EPD2_CARAU
ID EPD2_CARAU Reviewed; 215 AA.
AC P12958;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Ependymin-2;
DE AltName: Full=Ependymin II;
DE Short=EPD-II;
DE Flags: Precursor;
GN Name=epd2; Synonyms=epn2;
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 [MRNA].
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).
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=AAA49165.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J04986; AAA49165.1; ALT_INIT; mRNA.
DR PIR; A32636; A32636.
DR AlphaFoldDB; P12958; -.
DR SMR; P12958; -.
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-2"
FT /id="PRO_0000008342"
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; 23934 MW; 9F45FC95951B04EF CRC64;
MHTVKLLCVV FSCLCAVAWA SSDRQPCHSP PLISGTMKVV STGGHDLASG EFSYDSKANK
FRFVEDAAHA NKTSHTDVLV HFEEGTLYEI DSKNESCKKE TLQFRKHLME IPPDATHESE
IYMGSPSITE QGLRVRVWSG KLPELHAHYS LSITSCGCLP VSGSYYGDKK DLLFSFFGVE
TEVDDLQVFV PPAYCEGVAF EEAPDDHSFF DLFHD