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PWAP_HALLA
ID   PWAP_HALLA              Reviewed;         134 AA.
AC   P84811;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Perlwapin;
OS   Haliotis laevigata (Smooth Australian abalone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=36097;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, AND VARIANTS ASP-11;
RP   GLY-12; ARG-12; GLY-TYR-13; ALA-15; ALA-22; ASP-26; ILE-86; VAL-101;
RP   ALA-103; ALA-106; LEU-127 AND ASN-134.
RC   TISSUE=Shell {ECO:0000269|PubMed:16861275};
RX   PubMed=16861275; DOI=10.1529/biophysj.106.086108;
RA   Treccani L., Mann K., Heinemann F., Fritz M.;
RT   "Perlwapin, an abalone nacre protein with three four-disulfide core (whey
RT   acidic protein) domains, inhibits the growth of calcium carbonate
RT   crystals.";
RL   Biophys. J. 91:2601-2608(2006).
CC   -!- FUNCTION: Inhibits growth of calcium carbonate crystals. May inhibit
CC       growth of certain crystallographic planes in the mineral phase of nacre
CC       in the shell. {ECO:0000269|PubMed:16861275}.
CC   -!- TISSUE SPECIFICITY: Nacreous layer of shell.
CC       {ECO:0000269|PubMed:16861275}.
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DR   AlphaFoldDB; P84811; -.
DR   SMR; P84811; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 4.10.75.10; -; 3.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR008197; WAP_dom.
DR   Pfam; PF00095; WAP; 3.
DR   PRINTS; PR00003; 4DISULPHCORE.
DR   SMART; SM00217; WAP; 2.
DR   SUPFAM; SSF57256; SSF57256; 2.
DR   PROSITE; PS51390; WAP; 3.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Repeat.
FT   CHAIN           1..134
FT                   /note="Perlwapin"
FT                   /id="PRO_0000248608"
FT   DOMAIN          2..45
FT                   /note="WAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DOMAIN          46..89
FT                   /note="WAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DOMAIN          90..132
FT                   /note="WAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        8..34
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        17..38
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        21..33
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        27..42
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        51..77
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        59..82
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        64..76
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        70..85
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        94..121
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        104..124
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        108..120
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        114..128
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0L8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00722"
FT   VARIANT         11
FT                   /note="G -> D"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         12
FT                   /note="P -> G"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         12
FT                   /note="P -> R"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         13
FT                   /note="Y -> GY"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         15
FT                   /note="R -> A"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         22
FT                   /note="H -> A"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         26
FT                   /note="E -> D"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         86
FT                   /note="Y -> I"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         101
FT                   /note="A -> V"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         103
FT                   /note="V -> A"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         106
FT                   /note="I -> A"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         127
FT                   /note="R -> L"
FT                   /evidence="ECO:0000269|PubMed:16861275"
FT   VARIANT         134
FT                   /note="D -> N"
FT                   /evidence="ECO:0000269|PubMed:16861275"
SQ   SEQUENCE   134 AA;  14528 MW;  6674C0F28485C79A CRC64;
     YGPNLPGCPP GPYPRICARY CHSDRECKAG YYCCNTGCLN ICVPKPKPGL CPAIRPGPCK
     GNVCSNDQDC PGNQKCCGKP GCRRCYRPEK PGSCPPRKYD AGVCVIYCVG DFDCPGNEKC
     CGSCPRRCEK PCFD
 
 
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