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Protein

Cation-dependent mannose-6-phosphate receptor

Gene

M6PR

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. mannose binding Source: InterPro
  2. mannose transmembrane transporter activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Cation-dependent mannose-6-phosphate receptor
Short name:
CD Man-6-P receptor
Short name:
CD-MPR
Alternative name(s):
46 kDa mannose 6-phosphate receptor
Short name:
MPR 46
Gene namesi
Name:M6PR
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 5

Subcellular locationi

Lysosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 187159LumenalCuratedAdd
BLAST
Transmembranei188 – 21326HelicalCuratedAdd
BLAST
Topological domaini214 – 27966CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  1. endosome Source: AgBase
  2. Golgi apparatus Source: AgBase
  3. integral component of membrane Source: UniProtKB-KW
  4. late endosome Source: Ensembl
  5. lysosomal membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi246 – 2516CRSKPR → AAAAAA: Leads to rapid lysosomal degradation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Add
BLAST
Chaini29 – 279251Cation-dependent mannose-6-phosphate receptorPRO_0000019225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi85 – 851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Modified residuei269 – 2691PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP11456.
PRIDEiP11456.

Interactioni

Subunit structurei

Homodimer. Interacts with GGA1, GGA2 and GGA3 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024233.

Structurei

Secondary structure

1
279
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 393Combined sources
Turni40 – 423Combined sources
Helixi45 – 539Combined sources
Helixi55 – 573Combined sources
Beta strandi62 – 665Combined sources
Beta strandi73 – 775Combined sources
Beta strandi79 – 813Combined sources
Beta strandi84 – 885Combined sources
Beta strandi90 – 967Combined sources
Turni97 – 993Combined sources
Beta strandi102 – 11514Combined sources
Beta strandi117 – 12610Combined sources
Beta strandi131 – 1333Combined sources
Helixi134 – 1363Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi152 – 16211Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi170 – 1778Combined sources
Helixi178 – 1803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C39X-ray1.85A/B31-182[»]
1KEOX-ray2.20A/B29-182[»]
1M6PX-ray1.80A/B31-182[»]
2RL7X-ray2.00A/B/C/D29-182[»]
2RL8X-ray1.45A/B29-182[»]
2RL9X-ray2.40A/B29-182[»]
2RLBX-ray1.75A/B29-182[»]
3CY4X-ray1.51A/B29-182[»]
3K41X-ray1.90A/B29-182[»]
3K42X-ray2.30A/B29-182[»]
3K43X-ray2.00A/B29-182[»]
ProteinModelPortaliP11456.
SMRiP11456. Positions 29-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11456.

Family & Domainsi

Domaini

The extracellular domain is homologous to the repeating units (of approximately 147 AA) of the cation-independent mannose 6-phosphate receptor.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG45234.
GeneTreeiENSGT00390000002109.
HOGENOMiHOG000013085.
HOVERGENiHBG006395.
InParanoidiP11456.
KOiK10089.
OMAiSDWIMLI.
OrthoDBiEOG7PP576.
TreeFamiTF328910.

Family and domain databases

Gene3Di2.70.130.10. 1 hit.
InterProiIPR028927. Man-6-P_rcpt.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR000296. Man_6_P_rcpt.
[Graphical view]
PfamiPF02157. Man-6-P_recep. 1 hit.
[Graphical view]
PRINTSiPR00715. MAN6PRECEPTR.
SUPFAMiSSF50911. SSF50911. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11456-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMSPLHSSWR TGLLLLLLFS VAVRESWQTE EKTCDLVGEK GKESEKELAL
60 70 80 90 100
LKRLTPLFNK SFESTVGQSP DMYSYVFRVC REAGNHSSGA GLVQINKSNG
110 120 130 140 150
KETVVGRFNE TQIFNGSNWI MLIYKGGDEY DNHCGREQRR AVVMISCNRH
160 170 180 190 200
TLADNFNPVS EERGKVQDCF YLFEMDSSLA CSPEISHLSV GSILLVTLAS
210 220 230 240 250
LVAVYIIGGF LYQRLVVGAK GMEQFPHLAF WQDLGNLVAD GCDFVCRSKP
260 270
RNVPAAYRGV GDDQLGEESE ERDDHLLPM
Length:279
Mass (Da):31,201
Last modified:October 1, 1989 - v1
Checksum:i7351C85A32F39A70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17025 mRNA. Translation: AAA30634.1.
BT029887 mRNA. Translation: ABM06137.1.
BC120081 mRNA. Translation: AAI20082.1.
PIRiA27068.
RefSeqiNP_786973.1. NM_175779.3.
UniGeneiBt.5032.

Genome annotation databases

EnsembliENSBTAT00000024233; ENSBTAP00000024233; ENSBTAG00000018207.
GeneIDi281291.
KEGGibta:281291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17025 mRNA. Translation: AAA30634.1.
BT029887 mRNA. Translation: ABM06137.1.
BC120081 mRNA. Translation: AAI20082.1.
PIRiA27068.
RefSeqiNP_786973.1. NM_175779.3.
UniGeneiBt.5032.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C39X-ray1.85A/B31-182[»]
1KEOX-ray2.20A/B29-182[»]
1M6PX-ray1.80A/B31-182[»]
2RL7X-ray2.00A/B/C/D29-182[»]
2RL8X-ray1.45A/B29-182[»]
2RL9X-ray2.40A/B29-182[»]
2RLBX-ray1.75A/B29-182[»]
3CY4X-ray1.51A/B29-182[»]
3K41X-ray1.90A/B29-182[»]
3K42X-ray2.30A/B29-182[»]
3K43X-ray2.00A/B29-182[»]
ProteinModelPortaliP11456.
SMRiP11456. Positions 29-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024233.

Proteomic databases

PaxDbiP11456.
PRIDEiP11456.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000024233; ENSBTAP00000024233; ENSBTAG00000018207.
GeneIDi281291.
KEGGibta:281291.

Organism-specific databases

CTDi4074.

Phylogenomic databases

eggNOGiNOG45234.
GeneTreeiENSGT00390000002109.
HOGENOMiHOG000013085.
HOVERGENiHBG006395.
InParanoidiP11456.
KOiK10089.
OMAiSDWIMLI.
OrthoDBiEOG7PP576.
TreeFamiTF328910.

Miscellaneous databases

EvolutionaryTraceiP11456.
NextBioi20805321.

Family and domain databases

Gene3Di2.70.130.10. 1 hit.
InterProiIPR028927. Man-6-P_rcpt.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR000296. Man_6_P_rcpt.
[Graphical view]
PfamiPF02157. Man-6-P_recep. 1 hit.
[Graphical view]
PRINTSiPR00715. MAN6PRECEPTR.
SUPFAMiSSF50911. SSF50911. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "46 kd mannose 6-phosphate receptor: cloning, expression, and homology to the 215 kd mannose 6-phosphate receptor."
    Dahms N.M., Lobel P., Breitmeyer J., Chirgwin J.M., Kornfeld S.
    Cell 50:181-192(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal cerebellum.
  4. "The cation-dependent mannose 6-phosphate receptor. Structural requirements for mannose 6-phosphate binding and oligomerization."
    Dahms N.M., Kornfeld S.
    J. Biol. Chem. 264:11458-11467(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION.
  5. "A determinant in the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor prevents trafficking to lysosomes."
    Rohrer J., Schweizer A., Johnson K.F., Kornfeld S.
    J. Cell Biol. 130:1297-1306(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 246-CYS--ARG-251, SUBCELLULAR LOCATION.
  6. "Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor."
    Roberts D.L., Weix D.J., Dahms N.M., Kim J.-J.P.
    Cell 93:639-648(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-182.

Entry informationi

Entry nameiMPRD_BOVIN
AccessioniPrimary (citable) accession number: P11456
Secondary accession number(s): A1L5A0, Q0VCN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: January 7, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This receptor has optimal binding in the presence of divalent cations.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.