ID EPD_CYPCA Reviewed; 215 AA.
AC P38528;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Ependymin;
DE Short=EPD;
DE Flags: Precursor;
GN Name=epd; Synonyms=epn;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: EPDs are synthesized in the meninx and secreted in
CC the cerebrospinal fluid.
CC -!- PTM: Binds calcium through the terminal sialic acids.
CC -!- SIMILARITY: Belongs to the ependymin family. {ECO:0000305}.
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DR EMBL; U00432; AAA19565.1; -; Genomic_DNA.
DR PIR; I51377; I51377.
DR AlphaFoldDB; P38528; -.
DR SMR; P38528; -.
DR GlyCosmos; P38528; 2 sites, No reported glycans.
DR Proteomes; UP000694384; Unplaced.
DR Proteomes; UP000694427; Unplaced.
DR Proteomes; UP000694700; Unplaced.
DR Proteomes; UP000694701; Unplaced.
DR Proteomes; UP001155660; 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:SF5; EPENDYMIN-RELATED; 1.
DR PANTHER; PTHR10697; MAMMALIAN EPENDYMIN-RELATED PROTEIN 1; 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 /evidence="ECO:0000250"
FT CHAIN 21..215
FT /note="Ependymin"
FT /id="PRO_0000008344"
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; 23992 MW; 37007AB6ABDBCBBE CRC64;
MHTVKLLCVV FSCLCAVAWA SSNRQPCHSP PLTSGTMKVV STGGHDLASG EFSYDSKANK
FRFVEDTAHA NKTSHMDVLV HFEEGVLYEI DSKNESCKKE TLQFRKHLME IPPDATHESE
IYMGSPSITE QGLRVRVWNG KLPELHAHYS LSTTSCGCLP VSGSYYGDKK DLLFSFFGVE
TEVDDPQVFV PPAYCEAVAF EEAPDDHSFF DLFHD
//
