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   25-MAY-2022, entry version 21.
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; 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 204-226 AND 265-274, 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 of
CC       calcified layers of the shell (at protein level).
CC       {ECO:0000269|PubMed:23145877}.
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DR   EMBL; FC621435; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC628777; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3A0R6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Glycoprotein;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..513
FT                   /note="EGF-like domain-containing protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000415253"
FT   DOMAIN          72..108
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          115..364
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   REGION          356..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..396
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        80..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        98..107
FT                   /evidence="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