ID   EPDR1_HALAI             Reviewed;         200 AA.
AC   P86734;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Ependymin-related protein 1;
DE   Flags: Precursor;
GN   Name=Sometsuke {ECO:0000303|PubMed:17121673};
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Mantle {ECO:0000269|PubMed:17121673};
RX   PubMed=17121673; DOI=10.1186/1741-7007-4-40;
RA   Jackson D.J., McDougall C., Green K., Simpson F., Woerheide G.,
RA   Degnan B.M.;
RT   "A rapidly evolving secretome builds and patterns a sea shell.";
RL   BMC Biol. 4:40-40(2006).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 43-62; 68-78; 81-88 AND 188-200, SUBCELLULAR LOCATION,
RP   AND TISSUE 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 prismatic shell layers (at protein level). Expressed
CC       discontinuously in the anterior zone of the outer fold of the mantle
CC       where its expression correlates with shell pigmentation.
CC       {ECO:0000269|PubMed:17121673, ECO:0000269|PubMed:21050442}.
CC   -!- SIMILARITY: Belongs to the ependymin family. {ECO:0000255}.
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DR   EMBL; DW986219; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86734; -.
DR   SMR; P86734; -.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..200
FT                   /note="Ependymin-related protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000399462"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   200 AA;  22066 MW;  84A64A27F37D68F4 CRC64;
     MILQAALFLA GLTVVSGSIC CPPKQFNSYQ YVTFVNSTTT IRALYYIVYD GDNQRYLITG
     DRNNKQLVGT TKVIYDYKKR IAYSIDAKAR TCSKFPVQGQ FEDQENVCVP GGAEILGPLF
     YGYNQSRLNS QSYAYNTTSL DGSHHNVVTT VSEDDCVPIV ICTITTGGPG GNSLYTVGYN
     DFYPGIKDIT VFDIPPYCNA