ID   ELDP1_PINMG             Reviewed;         348 AA.
AC   H2A0L2;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=EGF-like domain containing protein 1 {ECO:0000250|UniProtKB:P86953};
DE   Flags: Precursor;
OS   Margaritifera margaritifera (Freshwater pearl mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=102329;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle;
RX   PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA   Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA   Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT   "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT   mantle and shell: focus on biomineralization.";
RL   BMC Genomics 11:613-613(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-55; 100-125; 146-157; 194-215; 220-248 AND 281-305,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA   Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA   Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT   "Different secretory repertoires control the biomineralization processes of
RT   prism and nacre deposition of the pearl oyster shell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC   -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC       Expressed primarily in the mantle with highest level in the mantle edge
CC       and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
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DR   EMBL; HE610379; CCE46153.1; -; mRNA.
DR   AlphaFoldDB; H2A0L2; -.
DR   PRIDE; H2A0L2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR001507; ZP_dom.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..348
FT                   /note="EGF-like domain containing protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417946"
FT   DOMAIN          60..92
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          99..342
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   DISULFID        64..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        68..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        82..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   348 AA;  38479 MW;  6DCEA13DD44EF1A6 CRC64;
     MFYLSTFMTI VISLSLVSCS YDCNNPGFTC HGECHYYGSC ICNERLTGYD CSVLKSSLST
     GSDCKVTCQN NGRCYDGNKC LCSSDYTGHL CEKQTTGARC TLDGVVFEAY RPIGFDGETY
     LSQSRSCKLL QSESDVPGMI KFERKIFHGD TSMCGLKKHM DMPNAGDITY EADIYSTFVY
     NSWGTRDFVD NVKCQYKPTR VGLSMDAPDS LFPIKMSARD GASSNVQATT QSAPISLLFS
     PQNIPDVKGA MVDYMEVYSI NSTSKEYKSV VAVKNGCAQK TEYNVAFDNL DELDPVTSTW
     IGLVKMQAFI IFENEPLLFN YRLRFCPDRC SKPTCAAPAV SQAPSTAV