位置:首页 > 蛋白库 > RAMP3_HUMAN
RAMP3_HUMAN
ID   RAMP3_HUMAN             Reviewed;         148 AA.
AC   O60896; Q7Z2Y1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Receptor activity-modifying protein 3;
DE   AltName: Full=Calcitonin-receptor-like receptor activity-modifying protein 3;
DE            Short=CRLR activity-modifying protein 3;
DE   Flags: Precursor;
GN   Name=RAMP3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9620797; DOI=10.1038/30666;
RA   McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J., Thompson N.,
RA   Solari R., Lee M.G., Foord S.M.;
RT   "RAMPs regulate the transport and ligand specificity of the calcitonin-
RT   receptor-like receptor.";
RL   Nature 393:333-339(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-33.
RC   TISSUE=Lung, and PNS;
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   [5]
RP   FUNCTION, INTERACTION WITH GPER1, 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       and GPER1 to the plasma membrane. Acts as a receptor for adrenomedullin
CC       (AM) together with CALCRL. {ECO:0000269|PubMed:23674134,
CC       ECO:0000269|PubMed:9620797}.
CC   -!- SUBUNIT: Heterodimer of CALCRL and RAMP3 (By similarity). Interacts
CC       with GPER1. {ECO:0000250, ECO:0000269|PubMed:23674134}.
CC   -!- INTERACTION:
CC       O60896; A8MQ03: CYSRT1; NbExp=6; IntAct=EBI-720447, EBI-3867333;
CC       O60896; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-720447, EBI-11974251;
CC       O60896; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-720447, EBI-11987425;
CC       O60896; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-720447, EBI-3958099;
CC       O60896; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-720447, EBI-1043191;
CC       O60896; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-720447, EBI-945833;
CC       O60896; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-720447, EBI-22310682;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23674134};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:23674134}.
CC       Membrane {ECO:0000269|PubMed:23674134}; Single-pass type I membrane
CC       protein {ECO:0000269|PubMed:23674134}. Note=Moves from intracellular
CC       puncta to the plasma membrane in a RAMP3-dependent manner.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in lung, breast, immune system
CC       and fetal tissues. {ECO:0000269|PubMed:9620797}.
CC   -!- SIMILARITY: Belongs to the RAMP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ001016; CAA04474.1; -; mRNA.
DR   EMBL; AY265459; AAP23300.1; -; mRNA.
DR   EMBL; AC004844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC022304; AAH22304.1; -; mRNA.
DR   EMBL; BC053852; AAH53852.1; -; mRNA.
DR   CCDS; CCDS5503.1; -.
DR   RefSeq; NP_005847.1; NM_005856.2.
DR   PDB; 6UUS; EM; 2.40 A; E=24-148.
DR   PDB; 6UVA; EM; 2.30 A; E=24-148.
DR   PDB; 7TZF; EM; 2.40 A; E=24-148.
DR   PDBsum; 6UUS; -.
DR   PDBsum; 6UVA; -.
DR   PDBsum; 7TZF; -.
DR   AlphaFoldDB; O60896; -.
DR   SMR; O60896; -.
DR   BioGRID; 115559; 203.
DR   ComplexPortal; CPX-3148; Adrenomedullin receptor AM2 complex.
DR   ComplexPortal; CPX-3187; Amylin receptor 3 complex.
DR   CORUM; O60896; -.
DR   IntAct; O60896; 9.
DR   STRING; 9606.ENSP00000242249; -.
DR   BindingDB; O60896; -.
DR   ChEMBL; CHEMBL2111190; -.
DR   ChEMBL; CHEMBL2111191; -.
DR   DrugBank; DB01278; Pramlintide.
DR   DrugCentral; O60896; -.
DR   GuidetoPHARMACOLOGY; 53; -.
DR   TCDB; 8.A.127.1.3; the receptor activity-modifying protein (ramp) family.
DR   GlyGen; O60896; 4 sites.
DR   PhosphoSitePlus; O60896; -.
DR   BioMuta; RAMP3; -.
DR   jPOST; O60896; -.
DR   MassIVE; O60896; -.
DR   PaxDb; O60896; -.
DR   PeptideAtlas; O60896; -.
DR   PRIDE; O60896; -.
DR   ProteomicsDB; 49659; -.
DR   Antibodypedia; 27450; 210 antibodies from 32 providers.
DR   DNASU; 10268; -.
DR   Ensembl; ENST00000242249.8; ENSP00000242249.4; ENSG00000122679.8.
DR   Ensembl; ENST00000481345.1; ENSP00000419012.1; ENSG00000122679.8.
DR   GeneID; 10268; -.
DR   KEGG; hsa:10268; -.
DR   MANE-Select; ENST00000242249.8; ENSP00000242249.4; NM_005856.3; NP_005847.1.
DR   UCSC; uc003tnb.4; human.
DR   CTD; 10268; -.
DR   DisGeNET; 10268; -.
DR   GeneCards; RAMP3; -.
DR   HGNC; HGNC:9845; RAMP3.
DR   HPA; ENSG00000122679; Tissue enhanced (lung).
DR   MIM; 605155; gene.
DR   neXtProt; NX_O60896; -.
DR   OpenTargets; ENSG00000122679; -.
DR   PharmGKB; PA34204; -.
DR   VEuPathDB; HostDB:ENSG00000122679; -.
DR   eggNOG; ENOG502S3C2; Eukaryota.
DR   GeneTree; ENSGT00940000161026; -.
DR   InParanoid; O60896; -.
DR   OMA; FTNCTEE; -.
DR   OrthoDB; 1432933at2759; -.
DR   PhylomeDB; O60896; -.
DR   TreeFam; TF333286; -.
DR   PathwayCommons; O60896; -.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
DR   Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR   SignaLink; O60896; -.
DR   BioGRID-ORCS; 10268; 4 hits in 1068 CRISPR screens.
DR   ChiTaRS; RAMP3; human.
DR   GeneWiki; RAMP3; -.
DR   GenomeRNAi; 10268; -.
DR   Pharos; O60896; Tclin.
DR   PRO; PR:O60896; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; O60896; protein.
DR   Bgee; ENSG00000122679; Expressed in right lung and 139 other tissues.
DR   ExpressionAtlas; O60896; baseline and differential.
DR   Genevisible; O60896; HS.
DR   GO; GO:1903143; C:adrenomedullin receptor complex; IDA:UniProtKB.
DR   GO; GO:0150058; C:amylin receptor complex 3; IDA:ARUK-UCL.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR   GO; GO:0001605; F:adrenomedullin receptor activity; IPI:UniProtKB.
DR   GO; GO:0001540; F:amyloid-beta binding; IC:ARUK-UCL.
DR   GO; GO:0015026; F:coreceptor activity; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IGI:ARUK-UCL.
DR   GO; GO:1990410; P:adrenomedullin receptor signaling pathway; IPI:UniProtKB.
DR   GO; GO:0097647; P:amylin receptor signaling pathway; IGI:ARUK-UCL.
DR   GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; ISS: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; IPI:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:1905665; P:positive regulation of calcium ion import across plasma membrane; IGI:ARUK-UCL.
DR   GO; GO:0010942; P:positive regulation of cell death; IGI:ARUK-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IGI:ARUK-UCL.
DR   GO; GO:0010739; P:positive regulation of protein kinase A signaling; IGI:ARUK-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IGI:ARUK-UCL.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR   GO; GO:1904645; P:response to amyloid-beta; IGI:ARUK-UCL.
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   3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..148
FT                   /note="Receptor activity-modifying protein 3"
FT                   /id="PRO_0000030176"
FT   TOPO_DOM        24..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
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        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..104
FT                   /evidence="ECO:0000250"
FT   VARIANT         26
FT                   /note="G -> D (in dbSNP:rs10272187)"
FT                   /id="VAR_034437"
FT   VARIANT         33
FT                   /note="M -> L (in dbSNP:rs11550711)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_053628"
FT   VARIANT         56
FT                   /note="W -> R (in dbSNP:rs2074654)"
FT                   /id="VAR_024602"
FT   TURN            34..36
FT                   /evidence="ECO:0007829|PDB:6UUS"
FT   HELIX           37..47
FT                   /evidence="ECO:0007829|PDB:6UVA"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:6UVA"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:6UVA"
FT   HELIX           63..75
FT                   /evidence="ECO:0007829|PDB:6UVA"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:6UVA"
FT   HELIX           87..98
FT                   /evidence="ECO:0007829|PDB:6UVA"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:6UVA"
FT   HELIX           121..141
FT                   /evidence="ECO:0007829|PDB:6UVA"
SQ   SEQUENCE   148 AA;  16518 MW;  EEEE312496EF513C CRC64;
     METGALRRPQ LLPLLLLLCG GCPRAGGCNE TGMLERLPLC GKAFADMMGK VDVWKWCNLS
     EFIVYYESFT NCTEMEANVV GCYWPNPLAQ GFITGIHRQF FSNCTVDRVH LEDPPDEVLI
     PLIVIPVVLT VAMAGLVVWR SKRTDTLL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024