ID   EPD1_CARAU              Reviewed;         215 AA.
AC   P13506;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Ependymin-1;
DE   AltName: Full=Ependymin I;
DE            Short=EPD-I;
DE   Flags: Precursor;
GN   Name=epd1; Synonyms=epn1;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=2760037; DOI=10.1016/s0021-9258(18)80052-7;
RA   Koenigstorfer A., Sterrer S., Hoffmann W.;
RT   "Biosynthesis of ependymins from goldfish brain.";
RL   J. Biol. Chem. 264:13689-13692(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=2908890; DOI=10.1111/j.1471-4159.1989.tb10932.x;
RA   Koenigstorfer A., Sterrer S., Eckerskorn C., Lottspeich F., Schmidt R.,
RA   Hoffmann W.;
RT   "Molecular characterization of an ependymin precursor from goldfish
RT   brain.";
RL   J. Neurochem. 52:310-312(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=8163195; DOI=10.1016/0378-1119(94)90578-9;
RA   Adams D.S., Shashoua V.E.;
RT   "Cloning and sequencing the genes encoding goldfish and carp ependymin.";
RL   Gene 141:237-241(1994).
CC   -!- FUNCTION: May play a role in neural plasticity. May be involved during
CC       axon regeneration.
CC   -!- SUBUNIT: Forms disulfide-linked dimers.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: EPDs are synthesized in the meninx and secreted in
CC       the cerebrospinal fluid.
CC   -!- PTM: Different glycosylation variants are known as EPD-beta and EPD-
CC       gamma.
CC   -!- PTM: Binds calcium through the terminal sialic acids.
CC   -!- SIMILARITY: Belongs to the ependymin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA32352.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X14134; CAA32352.1; ALT_INIT; mRNA.
DR   EMBL; U00433; AAA19566.1; -; Unassigned_DNA.
DR   PIR; JL0090; JL0090.
DR   AlphaFoldDB; P13506; -.
DR   SMR; P13506; -.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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   Calcium; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..215
FT                   /note="Ependymin-1"
FT                   /id="PRO_0000008341"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   215 AA;  24137 MW;  7C286D094FA68409 CRC64;
     MHTVKLLCVV FSCLCAVAWA SSHRQPCHAP PLTSGTMKVV STGGHDLESG EFSYDSKANK
     FRFVEDTAHA NKTSHMDVLI HFEEGVLYEI DSKNESCKKE TLQFRKHLME IPPDATHESE
     IYMGSPSITE QGLRVRVWNG KFPELHAHYS MSTTSCGCLP VSGSYHGEKK DLHFSFFGVE
     TEVDDLQVFV PPAYCEGVAF EEAPDDHSFF DLFHD