MPRD_MOUSE
ID MPRD_MOUSE Reviewed; 278 AA.
AC P24668;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cation-dependent mannose-6-phosphate receptor;
DE Short=CD Man-6-P receptor;
DE Short=CD-MPR;
DE AltName: Full=46 kDa mannose 6-phosphate receptor;
DE Short=MPR 46;
DE Flags: Precursor;
GN Name=M6pr; Synonyms=46mpr;
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].
RC TISSUE=Liver;
RX PubMed=1376319; DOI=10.1016/s0021-9258(19)49826-8;
RA Ludwig T., Ruether U., Metzger R., Copeland N.G., Jenkins N.A., Lobel P.,
RA Hoflack B.;
RT "Gene and pseudogene of the mouse cation-dependent mannose 6-phosphate
RT receptor. Genomic organization, expression, and chromosomal localization.";
RL J. Biol. Chem. 267:12211-12219(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=1647783; DOI=10.1515/bchm3.1991.372.1.297;
RA Koester A., Nagel G., von Figura K., Pohlmann R.;
RT "Molecular cloning of the mouse 46-kDa mannose 6-phosphate receptor (MPR
RT 46).";
RL Biol. Chem. Hoppe-Seyler 372:297-300(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1645352; DOI=10.1016/s0021-9258(18)99264-1;
RA Ma Z., Grubb J.H., Sly W.S.;
RT "Cloning, sequencing, and functional characterization of the murine 46-kDa
RT mannose 6-phosphate receptor.";
RL J. Biol. Chem. 266:10589-10595(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Olfactory epithelium;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 156-233.
RX PubMed=1848553; DOI=10.1016/s0021-9258(19)67627-1;
RA Szebenyi G., Rotwein P.;
RT "Differential regulation of mannose 6-phosphate receptors and their ligands
RT during the myogenic development of C2 cells.";
RL J. Biol. Chem. 266:5534-5539(1991).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Transport of phosphorylated lysosomal enzymes from the Golgi
CC complex and the cell surface to lysosomes. Lysosomal enzymes bearing
CC phosphomannosyl residues bind specifically to mannose-6-phosphate
CC receptors in the Golgi apparatus and the resulting receptor-ligand
CC complex is transported to an acidic prelyosomal compartment where the
CC low pH mediates the dissociation of the complex.
CC -!- SUBUNIT: Homodimer. Binds GGA1, GGA2 and GGA3 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane
CC protein.
CC -!- DOMAIN: The extracellular domain is homologous to the repeating units
CC (of approximately 147 AA) of the cation-independent mannose 6-phosphate
CC receptor.
CC -!- MISCELLANEOUS: This receptor has optimal binding in the presence of
CC divalent cations.
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DR EMBL; X64068; CAA45423.1; -; mRNA.
DR EMBL; X64070; CAA45426.1; -; mRNA.
DR EMBL; X56831; CAA40162.1; -; mRNA.
DR EMBL; M63286; AAA39735.1; -; mRNA.
DR EMBL; BC027210; AAH27210.1; -; mRNA.
DR EMBL; BC046956; AAH46956.1; -; mRNA.
DR EMBL; BC080811; AAH80811.1; -; mRNA.
DR EMBL; M58585; AAA39482.1; -; mRNA.
DR CCDS; CCDS20493.1; -.
DR PIR; A40399; A40399.
DR RefSeq; NP_034879.2; NM_010749.7.
DR AlphaFoldDB; P24668; -.
DR SMR; P24668; -.
DR BioGRID; 201263; 8.
DR IntAct; P24668; 8.
DR STRING; 10090.ENSMUSP00000007602; -.
DR GlyConnect; 2194; 12 N-Linked glycans (2 sites).
DR GlyGen; P24668; 5 sites, 12 N-linked glycans (2 sites).
DR iPTMnet; P24668; -.
DR PhosphoSitePlus; P24668; -.
DR SwissPalm; P24668; -.
DR EPD; P24668; -.
DR jPOST; P24668; -.
DR PaxDb; P24668; -.
DR PeptideAtlas; P24668; -.
DR PRIDE; P24668; -.
DR ProteomicsDB; 252610; -.
DR Antibodypedia; 11573; 266 antibodies from 31 providers.
DR DNASU; 17113; -.
DR Ensembl; ENSMUST00000007602; ENSMUSP00000007602; ENSMUSG00000007458.
DR Ensembl; ENSMUST00000112610; ENSMUSP00000108229; ENSMUSG00000007458.
DR GeneID; 17113; -.
DR KEGG; mmu:17113; -.
DR UCSC; uc009dow.1; mouse.
DR CTD; 4074; -.
DR MGI; MGI:96904; M6pr.
DR VEuPathDB; HostDB:ENSMUSG00000007458; -.
DR eggNOG; ENOG502QTJ5; Eukaryota.
DR GeneTree; ENSGT00390000002109; -.
DR HOGENOM; CLU_058440_0_0_1; -.
DR InParanoid; P24668; -.
DR OMA; CKRGVTA; -.
DR OrthoDB; 1214298at2759; -.
DR PhylomeDB; P24668; -.
DR TreeFam; TF328910; -.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 17113; 3 hits in 72 CRISPR screens.
DR ChiTaRS; M6pr; mouse.
DR PRO; PR:P24668; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P24668; protein.
DR Bgee; ENSMUSG00000007458; Expressed in proximal tubule and 123 other tissues.
DR ExpressionAtlas; P24668; baseline and differential.
DR Genevisible; P24668; MM.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR GO; GO:1905394; F:retromer complex binding; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0007041; P:lysosomal transport; IDA:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; IBA:GO_Central.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IDA:MGI.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR028927; Man-6-P_rcpt.
DR InterPro; IPR000296; Man-6-P_rcpt_cation_dep.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR Pfam; PF02157; Man-6-P_recep; 1.
DR PRINTS; PR00715; MAN6PRECEPTR.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Lysosome; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT CHAIN 22..278
FT /note="Cation-dependent mannose-6-phosphate receptor"
FT /id="PRO_0000019227"
FT TOPO_DOM 22..186
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..182
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 257..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 133..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 146..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT CONFLICT 196
FT /note="I -> T (in Ref. 5; AAA39482)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="M -> T (in Ref. 5; AAA39482)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="H -> P (in Ref. 5; AAA39482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 31172 MW; 8E0E8727CE793E7D CRC64;
MFPFSGCWRT ELLLLLLLAV AVRESWQIEE KSCDLVGEKD KESKNEVALL ERLRPLFNKS
FESTVGQGSD TYSYIFRVCR EASNHSSGAG LVQINKSNDK ETVVGRINET HIFNGSNWIM
LIYKGGDEYD NHCGKEQRRA VVMISCNRHT LAANFNPVSE ERGKVQDCFY LFEMDSSLAC
SPEVSHLSVG SILLVIFASL VAVYIIGGFL YQRLVVGAKG MEQFPHLAFW QDLGNLVADG
CDFVCRSKPR NVPAAYRGVG DDQLGEESEE RDDHLLPM
