PWAPL_LOTGI
ID PWAPL_LOTGI Reviewed; 225 AA.
AC B3A0S1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Perlwapin-like protein;
DE Flags: Precursor; Fragment;
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 117-131, 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-soluble organic matrix of
CC calcified layers of the shell (at protein level).
CC {ECO:0000269|PubMed:23145877}.
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DR EMBL; FC634663; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B3A0S1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR InterPro; IPR008197; WAP_dom.
DR PROSITE; PS51390; WAP; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..225
FT /note="Perlwapin-like protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000415260"
FT DOMAIN 27..68
FT /note="WAP 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 117..169
FT /note="WAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT REGION 176..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..57
FT /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 36..61
FT /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 43..56
FT /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 49..65
FT /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 125..157
FT /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 135..161
FT /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 143..156
FT /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 149..165
FT /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT NON_TER 225
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 24775 MW; F7D6CE7F2B96CDED CRC64;
MNHLWLFIVT VSCIYLVYGQ GEESVPCKVK FMGTACPLGR LVCEEDGDCL GVNQVCCYDG
CGTTCHNKTT TLIPSTTQPQ IQPIIPSTQP QIQPIIPSTQ PQIQPFIPST QPQIQRIIPS
PELLCPVVTV RYAFCRFSTY TPCHTSNDCA VPGMKCCPDV CGKRCKFPIN STDHQQFQQT
PLKPTVPLPQ YQQTPLQPTV PSSQPPLQPT VPSPQSYNYK GACST