ID   EPD1_ONCMY              Reviewed;         221 AA.
AC   P28770;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Ependymin-1;
DE   AltName: Full=Ependymin I;
DE            Short=EPD-I;
DE   Flags: Precursor;
GN   Name=epd1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-43.
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=1511892; DOI=10.1016/0378-1119(92)90188-u;
RA   Mueller-Schmid A., Rinder H., Lottspeich F., Gertzen E.-M., Hoffmann W.;
RT   "Ependymins from the cerebrospinal fluid of salmonid fish: gene structure
RT   and molecular characterization.";
RL   Gene 118:189-196(1992).
CC   -!- FUNCTION: May play a role in neural plasticity. May be involved during
CC       axon regeneration.
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; M93697; AAA49399.1; -; mRNA.
DR   PIR; JC1250; JC1250.
DR   RefSeq; NP_001118165.1; NM_001124693.1.
DR   AlphaFoldDB; P28770; -.
DR   SMR; P28770; -.
DR   GeneID; 100136738; -.
DR   KEGG; omy:100136738; -.
DR   CTD; 30199; -.
DR   OrthoDB; 1284695at2759; -.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:1511892"
FT   CHAIN           22..221
FT                   /note="Ependymin-1"
FT                   /id="PRO_0000008348"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   221 AA;  24371 MW;  043D8B21F762A447 CRC64;
     MQAFAVAALS IWLCLGATTL AESHGPQHCT SPNMTGVLTV LALTGGEIKA TGHYSYDSTD
     KKIRFTESEM HLNKTEHLED YLMLFEEGVF YDIDMKNQSC KKMSLHSHAH ALELPAGAAH
     QVELFLGSDT VQEEDIKVNI WTGSVPETKG QYFLSTTVGE CLPLSTFYST DSITLLFSNS
     EVVTEVKAPE VFNLPSFCEG VELEEAPEGQ KNDFFSLFNS V