GenomeNet

Database: UniProt
Entry: H2A0L3
LinkDB: H2A0L3
Original site: H2A0L3 
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   07-NOV-2018, entry version 16.
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; 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 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.,
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; HE610380; CCE46154.1; -; mRNA.
DR   SMR; H2A0L3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR013032; EGF-like_CS.
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       {ECO:0000255}.
FT   CHAIN        21    359       EGF-like domain containing protein 2.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000417947.
FT   DOMAIN       21     55       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       61     93       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID     24     37       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     31     43       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     45     54       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     65     75       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     69     81       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     83     92       {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
//
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