb; Q9WUP1; -.
DR   PRIDE; Q9WUP1; -.
DR   ProteomicsDB; 253170; -.
DR   Antibodypedia; 27450; 210 antibodies from 32 providers.
DR   DNASU; 56089; -.
DR   Ensembl; ENSMUST00000045374; ENSMUSP00000047518; ENSMUSG00000041046.
DR   GeneID; 56089; -.
DR   KEGG; mmu:56089; -.
DR   UCSC; uc007hzd.1; mouse.
DR   CTD; 10268; -.
DR   MGI; MGI:1860292; Ramp3.
DR   VEuPathDB; HostDB:ENSMUSG00000041046; -.
DR   eggNOG; ENOG502S3C2; Eukaryota.
DR   GeneTree; ENSGT00940000161026; -.
DR   HOGENOM; CLU_116349_3_1_1; -.
DR   InParanoid; Q9WUP1; -.
DR   OMA; FTNCTEE; -.
DR   OrthoDB; 1432933at2759; -.
DR   PhylomeDB; Q9WUP1; -.
DR   TreeFam; TF333286; -.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-419812; Calcitonin-like ligand receptors.
DR   BioGRID-ORCS; 56089; 3 hits in 72 CRISPR screens.
DR   PRO; PR:Q9WUP1; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9WUP1; protein.
DR   Bgee; ENSMUSG00000041046; Expressed in medial dorsal nucleus of thalamus and 127 other tissues.
DR   Genevisible; Q9WUP1; MM.
DR   GO; GO:1903143; C:adrenomedullin receptor complex; ISO:MGI.
DR   GO; GO:0150058; C:amylin receptor complex 3; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005764; C:lysosome; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0001605; F:adrenomedullin receptor activity; ISO:MGI.
DR   GO; GO:0097643; F:amylin receptor activity; ISO:MGI.
DR   GO; GO:0015026; F:coreceptor activity; IDA:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:1990410; P:adrenomedullin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0097647; P:amylin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR   GO; GO:0038041; P:cross-receptor inhibition within G protein-coupled receptor heterodimer; ISO:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IPI:MGI.
DR   GO; GO:0086103; P:G protein-coupled receptor signaling pathway involved in heart process; IMP:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR   GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0015031; P:protein transport; ISO:MGI.
DR   GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR   GO; GO:1904645; P:response to amyloid-beta; ISO:MGI.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..147
FT                   /note="Receptor activity-modifying protein 3"
FT                   /id="PRO_0000030177"
FT   TOPO_DOM        23..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..103
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   147 AA;  16779 MW;  359EE741034C34E8 CRC64;
     MKTPAQRLHL LPLLLLLCGE CAQVCGCNET GMLERLPRCG KAFADMMQKV AVWKWCNLSE
     FIVYYESFTN CTEMETNIMG CYWPNPLAQS FITGIHRQFF SNCTVDRTHW EDPPDEVLIP
     LIAVPVVLTV AMAGLVVWRS KHTDRLL
 
 
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