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Database: UniProt
Entry: H2A0L2
LinkDB: H2A0L2
Original site: H2A0L2 
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   07-NOV-2018, entry version 16.
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; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia;
OC   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
RT   calcifying 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
RP   281-305, 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.,
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}.
DR   EMBL; HE610379; CCE46153.1; -; mRNA.
DR   ProteinModelPortal; H2A0L2; -.
DR   SMR; H2A0L2; -.
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_0000417946.
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}.
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
//
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