GenomeNet

Database: UniProt
Entry: B3A0R6
LinkDB: B3A0R6
Original site: B3A0R6 
ID   ELDP1_LOTGI             Reviewed;         513 AA.
AC   B3A0R6;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   10-MAY-2017, entry version 15.
DE   RecName: Full=EGF-like domain-containing protein 1;
DE   AltName: Full=Uncharacterized shell protein 17;
DE            Short=LUSP-17;
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 204-226 AND 265-274, SUBCELLULAR LOCATION, AND
RP   TISSUE 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; FC621435; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC628777; -; NOT_ANNOTATED_CDS; mRNA.
DR   SMR; B3A0R6; -.
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; 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     21       {ECO:0000255}.
FT   CHAIN        22    513       EGF-like domain-containing protein 1.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000415253.
FT   DOMAIN       72    108       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      115    364       ZP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00375}.
FT   COMPBIAS    363    401       Pro-rich. {ECO:0000255}.
FT   CARBOHYD    438    438       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    503    503       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     76     86       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     80     96       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     98    107       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   513 AA;  55793 MW;  FD83B57487C34AB6 CRC64;
     MMHTFLRRLC VVALCLGYIK ASADFDCRRT SQSCVTGTCN DVNGDCDCPT DANGVATHRN
     ADCGLEIAKV VPTALCGPPC LNGGECYEPT VGTYMCMCPE AFYGNKCENP RKKVECSGTE
     ITINYMPIPT FSGDIFILDN RNTPECAFTE ANGMYTATFT YQQCGVTTTN DQPNAGDTSY
     EISAAVRFNA NIERATDMKL TAKCVIDGTG QSNLNDNIGT VSVDQRTDLT EETALTEYQP
     VSFQLQGKNG NPMPVPVNLG DELRIYIPLA DTGRYTKLKI TELQTNNGMV EQDLVMETLI
     FNGCLTDIGE ALVTGDISSD PAIPAIIINF MAFRLRGSPQ VKFDARVQVC EGTDTSCDSV
     VCPSPPQSVP SNPQNIPPAN PQNIPPANPQ NIPPANPQIS PSSSQRKRRA APDNEVILHE
     TLTVLDPRSN EKLRLPHNKS DIKSQQNADP QQCLQSTEIM VMVIVLIVAV VLLLVITTCL
     AVKFMKQRAA QVKIYNPDMP TGNNTVRIPR AAC
//
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