ID   ELDP2_PINMG             Reviewed;         359 AA.
AC   H2A0L3;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=EGF-like domain containing protein 2 {ECO:0000250|UniProtKB:P86954};
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 51-72; 131-157; 306-322 AND 334-344, SUBCELLULAR
RP   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; HE610380; CCE46154.1; -; mRNA.
DR   AlphaFoldDB; H2A0L3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000742; EGF-like_dom.
DR   SMART; SM00181; EGF; 2.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..359
FT                   /note="EGF-like domain containing protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417947"
FT   DOMAIN          21..55
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          61..93
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        24..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        31..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        45..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        65..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        69..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        83..92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   359 AA;  39659 MW;  AAF474E6B415EA0D CRC64;
     MPPFISHFFL LSTFASLALC SFYCKNPGYP CLNGGTCLYN GECNCTSGFR GFNCGLDSST
     ISAACTVECH NKGICYNGDK CYCTKDYMGP TCQQAYDFAD CNKSSMKIKA YRPTEFNGEM
     FLMQSMFGCK LAEVTSTIAG YKQYELDVPH DSTGPCKLKK TIDATTGDVH FEVNVSTIHH
     AGQFGMYDGL KTVSCHYSSR DQAIVKDVTN QDLIVSVTAS DGSTPNLQEI PSNDVIHLTF
     KPVNLPGGYK AVKILDLEMY SVVEQWNEIN SMVLLKDQCM TQKADELGYS VSNEVDGTSG
     RAILKAIPLF ENVPAPVHFN YRLRFCRNRC ILKSCASPSL KPMPKGEIFK HQGQGIRIV