ID   ELDP2_PINMA             Reviewed;         357 AA.
AC   P86954;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=EGF-like domain-containing protein 2;
DE   Flags: Precursor;
OS   Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=104660;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|PubMed:19915030};
RX   PubMed=19915030; DOI=10.1093/molbev/msp278;
RA   Jackson D.J., McDougall C., Woodcroft B., Moase P., Rose R.A., Kube M.,
RA   Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C., Piquemal D.,
RA   Degnan B.M.;
RT   "Parallel evolution of nacre building gene sets in molluscs.";
RL   Mol. Biol. Evol. 27:591-608(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 143-157; 192-200 AND 282-299, SUBCELLULAR LOCATION, AND
RP   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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=GT283272; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; GT278471; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT278612; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT279486; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT279809; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT280125; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT280369; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281301; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281537; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281820; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT282070; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT283253; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT283272; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ420190; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86954; -.
DR   PRIDE; P86954; -.
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..357
FT                   /note="EGF-like domain-containing protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000413071"
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"
FT   CONFLICT        173
FT                   /note="V -> M (in Ref. 1; GT283272)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="H -> P (in Ref. 1; GT283272)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="D -> E (in Ref. 1; GT278612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="R -> K (in Ref. 1; GT281537)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  39637 MW;  C6D3EC1B3CE1D0F7 CRC64;
     MPPSLSHLFL LSTFASLALC SFYCKNPGYP CLNGGTCLYN GECNCTSGFR GFNCGLDSST
     ISAACTVECH NKGICFNGDK CYCTKDYMGP TCQQAYDFAD CNKSSMKIKA YRPTEFNGEI
     FLMQSMFGCK LTEVTSTIPG YKQYELDVPH DSTGPCKLKK TIDATTGDVH FEVNVSTIHH
     AGQFGMYDGL KTVSCHYSSR DQAIVKDVTN HELLVSVTTS DGNTQNIQEI QTNDVIHLTF
     NPVNLPGGYK GVKILDLEMY SVQWNEVNSI LLLKDQCMTQ KADELGYSVS NEVDGYSGRA
     ILKAIPLFEN VQASVYFNYR LRFCRNRCKI KSCPSQSPKP MPMGEIFKHQ GQGIRIV