GenomeNet

Database: UniProt
Entry: B3A0S3
LinkDB: B3A0S3
Original site: B3A0S3 
ID   ELDP2_LOTGI             Reviewed;         489 AA.
AC   B3A0S3;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   23-MAY-2018, entry version 15.
DE   RecName: Full=EGF-like domain-containing protein 2;
DE   AltName: Full=Uncharacterized shell protein 24;
DE            Short=LUSP-24;
DE   Flags: Precursor;
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|Ref.1};
RA   Richardson P., Lucas S., Rokhsar D., Wang M., Lindquist E.A.;
RT   "DOE Joint Genome Institute Lottia gigantea EST project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 266-275, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23145877; DOI=10.1111/febs.12062;
RA   Marie B., Jackson D.J., Ramos-Silva P., Zanella-Cleon I., Guichard N.,
RA   Marin F.;
RT   "The shell-forming proteome of Lottia gigantea reveals both deep
RT   conservations and lineage-specific novelties.";
RL   FEBS J. 280:214-232(2013).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23145877}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble organic matrix
CC       of calcified layers of the shell (at protein level).
CC       {ECO:0000269|PubMed:23145877}.
DR   EMBL; FC622605; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC627201; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC631303; -; NOT_ANNOTATED_CDS; mRNA.
DR   PRIDE; B3A0S3; -.
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   SMART; SM00181; EGF; 2.
DR   SMART; SM00241; ZP; 1.
DR   PROSITE; PS00022; EGF_1; 1.
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;
KW   Glycoprotein; Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    489       EGF-like domain-containing protein 2.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000415254.
FT   DOMAIN       73    109       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      116    370       ZP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00375}.
FT   CARBOHYD    229    229       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    414    414       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    479    479       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     77     87       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     81     97       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     99    108       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   489 AA;  52888 MW;  8F73E6AA1E7AB8FB CRC64;
     MMQTLLRGLC VVVLFWGYIK ASADFDCRRT SQTCVTGTCD DVSGSCVCPT DAGGSPSHTN
     KDCGLELAKV ASPATLCDPP CLNGGQCFEP TADTYMCMCS EAFYGSQCEN PRKQVECSGD
     QITINYMPIP TFSGDIFILD NRNTPECAFT EANGMYTATF TYQQCGVITT NDQPNVGDTS
     YQTSAAVRFN ANIERGTDMK LTAECVIDGS GQSNLNNNIG TVSVDQRSNL TEETALTQYQ
     PVSFQLQGKN GNPMPVPVNL GDELRIYIPL ADTGKYTKLK ITDLTTNNGM AAPDMVTETL
     IFNGCLTDIG EALVTGDISS DPAIPAIIIN FMAFRLRGSP QVKFEAKVKV CEAADTSCEP
     GSCPTPAPPA PVQPTPSENP GRKRRAASDN EVILHETLTV LDPRSNEKLR LPHNKSDKKS
     QQNADPQQCL QSTEIMVMVI VLIVAVVLLL VITTCLAVKF MKQRAAQVKI YNSDMPTGNN
     TVRIPHSAF
//
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