ID   EPD_ESOLU               Reviewed;         221 AA.
AC   P32188;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Ependymin;
DE            Short=EPD;
DE   Flags: Precursor;
GN   Name=epd;
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8350351; DOI=10.1007/bf00556362;
RA   Mueller-Schmid A., Ganss B., Gorr T., Hoffmann W.;
RT   "Molecular analysis of ependymins from the cerebrospinal fluid of the
RT   orders Clupeiformes and Salmoniformes: no indication for the existence of
RT   an euteleost infradivision.";
RL   J. Mol. Evol. 36:578-585(1993).
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; L09066; AAA49253.1; -; mRNA.
DR   PIR; I50538; I50538.
DR   RefSeq; NP_001297938.1; NM_001311009.1.
DR   AlphaFoldDB; P32188; -.
DR   STRING; 8010.XP_010895424.1; -.
DR   GeneID; 105025994; -.
DR   KEGG; els:105025994; -.
DR   CTD; 30199; -.
DR   OrthoDB; 1284695at2759; -.
DR   Proteomes; UP000265140; LG25.
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..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..221
FT                   /note="Ependymin"
FT                   /id="PRO_0000008346"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   221 AA;  24480 MW;  9B5E0C21D7B48EBB CRC64;
     MQAFAVAALS IWLCLGATTL AESLAQSHGP QHCTSPNMTG VLTVMALNGG EIKATGHYHY
     DTTDKKLRFT ESDMHLNKSE HLEDYLMLFE EGVFYDIDLK NQSCRKMSLQ SHAHALELPA
     GAVHQVELFL GSDTVQEENI KVNIWMGSVP ETKGQYSVST TVGDCLPLST FYSTDSITLL
     FSNSQVVTEV KEPEVFSLPS FCEGLELEDT HNDFFSIFNT V