ID   TRP_LOTGI               Reviewed;         349 AA.
AC   B3A0R4;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Threonine-rich protein;
DE   AltName: Full=Uncharacterized shell protein 15;
DE            Short=LUSP-15;
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=Larva {ECO:0000269|Ref.1}, and 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 49-56 AND 84-100, 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 and acid-soluble
CC       organic matrix of calcified layers of the shell (at protein level).
CC       {ECO:0000269|PubMed:23145877}.
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DR   EMBL; FC633389; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC771588; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC775354; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_009063264.1; XM_009065016.1.
DR   AlphaFoldDB; B3A0R4; -.
DR   SMR; B3A0R4; -.
DR   EnsemblMetazoa; LotgiT235609; LotgiP235609; LotgiG235609.
DR   GeneID; 20249901; -.
DR   KEGG; lgi:LOTGIDRAFT_235609; -.
DR   CTD; 20249901; -.
DR   HOGENOM; CLU_795215_0_0_1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..349
FT                   /note="Threonine-rich protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000415252"
FT   REGION          300..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          316..349
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        119
FT                   /note="I -> L (in Ref. 1; FC771588)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   349 AA;  39064 MW;  E68F4A550E6AD711 CRC64;
     MKGLTLACIA ATVVAASHAM TTIIAPIAEI STTSSPSTTT INPLLQSRID FEISRLTRRL
     ERRIRGLQVG SGRLDRSITS LQRELDFNNA VLAQLPELIK NIMINNPTQR LSSRTVASIM
     RSVQNAATKA SNEESAEVED RRRRAIFEVT SSIVIVEGTT DSTTTTQIPE VTTQEVDTTT
     EMVTTAAPEQ EVTSTATETT TEMTTQGTTL PSFLVSRINS VVSRIGRFFQ RRIQRIQRSL
     SRLSRFRPLY SRLIDENTSA LNNLPLLVRG LVTSPFQRRL RLSQVFRALR FRLTITTPSQ
     PDVSPMSVRK RRQAESAEED DDLVGDMEDL KELEQEIQEA LEEVEKLDV