ID   EPDR1_BOVIN             Reviewed;         236 AA.
AC   A6QLI0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Mammalian ependymin-related protein 1;
DE            Short=MERP-1;
DE   Flags: Precursor;
GN   Name=EPDR1; Synonyms=MERP1;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9UM22}.
CC       Secreted {ECO:0000250|UniProtKB:Q9UM22}. Note=Lysosomal and also
CC       secreted. {ECO:0000250|UniProtKB:Q9UM22}.
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; BC147972; AAI47973.1; -; mRNA.
DR   RefSeq; NP_001095758.1; NM_001102288.2.
DR   AlphaFoldDB; A6QLI0; -.
DR   SMR; A6QLI0; -.
DR   STRING; 9913.ENSBTAP00000044382; -.
DR   PaxDb; A6QLI0; -.
DR   PRIDE; A6QLI0; -.
DR   Ensembl; ENSBTAT00000047158; ENSBTAP00000044382; ENSBTAG00000033197.
DR   GeneID; 615376; -.
DR   KEGG; bta:615376; -.
DR   CTD; 54749; -.
DR   VEuPathDB; HostDB:ENSBTAG00000033197; -.
DR   VGNC; VGNC:28530; EPDR1.
DR   eggNOG; ENOG502QQ8T; Eukaryota.
DR   GeneTree; ENSGT00940000161910; -.
DR   HOGENOM; CLU_097673_0_0_1; -.
DR   InParanoid; A6QLI0; -.
DR   OMA; WVVYDHS; -.
DR   OrthoDB; 1284695at2759; -.
DR   TreeFam; TF328581; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000033197; Expressed in thyroid gland and 101 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:1905573; F:ganglioside GM1 binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   GO; GO:1990764; P:myofibroblast contraction; IEA:Ensembl.
DR   InterPro; IPR001299; Ependymin.
DR   PANTHER; PTHR10697; PTHR10697; 1.
DR   Pfam; PF00811; Ependymin; 1.
DR   PRINTS; PR00317; EPENDYMIN.
DR   SMART; SM00026; EPEND; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Lipid-binding; Lysosome; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..236
FT                   /note="Mammalian ependymin-related protein 1"
FT                   /id="PRO_0000322975"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..184
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM22"
FT   DISULFID        100..234
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM22"
FT   DISULFID        125..222
FT                   /evidence="ECO:0000250|UniProtKB:Q9UM22"
SQ   SEQUENCE   236 AA;  26485 MW;  3AA80DFEC22B1BB4 CRC64;
     MPRRAPLRVA RGSLDAWLLG GLWVCALGCL CGVGMAAPGA GAGAGGSLGA QRPCQAPQQW
     EGRQVLYRQS TGRYSRALLS YDGLNQRVRV LDERKALIPC KRLFEYILLY KDGVMFQIEQ
     ATKQCSKITL TEPWDPLDIP QNSTFEDQYS IGGPQEQITV QEWSDRKSAR SYETWIGIYT
     VKDCYPVQET VTKNYSVILS TRFFDIQLGI KDPSVFIPPS TCQTAQPERM SEECSW