ID   MPRD_RAT                Reviewed;         278 AA.
AC   Q6AY20;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Cation-dependent mannose-6-phosphate receptor;
DE            Short=CD Man-6-P receptor;
DE            Short=CD-MPR;
DE   Flags: Precursor;
GN   Name=M6pr;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Binds GGA1, GGA2 and GGA3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Single-pass type
CC       I membrane protein {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This receptor has optimal binding in the presence of
CC       divalent cations. {ECO:0000250}.
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DR   EMBL; BC079226; AAH79226.1; -; mRNA.
DR   RefSeq; NP_001007701.1; NM_001007700.1.
DR   RefSeq; XP_003752148.1; XM_003752100.1.
DR   RefSeq; XP_006257263.1; XM_006257201.2.
DR   RefSeq; XP_006257264.1; XM_006257202.1.
DR   RefSeq; XP_008761469.1; XM_008763247.2.
DR   AlphaFoldDB; Q6AY20; -.
DR   SMR; Q6AY20; -.
DR   STRING; 10116.ENSRNOP00000020364; -.
DR   GlyGen; Q6AY20; 5 sites, 9 N-linked glycans (1 site).
DR   iPTMnet; Q6AY20; -.
DR   PhosphoSitePlus; Q6AY20; -.
DR   jPOST; Q6AY20; -.
DR   PaxDb; Q6AY20; -.
DR   PRIDE; Q6AY20; -.
DR   GeneID; 312689; -.
DR   KEGG; rno:312689; -.
DR   UCSC; RGD:1359355; rat.
DR   CTD; 4074; -.
DR   RGD; 1359355; M6pr.
DR   VEuPathDB; HostDB:ENSRNOG00000014992; -.
DR   eggNOG; ENOG502QTJ5; Eukaryota.
DR   HOGENOM; CLU_058440_0_0_1; -.
DR   InParanoid; Q6AY20; -.
DR   OMA; CKRGVTA; -.
DR   OrthoDB; 1214298at2759; -.
DR   PhylomeDB; Q6AY20; -.
DR   TreeFam; TF328910; -.
DR   Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q6AY20; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000014992; Expressed in ovary and 19 other tissues.
DR   Genevisible; Q6AY20; RN.
DR   GO; GO:0005768; C:endosome; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; ISO:RGD.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
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:RGD.
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; ISO:RGD.
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                   /evidence="ECO:0000250"
FT   CHAIN           22..278
FT                   /note="Cation-dependent mannose-6-phosphate receptor"
FT                   /id="PRO_0000249712"
FT   TOPO_DOM        22..188
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..182
FT                   /note="MRH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   REGION          256..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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:0000255"
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"
SQ   SEQUENCE   278 AA;  31095 MW;  EA628873BB2D1198 CRC64;
     MFPLSGCWRT ELLLLLLLAV AVRESWQIEE KSCDLVGEKD KESKNEVALL ERLRPLFNKS
     FESTVGQGSD TYSYIFRVCR EAGNHSSGAG LVQINKSNEK ETVVGRINET HIFNGSNWIM
     LIYKGGDEYD NHCGKEQRRA VVMISCNRHT LAGNFNPVSE ERGKIQDCFY LFEMDSSLAC
     SPEVSHLSVG SILLVIFASL VAVYIIGGFL YQRLVVGAKG MEQFPHLAFW QDLGNLVADG
     CDFVCRSKPR SVPAAYRGVG DDQLGEESEE RDDHLLPM