RAMP2_MOUSE
ID RAMP2_MOUSE Reviewed; 189 AA.
AC Q9WUP0; Q6IS25;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Receptor activity-modifying protein 2;
DE Flags: Precursor;
GN Name=Ramp2;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Jaw, and Limb;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000269|PubMed:10854696}.
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 -!- TISSUE SPECIFICITY: Ubiquitous. Expressed predominantly in embryonic
CC brain, lung and gut and in adult heart, lung, skeletal muscle and
CC brain. {ECO:0000269|PubMed:10777702, ECO:0000269|PubMed:10854696}.
CC -!- SIMILARITY: Belongs to the RAMP family. {ECO:0000305}.
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DR EMBL; AF146523; AAD35019.1; -; mRNA.
DR EMBL; AJ250490; CAB59512.1; -; mRNA.
DR EMBL; AF209906; AAF21038.1; -; mRNA.
DR EMBL; AK003810; BAB23009.1; -; mRNA.
DR EMBL; BC069992; AAH69992.1; -; mRNA.
DR CCDS; CCDS25457.1; -.
DR PIR; JC7262; JC7262.
DR RefSeq; NP_062317.1; NM_019444.2.
DR AlphaFoldDB; Q9WUP0; -.
DR SMR; Q9WUP0; -.
DR ComplexPortal; CPX-3150; Adrenomedullin receptor AM1 complex.
DR ComplexPortal; CPX-3236; Amylin receptor 2 complex.
DR STRING; 10090.ENSMUSP00000122072; -.
DR GuidetoPHARMACOLOGY; 52; -.
DR GlyGen; Q9WUP0; 4 sites.
DR PhosphoSitePlus; Q9WUP0; -.
DR MaxQB; Q9WUP0; -.
DR PaxDb; Q9WUP0; -.
DR PeptideAtlas; Q9WUP0; -.
DR PRIDE; Q9WUP0; -.
DR ProteomicsDB; 255092; -.
DR Antibodypedia; 29403; 298 antibodies from 32 providers.
DR DNASU; 54409; -.
DR Ensembl; ENSMUST00000129680; ENSMUSP00000122072; ENSMUSG00000001240.
DR GeneID; 54409; -.
DR KEGG; mmu:54409; -.
DR UCSC; uc007lny.1; mouse.
DR CTD; 10266; -.
DR MGI; MGI:1859650; Ramp2.
DR VEuPathDB; HostDB:ENSMUSG00000001240; -.
DR eggNOG; ENOG502S5WC; Eukaryota.
DR GeneTree; ENSGT00940000160264; -.
DR InParanoid; Q9WUP0; -.
DR OMA; CDWAVIS; -.
DR OrthoDB; 1482534at2759; -.
DR PhylomeDB; Q9WUP0; -.
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; 54409; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Ramp2; mouse.
DR PRO; PR:Q9WUP0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WUP0; protein.
DR Bgee; ENSMUSG00000001240; Expressed in right lung and 241 other tissues.
DR ExpressionAtlas; Q9WUP0; baseline and differential.
DR Genevisible; Q9WUP0; MM.
DR GO; GO:1903143; C:adrenomedullin receptor complex; ISO:MGI.
DR GO; GO:0150057; C:amylin receptor complex 2; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR GO; GO:1990409; F:adrenomedullin binding; 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:0034333; P:adherens junction assembly; IMP:UniProtKB.
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:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0070831; P:basement membrane assembly; IMP:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IPI:MGI.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IMP:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; IMP: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; IMP:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; IMP:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..189
FT /note="Receptor activity-modifying protein 2"
FT /id="PRO_0000030173"
FT TOPO_DOM 45..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 49..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..113
FT /evidence="ECO:0000250"
FT DISULFID 98..145
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="P -> T (in Ref. 5; AAH69992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21017 MW; CEE51D9FE9751F10 CRC64;
MAPLRVERAP GGSRLGVTRA QRPTALCLPP LLLLLLLLLG AVSASPESLN QSLPESQNQS
HPTEDSLVSK GKMEDYETHV LPCWYEYKSC MDSVKDWCNW TLISRHYSDL QNCLEYNADK
FGLGFPNPLA ENIILEAHLI HFANCSLVQP TFSDPPEDVL LAMIIAPICL IPFLVTLVVW
RSKDSDAQA
