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EPDR1_MACFA
ID   EPDR1_MACFA             Reviewed;         224 AA.
AC   Q9N0C7; Q95K54; Q95K77;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 3.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Mammalian ependymin-related protein 1;
DE            Short=MERP-1;
DE   Flags: Precursor;
GN   Name=EPDR1; Synonyms=MERP1;
GN   ORFNames=QccE-12983, QmoA-12340, QmoA-13475, QtrA-11871;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, Medulla oblongata, and Temporal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Medulla oblongata;
RX   PubMed=11574149; DOI=10.1016/s0378-1119(01)00665-5;
RA   Osada N., Hida M., Kususda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA   Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.;
RT   "Assignment of 118 novel cDNAs of cynomolgus monkey brain to human
RT   chromosomes.";
RL   Gene 275:31-37(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB01585.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB60800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB62213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC41745.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB046003; BAB01585.1; ALT_INIT; mRNA.
DR   EMBL; AB063094; BAB60800.1; ALT_INIT; mRNA.
DR   EMBL; AB066537; BAB62213.1; ALT_INIT; mRNA.
DR   EMBL; AB097520; BAC41745.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q9N0C7; -.
DR   SMR; Q9N0C7; -.
DR   STRING; 9541.XP_005549818.1; -.
DR   eggNOG; ENOG502QQ8T; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   InterPro; IPR001299; Ependymin.
DR   InterPro; IPR018224; Ependymin_CS.
DR   PANTHER; PTHR10697; PTHR10697; 1.
DR   Pfam; PF00811; Ependymin; 1.
DR   PRINTS; PR00317; EPENDYMIN.
DR   SMART; SM00026; EPEND; 1.
DR   PROSITE; PS00898; EPENDYMIN_1; 1.
DR   PROSITE; PS00899; EPENDYMIN_2; 1.
PE   2: Evidence at transcript 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_0000008352"
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"
FT   CONFLICT        47
FT                   /note="Q -> L (in Ref. 1; BAB60800 and 2; BAC41745)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="V -> L (in Ref. 1; BAB62213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="F -> V (in Ref. 1; BAB01585)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   224 AA;  25532 MW;  358E80B615AB4BB7 CRC64;
     MPGRAPLHTV PGALGPWLLG CLWAWTLCGL CSLGAVGAPR PCQAPQQWEG RQVMYQQSSG
     RNSRALLSYD GLNQRVRVLD ERKALIPCKR LFEYILLYKD GVMFQIEQAT KQCSKMTLTE
     PWDPLDIPQN STFEDQYSIG GPQEQIMVQE WSDRKSARSY ETWIGIYTVK DCYPVQETFT
     KNYSVILSTR FFDIQLGIKD PSVFTPPSTC QIAQLEKMSE DCSW
 
 
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