PLC_HALLA
ID PLC_HALLA Reviewed; 155 AA.
AC P82596; Q7M4F8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 3.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Perlucin;
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, AND FUNCTION.
RC TISSUE=Shell;
RX PubMed=10931211; DOI=10.1046/j.1432-1327.2000.01602.x;
RA Mann K., Weiss I.M., Andre S., Gabius H.-J., Fritz M.;
RT "The amino-acid sequence of the abalone (Haliotis laevigata) nacre protein
RT perlucin. Detection of a functional C-type lectin domain with
RT galactose/mannose specificity.";
RL Eur. J. Biochem. 267:5257-5264(2000).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-32.
RC TISSUE=Shell;
RX PubMed=10623567; DOI=10.1006/bbrc.1999.1907;
RA Weiss I.M., Kaufmann S., Mann K., Fritz M.;
RT "Purification and characterization of perlucin and perlustrin, two new
RT proteins from the shell of the mollusc Haliotis laevigata.";
RL Biochem. Biophys. Res. Commun. 267:17-21(2000).
CC -!- FUNCTION: May promote nucleation and/or growth of calcium carbonate
CC crystals. Binds to D-galactose and D-mannose/D-glucose.
CC {ECO:0000269|PubMed:10931211}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:10931211}.
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DR PIR; S78774; S78774.
DR AlphaFoldDB; P82596; -.
DR SMR; P82596; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin; Repeat.
FT CHAIN 1..155
FT /note="Perlucin"
FT /id="PRO_0000046722"
FT DOMAIN 9..128
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REPEAT 136..145
FT /note="1"
FT REPEAT 146..155
FT /note="2"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 2..13
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 30..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 102..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 4
FT /note="L -> I"
FT /evidence="ECO:0000269|PubMed:10931211,
FT ECO:0000303|PubMed:10623567"
FT VARIANT 4
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:10931211,
FT ECO:0000303|PubMed:10623567"
FT VARIANT 9
FT /note="N -> H"
FT /evidence="ECO:0000269|PubMed:10931211"
FT VARIANT 11
FT /note="R -> G"
FT /evidence="ECO:0000269|PubMed:10931211,
FT ECO:0000303|PubMed:10623567"
FT VARIANT 20
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:10931211,
FT ECO:0000303|PubMed:10623567"
FT VARIANT 45
FT /note="E -> D"
FT /evidence="ECO:0000269|PubMed:10931211"
FT VARIANT 60
FT /note="F -> V"
FT /evidence="ECO:0000269|PubMed:10931211"
FT VARIANT 61
FT /note="N -> K"
FT /evidence="ECO:0000269|PubMed:10931211"
FT VARIANT 80
FT /note="Q -> E"
FT /evidence="ECO:0000269|PubMed:10931211"
FT VARIANT 131
FT /note="R -> H"
FT /evidence="ECO:0000269|PubMed:10931211"
FT VARIANT 133
FT /note="P -> S"
FT /evidence="ECO:0000269|PubMed:10931211"
FT VARIANT 145
FT /note="R -> M"
FT /evidence="ECO:0000269|PubMed:10931211"
FT VARIANT 155
FT /note="R -> K"
FT /evidence="ECO:0000269|PubMed:10931211"
FT UNSURE 84
SQ SEQUENCE 155 AA; 18155 MW; CBB8AF788B878387 CRC64;
GCPLGFHQNR RSCYWFSTIK SSFAEAAGYC RYLESHLAII SNKDEDSFIR GYATRLGEAF
NYWLGASDLN IEGRWLWEGQ RRMNYTNWSP GQPDNAGGIE HCLELRRDLG NYLWNDYQCQ
KPSHFICEKE RIPYTNSLHA NLQQRDSLHA NLQQR