LECC_PHYAM
ID LECC_PHYAM Reviewed; 194 AA.
AC Q9AYP9; Q9S9F4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Lectin-C;
DE AltName: Full=PL-C;
DE Flags: Precursor;
OS Phytolacca americana (American pokeweed) (Phytolacca decandra).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Phytolaccaceae; Phytolacca.
OX NCBI_TaxID=3527;
RN [1] {ECO:0000312|EMBL:BAB21577.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mizuta S., Ishiguro M.;
RT "Identification and cDNA cloning of a systemic lectin, PL-C, a major
RT component of pokeweed mitogens.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 45-52, AND FUNCTION.
RX PubMed=7772833; DOI=10.1271/bbb.59.683;
RA Kino M., Yamaguchi K., Umekawa H., Funatsu G.;
RT "Purification and characterization of three mitogenic lectins from the
RT roots of pokeweed (Phytolacca americana).";
RL Biosci. Biotechnol. Biochem. 59:683-688(1995).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 45-170, AND CHITIN-BINDING PROPERTIES.
RC TISSUE=Root {ECO:0000269|PubMed:7670205};
RX PubMed=7670205; DOI=10.1271/bbb.59.1384;
RA Yamaguchi K., Mori A., Funatsu G.;
RT "The complete amino acid sequence of lectin-C from the roots of pokeweed
RT (Phytolacca americana).";
RL Biosci. Biotechnol. Biochem. 59:1384-1385(1995).
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 45-170.
RX PubMed=14623194; DOI=10.1016/j.jmb.2003.09.076;
RA Hayashida M., Fujii T., Hamasu M., Ishiguro M., Hata Y.;
RT "Similarity between protein-protein and protein-carbohydrate interactions,
RT revealed by two crystal structures of lectins from the roots of pokeweed.";
RL J. Mol. Biol. 334:551-565(2003).
CC -!- FUNCTION: N-acetyl-D-glucosamine binding lectin. Almost no
CC hemagglutinating activity towards human erythrocytes. Low mitogenic
CC activity towards human peripheral blood lymphocytes.
CC {ECO:0000269|PubMed:7670205, ECO:0000269|PubMed:7772833}.
CC -!- SUBUNIT: Homodimer. The homodimers are asymmetric; formed in a 'head-
CC to-tail' fashion via hydrophobic interactions between aromatic residues
CC of the carbohydrate-binding sites of each subunit.
CC {ECO:0000269|PubMed:14623194}.
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DR EMBL; AB052963; BAB21577.1; -; mRNA.
DR PDB; 1ULK; X-ray; 1.80 A; A/B=45-170.
DR PDBsum; 1ULK; -.
DR AlphaFoldDB; Q9AYP9; -.
DR SMR; Q9AYP9; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR UniLectin; Q9AYP9; -.
DR EvolutionaryTrace; Q9AYP9; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR Gene3D; 3.30.60.10; -; 3.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR Pfam; PF00187; Chitin_bind_1; 3.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 3.
DR SUPFAM; SSF57016; SSF57016; 3.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Chitin-binding; Direct protein sequencing; Disulfide bond;
KW Lectin; Mitogen; Repeat; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..44
FT /note="Removed in mature form"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:7670205"
FT /id="PRO_0000005271"
FT CHAIN 45..170
FT /note="Lectin-C"
FT /evidence="ECO:0000269|PubMed:7670205"
FT /id="PRO_0000005272"
FT PROPEP 171..194
FT /note="Removed in mature form"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:7670205"
FT /id="PRO_0000005273"
FT DOMAIN 45..86
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 87..127
FT /note="Chitin-binding type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 128..168
FT /note="Chitin-binding type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 48..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 57..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 62..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 80..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 89..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 98..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 103..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 121..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 130..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 139..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 144..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT DISULFID 162..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1ULK"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1ULK"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1ULK"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:1ULK"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:1ULK"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1ULK"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1ULK"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1ULK"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:1ULK"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:1ULK"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1ULK"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1ULK"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1ULK"
SQ SEQUENCE 194 AA; 21042 MW; 8FA0C697AF82563A CRC64;
MKRSNSIAVM LVLVLSSLML LLPVEGQGHE GHGVGEILLM GKLGAPVCGV RASGRVCPDG
YCCSQWGYCG TTEEYCGKGC QSQCDYNRCG KEFGGKECHD ELCCSQYGWC GNSDGHCGEG
CQSQCSYWRC GKDFGGRLCT EDMCCSQYGW CGLTDDHCED GCQSQCDLPT LLPSPLRRII
AIRKLKANLA NMLS
