EPD2_SALSA
ID EPD2_SALSA Reviewed; 221 AA.
AC P28772;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ependymin-2;
DE AltName: Full=Ependymin II;
DE Short=EPD-II;
DE Flags: Precursor;
GN Name=epd2;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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; M93699; AAA49551.1; -; Genomic_DNA.
DR AlphaFoldDB; P28772; -.
DR SMR; P28772; -.
DR OMA; MSVTMGC; -.
DR Proteomes; UP000087266; Genome assembly.
DR Bgee; ENSSSAG00000073991; Expressed in brain and 4 other tissues.
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; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..221
FT /note="Ependymin-2"
FT /id="PRO_0000008350"
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; 24510 MW; CB9474FECFC554B3 CRC64;
MQDFAFAALS IWLCLGATAL AESHGPQHCT SPNMTGVLTV MALTGGEIKA TGHYSYDSTD
KKLRFTESEM HLNKTEHLED YLMLFEEGVF YDIDMKNQSC KKMSLHSHAH ALELPAGAAH
QVELFLGSDT VQEENIKVNI WMGSVAETKG QYSVLTTVGE CLPLSTFYST DSITLLFSNS
EVVTEVKAPE MFTLPSFCEA VELEETPKGQ KNDFFNIFNT V