Q07113 (MPRI_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 119.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cation-independent mannose-6-phosphate receptor Short name=CI Man-6-P receptor Short name=CI-MPR Short name=M6PR Alternative name(s): 300 kDa mannose 6-phosphate receptor Short name=MPR 300 Insulin-like growth factor 2 receptor Insulin-like growth factor II receptor Short name=IGF-II receptor M6P/IGF2 receptor Short name=M6P/IGF2R CD_antigen=CD222 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 2483 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Acts as a positive regulator of T-cell coactivation, by binding DPP4 By similarity. Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. |
| Subunit structure | Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3. Binds HA-I and HA-II plasma membrane adapters By similarity. |
| Subcellular location | |
| Domain | Contains 15 repeating units of approximately 147 AA harboring four disulfide bonds each. The most highly conserved region within the repeat consists of a stretch of 13 AA that contains cysteines at both ends. |
| Sequence similarities | Belongs to the MRL1/IGF2R family. Contains 1 fibronectin type-II domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 35 | 35 | Potential | ||||||||
| Chain | 36 – 2483 | 2448 | Cation-independent mannose-6-phosphate receptor | PRO_0000019230 | |||||||
Regions | |||||||||||
| Topological domain | 36 – 2295 | 2260 | Lumenal Potential | ||||||||
| Transmembrane | 2296 – 2316 | 21 | Helical; Potential | ||||||||
| Topological domain | 2317 – 2483 | 167 | Cytoplasmic Potential | ||||||||
| Repeat | 35 – 184 | 150 | 1 | ||||||||
| Repeat | 185 – 339 | 155 | 2 | ||||||||
| Repeat | 340 – 484 | 145 | 3 | ||||||||
| Repeat | 485 – 637 | 153 | 4 | ||||||||
| Repeat | 638 – 776 | 139 | 5 | ||||||||
| Repeat | 777 – 943 | 167 | 6 | ||||||||
| Repeat | 945 – 1092 | 148 | 7 | ||||||||
| Repeat | 1093 – 1236 | 144 | 8 | ||||||||
| Repeat | 1237 – 1377 | 141 | 9 | ||||||||
| Repeat | 1378 – 1525 | 148 | 10 | ||||||||
| Repeat | 1526 – 1659 | 134 | 11 | ||||||||
| Repeat | 1660 – 1813 | 154 | 12 | ||||||||
| Repeat | 1814 – 2001 | 188 | 13 | ||||||||
| Domain | 1891 – 1937 | 47 | Fibronectin type-II | ||||||||
| Repeat | 2002 – 2130 | 129 | 14 | ||||||||
| Repeat | 2158 – 2282 | 125 | 15 | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 2342 | 1 | N6-acetyllysine By similarity | ||||||||
| Modified residue | 2393 | 1 | Phosphoserine Ref.11 | ||||||||
| Modified residue | 2401 | 1 | Phosphoserine Ref.9 Ref.11 Ref.13 | ||||||||
| Modified residue | 2471 | 1 | Phosphoserine Ref.11 | ||||||||
| Modified residue | 2476 | 1 | Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 | ||||||||
| Glycosylation | 107 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 395 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 430 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 537 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 575 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 620 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 740 | 1 | N-linked (GlcNAc...) Ref.14 | ||||||||
| Glycosylation | 864 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 944 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1157 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1239 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1305 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1358 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1423 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1532 | 1 | N-linked (GlcNAc...) Ref.12 Ref.14 | ||||||||
| Glycosylation | 1649 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1750 | 1 | N-linked (GlcNAc...) Ref.14 | ||||||||
| Glycosylation | 1809 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2078 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2129 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 44 ↔ 64 | By similarity | |||||||||
| Disulfide bond | 72 ↔ 79 | By similarity | |||||||||
| Disulfide bond | 112 ↔ 144 | By similarity | |||||||||
| Disulfide bond | 129 ↔ 156 | By similarity | |||||||||
| Disulfide bond | 169 ↔ 207 | By similarity | |||||||||
| Disulfide bond | 223 ↔ 230 | By similarity | |||||||||
| Disulfide bond | 270 ↔ 301 | By similarity | |||||||||
| Disulfide bond | 283 ↔ 313 | By similarity | |||||||||
| Disulfide bond | 323 ↔ 361 | By similarity | |||||||||
| Disulfide bond | 369 ↔ 377 | By similarity | |||||||||
| Disulfide bond | 415 ↔ 449 | By similarity | |||||||||
| Disulfide bond | 429 ↔ 461 | By similarity | |||||||||
| Disulfide bond | 621 ↔ 658 | By similarity | |||||||||
| Disulfide bond | 666 ↔ 673 | By similarity | |||||||||
| Disulfide bond | 724 ↔ 753 | By similarity | |||||||||
| Disulfide bond | 1509 ↔ 1546 | By similarity | |||||||||
| Disulfide bond | 1552 ↔ 1559 | By similarity | |||||||||
| Disulfide bond | 1591 ↔ 1627 | By similarity | |||||||||
| Disulfide bond | 1607 ↔ 1639 | By similarity | |||||||||
| Disulfide bond | 1645 ↔ 1688 | By similarity | |||||||||
| Disulfide bond | 1699 ↔ 1706 | By similarity | |||||||||
| Disulfide bond | 1743 ↔ 1776 | By similarity | |||||||||
| Disulfide bond | 1759 ↔ 1788 | By similarity | |||||||||
| Disulfide bond | 1797 ↔ 1832 | By similarity | |||||||||
| Disulfide bond | 1843 ↔ 1849 | By similarity | |||||||||
| Disulfide bond | 1886 ↔ 1968 | By similarity | |||||||||
| Disulfide bond | 1896 ↔ 1920 | By similarity | |||||||||
| Disulfide bond | 1910 ↔ 1935 | By similarity | |||||||||
| Disulfide bond | 1950 ↔ 1980 | By similarity | |||||||||
| Disulfide bond | 1987 ↔ 2022 | By similarity | |||||||||
| Disulfide bond | 2032 ↔ 2039 | By similarity | |||||||||
| Disulfide bond | 2075 ↔ 2106 | By similarity | |||||||||
| Disulfide bond | 2089 ↔ 2118 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 10 – 11 | 2 | PS → RP Ref.2 | ||||||||
| Sequence conflict | 13 | 1 | Missing Ref.2 | ||||||||
| Sequence conflict | 209 | 1 | D → V in AAA19568. Ref.2 | ||||||||
| Sequence conflict | 456 – 457 | 2 | DT → VS Ref.2 | ||||||||
| Sequence conflict | 1626 – 1631 | 6 | TCTLFF → GSTFFS in CAA42940. Ref.6 | ||||||||
| Sequence conflict | 1694 – 1695 | 2 | MH → TC in CAA42940. Ref.6 | ||||||||
| Sequence conflict | 1699 | 1 | C → R in CAA42940. Ref.6 | ||||||||
| Sequence conflict | 1759 | 1 | C → Y in AAA19568. Ref.2 | ||||||||
| Sequence conflict | 2028 | 1 | G → V in CAA42940. Ref.6 | ||||||||
| Sequence conflict | 2032 | 1 | C → S in CAA42940. Ref.6 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The mouse insulin-like growth factor II/cation-independent mannose 6-phosphate (IGF-II/MPR) receptor gene: molecular cloning and genomic organization." Szebenyi G., Rotwein P. Genomics 19:120-129(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Cloning and sequencing of cDNAs encoding the full-length mouse mannose 6-phosphate/insulin-like growth factor II receptor." Ludwig T., Tenscher K., Remmler J., Hoflack B., Lobel P. Gene 142:311-312(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6 X CBA. Tissue: Liver. |
| [3] | "Maternal-specific methylation of the imprinted mouse Igf2r locus identifies the expressed locus as carrying the imprinting signal." Stoger R., Kubicka P., Liu C.G., Kafri T., Razin A., Cedar H., Barlow D.P. Cell 73:61-71(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 AND 93-106. Strain: 129 and C57BL/6. |
| [4] | "Control of insulin-like growth factor-II/mannose 6-phosphate receptor gene transcription by proximal promoter elements." Liu Z., Mittanck D.W., Kim S., Rotwein P. Mol. Endocrinol. 9:1477-1487(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44. Strain: 129/Sv. |
| [5] | "Differential regulation of mannose 6-phosphate receptors and their ligands during the myogenic development of C2 cells." Szebenyi G., Rotwein P. J. Biol. Chem. 266:5534-5539(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 435-488. Tissue: Liver. |
| [6] | Matzner U. Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1625-2045. Strain: C57BL/6. |
| [7] | "Mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor. A consensus casein kinase II site followed by 2 leucines near the carboxyl terminus is important for intracellular targeting of lysosomal enzymes." Chen H.J., Remmler J., Delaney J.C., Messner D.J., Lobel P. J. Biol. Chem. 268:22338-22346(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2249-2483. Strain: C57BL/6 X CBA. Tissue: Liver. |
| [8] | "Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2476, MASS SPECTROMETRY. Tissue: Liver. |
| [9] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, MASS SPECTROMETRY. Tissue: Liver. |
| [10] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2476, MASS SPECTROMETRY. Tissue: Melanoma. |
| [11] | "The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2393; SER-2401; SER-2471 AND SER-2476, MASS SPECTROMETRY. Tissue: Macrophage. |
| [12] | "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1532, MASS SPECTROMETRY. Tissue: Myoblast. |
| [13] | "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, MASS SPECTROMETRY. Tissue: Embryonic fibroblast. |
| [14] | "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-740; ASN-1532 AND ASN-1750, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L22143 L22142 Genomic DNA. Translation: AAA39320.1.U04710 mRNA. Translation: AAA19568.1. L06445 Genomic DNA. Translation: AAA37921.1. L06446 Genomic DNA. Translation: AAA37922.1. U26348 Genomic DNA. Translation: AAA98844.1. M58586 Genomic DNA. Translation: AAA39483.1. X60389 mRNA. Translation: CAA42940.1. L19500 mRNA. Translation: AAA16037.1. |
| IPI | IPI00308971. |
| PIR | A49617. I48922. |
| RefSeq | NP_034645.2. NM_010515.2. |
| UniGene | Mm.26553. |
3D structure databases | |
| ProteinModelPortal | Q07113. |
| SMR | Q07113. Positions 43-2274. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q07113. 3 interactions. |
| MINT | MINT-200350. |
PTM databases | |
| PhosphoSite | Q07113. |
Proteomic databases | |
| PaxDb | Q07113. |
| PRIDE | Q07113. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000024599; ENSMUSP00000024599; ENSMUSG00000023830. |
| GeneID | 16004. |
| KEGG | mmu:16004. |
| UCSC | uc008aky.1. mouse. |
Organism-specific databases | |
| CTD | 3482. |
| MGI | MGI:96435. Igf2r. |
Phylogenomic databases | |
| eggNOG | NOG260109. |
| GeneTree | ENSGT00390000013943. |
| HOGENOM | HOG000113638. |
| HOVERGEN | HBG000334. |
| InParanoid | Q07113. |
| KO | K06564. |
| OMA | NTEAACP. |
| OrthoDB | EOG4G1MFG. |
Gene expression databases | |
| ArrayExpress | Q07113. |
| Bgee | Q07113. |
| CleanEx | MM_IGF2R. |
| Genevestigator | Q07113. |
| GermOnline | ENSMUSG00000023830. Mus musculus. |
Family and domain databases | |
| Gene3D | 2.10.10.10. 1 hit. |
| InterPro | IPR000479. CIMR. IPR000562. FN_type2_col-bd. IPR013806. Kringle-like. IPR009011. Man6P_isomerase_rcpt-bd_dom. [Graphical view] |
| Pfam | PF00878. CIMR. 14 hits. PF00040. fn2. 1 hit. [Graphical view] |
| SMART | SM00059. FN2. 1 hit. [Graphical view] |
| SUPFAM | SSF57440. Kringle-like. 1 hit. SSF50911. Man6php_recept. 15 hits. |
| PROSITE | PS00023. FN2_1. 1 hit. PS51092. FN2_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 288798. |
| SOURCE | Search... |
Entry information
| Entry name | MPRI_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q07113 Secondary accession number(s): Q61822, Q6LED1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
