ID   EPDR1_RAT               Reviewed;         224 AA.
AC   Q5XII0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Mammalian ependymin-related protein 1;
DE            Short=MERP-1;
DE   Flags: Precursor;
GN   Name=Epdr1; Synonyms=Epdr2, Merp1, Merp2;
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=Heart;
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16954209; DOI=10.1074/jbc.m606208200;
RA   Della Valle M.C., Sleat D.E., Sohar I., Wen T., Pintar J.E., Jadot M.,
RA   Lobel P.;
RT   "Demonstration of lysosomal localization for the mammalian ependymin-
RT   related protein using classical approaches combined with a novel density
RT   shift method.";
RL   J. Biol. Chem. 281:35436-35445(2006).
CC   -!- FUNCTION: Binds anionic lipids and gangliosides at acidic pH.
CC       {ECO:0000250|UniProtKB:Q9UM22}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UM22}.
CC   -!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:16954209}.
CC       Secreted {ECO:0000250|UniProtKB:Q9UM22}. Note=Lysosomal and also
CC       secreted. {ECO:0000250|UniProtKB:Q9UM22}.
CC   -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC       {ECO:0000269|PubMed:16954209}.
CC   -!- PTM: N-glycosylated; the glycan contains mannose-6-phosphate moieties.
CC       {ECO:0000250|UniProtKB:Q99M71}.
CC   -!- SIMILARITY: Belongs to the ependymin family. {ECO:0000305}.
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DR   EMBL; BC083701; AAH83701.1; -; mRNA.
DR   RefSeq; NP_001007626.1; NM_001007625.1.
DR   AlphaFoldDB; Q5XII0; -.
DR   SMR; Q5XII0; -.
DR   IntAct; Q5XII0; 1.
DR   STRING; 10116.ENSRNOP00000025674; -.
DR   GlyGen; Q5XII0; 2 sites, 2 N-linked glycans (1 site).
DR   SwissPalm; Q5XII0; -.
DR   PaxDb; Q5XII0; -.
DR   PRIDE; Q5XII0; -.
DR   Ensembl; ENSRNOT00000085923; ENSRNOP00000073174; ENSRNOG00000060141.
DR   GeneID; 291180; -.
DR   KEGG; rno:291180; -.
DR   UCSC; RGD:1359161; rat.
DR   CTD; 54749; -.
DR   RGD; 1359161; Epdr1.
DR   eggNOG; ENOG502QQ8T; Eukaryota.
DR   GeneTree; ENSGT00940000164413; -.
DR   HOGENOM; CLU_097673_0_0_1; -.
DR   InParanoid; Q5XII0; -.
DR   OMA; WVVYDHS; -.
DR   OrthoDB; 1284695at2759; -.
DR   PhylomeDB; Q5XII0; -.
DR   TreeFam; TF328581; -.
DR   PRO; PR:Q5XII0; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000060141; Expressed in Ammon's horn and 17 other tissues.
DR   Genevisible; Q5XII0; RN.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:1905573; F:ganglioside GM1 binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   GO; GO:1990764; P:myofibroblast contraction; ISO:RGD.
DR   InterPro; IPR001299; Ependymin.
DR   PANTHER; PTHR10697; PTHR10697; 1.
DR   Pfam; PF00811; Ependymin; 1.
DR   PRINTS; PR00317; EPENDYMIN.
DR   SMART; SM00026; EPEND; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Lipid-binding; Lysosome; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..224
FT                   /note="Mammalian ependymin-related protein 1"
FT                   /id="PRO_0000322977"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..172
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM22"
FT   DISULFID        88..222
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM22"
FT   DISULFID        113..210
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM22"
SQ   SEQUENCE   224 AA;  25639 MW;  B8DE78133B1CCB21 CRC64;
     MLTRAPRRLV QGPRETWLLG GLWVWILCGL GMAGSPGTPQ PCQAPQQWEG RQVLYQQSSG
     HNSRALVSYD GLNQRVRVLD ERKALIPCKR LFEYILLYKD GVMFQIEQAT KLCAKIPLAE
     PWDPLDIPQN STFEDQYSIG GPQEQIMVQE WSDRRTARSY ETWIGVYTAK DCYPVQETFI
     RNYTVVLSTR FFDVQLGIKD PSVFTPPSTC QTAQPEKMKE NCSL