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   25-MAY-2022, entry version 20.
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; Spiralia; 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 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 of
CC       calcified layers of the shell (at protein level).
CC       {ECO:0000269|PubMed:23145877}.
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DR   EMBL; FC622605; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC627201; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC631303; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3A0S3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Glycoprotein;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..489
FT                   /note="EGF-like domain-containing protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000415254"
FT   DOMAIN          73..109
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          116..370
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   REGION          358..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..376
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        81..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        99..108
FT                   /evidence="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