ID   EPDR2_HALAI             Reviewed;         201 AA.
AC   P86729;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Ependymin-related protein 2;
DE   Flags: Precursor;
OS   Haliotis asinina (Donkey's ear abalone) (Ass's ear abalone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=109174;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Larva {ECO:0000269|PubMed:19207244};
RX   PubMed=19207244; DOI=10.1111/j.1365-294x.2008.04078.x;
RA   Williams E.A., Degnan B.M., Gunter H., Jackson D.J., Woodcroft B.J.,
RA   Degnan S.M.;
RT   "Widespread transcriptional changes pre-empt the critical pelagic-benthic
RT   transition in the vetigastropod Haliotis asinina.";
RL   Mol. Ecol. 18:1006-1025(2009).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 45-64 AND 81-91, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Shell {ECO:0000269|PubMed:21050442};
RX   PubMed=21050442; DOI=10.1186/1477-5956-8-54;
RA   Marie B., Marie A., Jackson D.J., Dubost L., Degnan B.M., Milet C.,
RA   Marin F.;
RT   "Proteomic analysis of the organic matrix of the abalone Haliotis asinina
RT   calcified shell.";
RL   Proteome Sci. 8:54-54(2010).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21050442}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-soluble and acid-insoluble
CC       organic matrix of calcified shell layers (at protein level).
CC       {ECO:0000269|PubMed:21050442}.
CC   -!- SIMILARITY: Belongs to the ependymin family. {ECO:0000255}.
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DR   EMBL; GD272908; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86729; -.
DR   SMR; P86729; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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   PANTHER; PTHR10697; PTHR10697; 1.
DR   Pfam; PF00811; Ependymin; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..201
FT                   /note="Ependymin-related protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000399463"
FT   MOTIF           199..201
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   201 AA;  22614 MW;  7252321F13DCC2E8 CRC64;
     MILQVVLLLA CLSGAIVSTG ACCPPSRFNA FQYVTIVNST TRTRGLYYMV YDGPNERYLL
     TGDRLKNLYG TTRVIYDYKK GIAYNIDVQK RSCTTFPLHG KFEDQENVCV PRDAVYTGRS
     AYGFDQGALH SWSYEYNRTH PDGRHQNIET TVTKENCIPI VTTTISTDAS GGNSLHILGY
     NDFYPGIRDI SMLEIPSYCR A