MPRD_BOVIN
ID MPRD_BOVIN Reviewed; 279 AA.
AC P11456; A1L5A0; Q0VCN7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 170.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2954652; DOI=10.1016/0092-8674(87)90214-5;
RA Dahms N.M., Lobel P., Breitmeyer J., Chirgwin J.M., Kornfeld S.;
RT "46 kd mannose 6-phosphate receptor: cloning, expression, and homology to
RT the 215 kd mannose 6-phosphate receptor.";
RL Cell 50:181-192(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP HOMODIMERIZATION.
RX PubMed=2544594; DOI=10.1016/s0021-9258(18)60486-7;
RA Dahms N.M., Kornfeld S.;
RT "The cation-dependent mannose 6-phosphate receptor. Structural requirements
RT for mannose 6-phosphate binding and oligomerization.";
RL J. Biol. Chem. 264:11458-11467(1989).
RN [5]
RP MUTAGENESIS OF 246-CYS--ARG-251, AND SUBCELLULAR LOCATION.
RX PubMed=7559753; DOI=10.1083/jcb.130.6.1297;
RA Rohrer J., Schweizer A., Johnson K.F., Kornfeld S.;
RT "A determinant in the cytoplasmic tail of the cation-dependent mannose 6-
RT phosphate receptor prevents trafficking to lysosomes.";
RL J. Cell Biol. 130:1297-1306(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-182.
RX PubMed=9604938; DOI=10.1016/s0092-8674(00)81192-7;
RA Roberts D.L., Weix D.J., Dahms N.M., Kim J.-J.P.;
RT "Molecular basis of lysosomal enzyme recognition: three-dimensional
RT structure of the cation-dependent mannose 6-phosphate receptor.";
RL Cell 93:639-648(1998).
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. Interacts with GGA1, GGA2 and GGA3 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:7559753};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:7559753}.
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; M17025; AAA30634.1; -; mRNA.
DR EMBL; BT029887; ABM06137.1; -; mRNA.
DR EMBL; BC120081; AAI20082.1; -; mRNA.
DR PIR; A27068; A27068.
DR RefSeq; NP_786973.1; NM_175779.3.
DR PDB; 1C39; X-ray; 1.85 A; A/B=31-182.
DR PDB; 1KEO; X-ray; 2.20 A; A/B=29-182.
DR PDB; 1M6P; X-ray; 1.80 A; A/B=31-182.
DR PDB; 2RL7; X-ray; 2.00 A; A/B/C/D=29-182.
DR PDB; 2RL8; X-ray; 1.45 A; A/B=29-182.
DR PDB; 2RL9; X-ray; 2.40 A; A/B=29-182.
DR PDB; 2RLB; X-ray; 1.75 A; A/B=29-182.
DR PDB; 3CY4; X-ray; 1.51 A; A/B=29-182.
DR PDB; 3K41; X-ray; 1.90 A; A/B=29-182.
DR PDB; 3K42; X-ray; 2.30 A; A/B=29-182.
DR PDB; 3K43; X-ray; 2.00 A; A/B=29-182.
DR PDBsum; 1C39; -.
DR PDBsum; 1KEO; -.
DR PDBsum; 1M6P; -.
DR PDBsum; 2RL7; -.
DR PDBsum; 2RL8; -.
DR PDBsum; 2RL9; -.
DR PDBsum; 2RLB; -.
DR PDBsum; 3CY4; -.
DR PDBsum; 3K41; -.
DR PDBsum; 3K42; -.
DR PDBsum; 3K43; -.
DR AlphaFoldDB; P11456; -.
DR SMR; P11456; -.
DR ELM; P11456; -.
DR STRING; 9913.ENSBTAP00000024233; -.
DR UniLectin; P11456; -.
DR iPTMnet; P11456; -.
DR SwissPalm; P11456; -.
DR PaxDb; P11456; -.
DR PeptideAtlas; P11456; -.
DR PRIDE; P11456; -.
DR Ensembl; ENSBTAT00000024233; ENSBTAP00000024233; ENSBTAG00000018207.
DR Ensembl; ENSBTAT00000067687; ENSBTAP00000059756; ENSBTAG00000018207.
DR GeneID; 281291; -.
DR KEGG; bta:281291; -.
DR CTD; 4074; -.
DR VEuPathDB; HostDB:ENSBTAG00000018207; -.
DR VGNC; VGNC:31125; M6PR.
DR eggNOG; ENOG502QTJ5; Eukaryota.
DR GeneTree; ENSGT00390000002109; -.
DR HOGENOM; CLU_058440_0_0_1; -.
DR InParanoid; P11456; -.
DR OMA; CKRGVTA; -.
DR OrthoDB; 1214298at2759; -.
DR TreeFam; TF328910; -.
DR Reactome; R-BTA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR EvolutionaryTrace; P11456; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000018207; Expressed in monocyte and 105 other tissues.
DR GO; GO:0005768; C:endosome; ISS:AgBase.
DR GO; GO:0005794; C:Golgi apparatus; TAS:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; IBA:GO_Central.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IEA:Ensembl.
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 3D-structure; Disulfide bond; Glycoprotein; Lysosome; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..28
FT CHAIN 29..279
FT /note="Cation-dependent mannose-6-phosphate receptor"
FT /id="PRO_0000019225"
FT TOPO_DOM 29..187
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..213
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 214..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 32..183
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 258..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24668"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 134..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 147..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT MUTAGEN 246..251
FT /note="CRSKPR->AAAAAA: Leads to rapid lysosomal
FT degradation."
FT /evidence="ECO:0000269|PubMed:7559753"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2RL8"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1KEO"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:2RL8"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3CY4"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2RL8"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 102..115
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2RL8"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2RL8"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:2RL8"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2RL8"
SQ SEQUENCE 279 AA; 31201 MW; 7351C85A32F39A70 CRC64;
MMSPLHSSWR TGLLLLLLFS VAVRESWQTE EKTCDLVGEK GKESEKELAL LKRLTPLFNK
SFESTVGQSP DMYSYVFRVC REAGNHSSGA GLVQINKSNG KETVVGRFNE TQIFNGSNWI
MLIYKGGDEY DNHCGREQRR AVVMISCNRH TLADNFNPVS EERGKVQDCF YLFEMDSSLA
CSPEISHLSV GSILLVTLAS LVAVYIIGGF LYQRLVVGAK GMEQFPHLAF WQDLGNLVAD
GCDFVCRSKP RNVPAAYRGV GDDQLGEESE ERDDHLLPM
