PWAP_HALAI
ID PWAP_HALAI Reviewed; 152 AA.
AC P86730;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Perlwapin {ECO:0000250|UniProtKB:P84811};
DE Flags: Precursor; Fragment;
OS Haliotis asinina (Donkey's ear abalone) (Ass's ear abalone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX NCBI_TaxID=109174;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mantle {ECO:0000269|PubMed:17121673};
RX PubMed=17121673; DOI=10.1186/1741-7007-4-40;
RA Jackson D.J., McDougall C., Green K., Simpson F., Woerheide G.,
RA Degnan B.M.;
RT "A rapidly evolving secretome builds and patterns a sea shell.";
RL BMC Biol. 4:40-40(2006).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 79-92 AND 138-152, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Shell {ECO:0000269|PubMed:21050442};
RX PubMed=21050442; DOI=10.1186/1477-5956-8-54;
RA Marie B., Marie A., Jackson D.J., Dubost L., Degnan B.M., Milet C.,
RA Marin F.;
RT "Proteomic analysis of the organic matrix of the abalone Haliotis asinina
RT calcified shell.";
RL Proteome Sci. 8:54-54(2010).
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 (By similarity). {ECO:0000250|UniProtKB:P84811}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21050442}.
CC -!- TISSUE SPECIFICITY: Component of the acid-soluble and acid-insoluble
CC organic matrix of prismatic shell layers (at protein level).
CC {ECO:0000269|PubMed:21050442}.
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DR EMBL; DW986256; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P86730; -.
DR SMR; P86730; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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; Secreted; Signal.
FT SIGNAL <1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..152
FT /note="Perlwapin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399445"
FT DOMAIN 19..61
FT /note="WAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 62..107
FT /note="WAP 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 108..150
FT /note="WAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 26..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 35..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 39..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 45..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 69..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 77..100
FT /evidence="ECO:0000250|UniProtKB:P84811,
FT ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 82..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 88..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 112..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 122..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 126..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 132..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 16127 MW; 01FEB3BF5565FD8A CRC64;
LILCVVVCTA AVLGTAAGYE SQLPGCPPGA YPAICARYCY SDRDCASGYY CCNTGCLNIC
VPKPKPGLCP SITQSPCRGN VCNNDQDCPG NRKCCGKPGC KRCYRPKKPG SCPARKYEAG
PCVVYCDGDF DCPGDKKCCG GCPRLCEKPC YD
