ID   SCP2_LOTGI              Reviewed;         318 AA.
AC   B3A0P8;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=SCP domain-containing protein 2;
DE   AltName: Full=Uncharacterized shell protein 3;
DE            Short=LUSP-3;
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 95-116; 126-151; 188-218; 229-261 AND 298-317,
RP   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 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; FC620500; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC628872; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_009057011.1; XM_009058763.1.
DR   AlphaFoldDB; B3A0P8; -.
DR   SMR; B3A0P8; -.
DR   EnsemblMetazoa; LotgiT233200; LotgiP233200; LotgiG233200.
DR   GeneID; 20249178; -.
DR   KEGG; lgi:LOTGIDRAFT_233200; -.
DR   CTD; 20249178; -.
DR   HOGENOM; CLU_1016661_0_0_1; -.
DR   OrthoDB; 1528782at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..318
FT                   /note="SCP domain-containing protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000415258"
FT   DOMAIN          158..272
FT                   /note="SCP"
FT                   /evidence="ECO:0000255"
FT   REGION          27..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  35355 MW;  8927E10B762F5D1A CRC64;
     MNFRVVFLTV FLSVPFCCCQ NVTELSGTSP NGSSLSGTNQ NSEPQKGVIN AGSTPSSGTL
     SIASLQAMLA TLMMTNKQTV AAASKPTVTN TGSKQPTATG QPTLSQPRKQ LILTNRRRNP
     RRWGRVFIDN KSNLCAFERQ NFLNSFGLHD KLKKDIVENL NKIRKDVKAQ NMNCLLWSEK
     LAAKAAKLVK ECTYQNTNKA AITSMVYEKE IGDQLVGRSL SRWMDNKKYF SYGNDCRDTG
     GCQFSQIVWA RSKIIGCAAE RCSDMTNMVC LFEPKGNVRN ELPYLTGNQC AQCSASRGST
     PTCNKDKLCE WYFPRPKF