EPD_DANRE
ID EPD_DANRE Reviewed; 217 AA.
AC P17561; Q561Y9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ependymin;
DE Short=EPD;
DE Flags: Precursor;
GN Name=epd;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2243597; DOI=10.1016/0306-4522(90)90214-o;
RA Sterrer S., Koenigstorfer A., Hoffmann W.;
RT "Biosynthesis and expression of ependymin homologous sequences in zebrafish
RT brain.";
RL Neuroscience 37:277-284(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1524676; DOI=10.1089/dna.1992.11.425;
RA Rinder H., Bayer T.A., Gertzen E., Hoffmann W.;
RT "Molecular analysis of the ependymin gene and functional test of its
RT promoter region by transient expression in Brachydanio rerio.";
RL DNA Cell Biol. 11:425-432(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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: Binds calcium through the terminal sialic acids.
CC -!- SIMILARITY: Belongs to the ependymin family. {ECO:0000305}.
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DR EMBL; X52502; CAA36742.1; -; mRNA.
DR EMBL; M89643; AAA50026.1; -; Genomic_DNA.
DR EMBL; BC092712; AAH92712.1; -; mRNA.
DR PIR; A43820; A43820.
DR RefSeq; NP_571080.1; NM_131005.2.
DR AlphaFoldDB; P17561; -.
DR SMR; P17561; -.
DR STRING; 7955.ENSDARP00000049894; -.
DR PaxDb; P17561; -.
DR Ensembl; ENSDART00000171617; ENSDARP00000134034; ENSDARG00000103498.
DR GeneID; 30199; -.
DR KEGG; dre:30199; -.
DR CTD; 30199; -.
DR ZFIN; ZDB-GENE-980526-111; epd.
DR eggNOG; ENOG502S4KH; Eukaryota.
DR GeneTree; ENSGT00940000168284; -.
DR HOGENOM; CLU_097673_1_0_1; -.
DR InParanoid; P17561; -.
DR OMA; MSVTMGC; -.
DR OrthoDB; 1284695at2759; -.
DR PhylomeDB; P17561; -.
DR PRO; PR:P17561; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000103498; Expressed in brain and 12 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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..217
FT /note="Ependymin"
FT /id="PRO_0000008340"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 78
FT /note="M -> I (in Ref. 1; CAA36742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24472 MW; 3EED80F2A39FFA43 CRC64;
MHTVKLLCVV FSCLCAIGWA SHHSHRQPCH SPQLTSGTMK VVSTGGHDLA SGEFSYDSKT
NKFRFVEDTT HANKTSYMDV LIHFEEGVLY EIDSKNESCK KETLQFRKHL MEIPVDATHE
SESYMGSPSL TEQGLRVRVW NGKFPELHAH YSLSTTSCGC LTVSGSYYGE KKDLFFSFFG
VETEVDDLQV FAPPAYCEGV SFEEAPDDHS FFDLFHD