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Database: UniProt
Entry: P86953
LinkDB: P86953
Original site: P86953 
ID   ELDP1_PINMA             Reviewed;         348 AA.
AC   P86953;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   15-FEB-2017, entry version 14.
DE   RecName: Full=EGF-like domain-containing protein 1;
DE   Flags: Precursor; Fragment;
OS   Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl
OS   oyster).
OC   Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia;
OC   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.,
RA   Kube M., Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C.,
RA   Piquemal D., 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 32-55; 146-157 AND 187-215, SUBCELLULAR LOCATION,
RP   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.,
RA   Montagnani C.;
RT   "Different secretory repertoires control the biomineralization
RT   processes of 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
CC       edge and lower level in the mantle pallium.
CC       {ECO:0000269|PubMed:23213212}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=GT282449; Type=Frameshift; Positions=196; Evidence={ECO:0000305};
DR   EMBL; GT278041; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT282449; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT284230; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ420398; -; NOT_ANNOTATED_CDS; mRNA.
DR   PRIDE; P86953; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR013032; EGF-like_CS.
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       {ECO:0000255}.
FT   CHAIN        20    348       EGF-like domain-containing protein 1.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000413070.
FT   DOMAIN       60     92       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       99    342       ZP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00375}.
FT   DISULFID     64     74       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     68     80       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     82     91       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CONFLICT    159    159       H -> R (in Ref. 1; GT278041).
FT                                {ECO:0000305}.
FT   CONFLICT    162    162       I -> M (in Ref. 1; EZ420398/GT278041).
FT                                {ECO:0000305}.
FT   NON_TER     348    348       {ECO:0000305}.
SQ   SEQUENCE   348 AA;  38362 MW;  78A2C7C8035401AE CRC64;
     MFYLSTFMTI VISLSLVSCS YDCNNPGYSC KGTCHYYGPC ICNEKLMGYD CSVLKSRMST
     GSNCTVTCQN NGKCYDGSKC LCSSDYTGDL CEKQTTGARC TLDAVVFEAY RPIGFVGETY
     LSQSRSCKLL ETTSDVPGMI KFERKIFHGD TSMCGLKKHM DIPSAGDVTY EADIYSTFQY
     NSWGTRDFMD NVKCQYKPTR VGLSMDAPDS LFPIKMSARD GASSNVQATT QSAPISLLFS
     PQNIPDVKGA MVDYLEVYSI NSTSKEYKSV VAVKNGCAQK NEYNVAFSNL DELDPATSKW
     IGLVKMQAFI IFENEPILFN YRLRFCPDRC TTPTCAAPXV GQATSAAV
//
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