LECB_PHYAM
ID LECB_PHYAM Reviewed; 361 AA.
AC Q9AVB0;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Lectin-B;
DE AltName: Full=PL-B;
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:BAB40792.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mizuta S., Ohnuma T., Yamaguchi K., Ishiguro M.;
RT "Molecular cloning and mass spectrometric analysis of two pokeweed
RT mitogens, PL-B and PL-C: systemic tissue distribution of different classes
RT of pokeweed lectins.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 42-336, DISULFIDE BONDS, AND GLYCOSYLATION.
RC TISSUE=Root {ECO:0000269|PubMed:9145528};
RX PubMed=9145528; DOI=10.1271/bbb.61.690;
RA Yamaguchi K., Yurino N., Kino M., Ishiguro M., Funatsu G.;
RT "The amino acid sequence of mitogenic lectin-B from the roots of pokeweed
RT (Phytolacca americana).";
RL Biosci. Biotechnol. Biochem. 61:690-698(1997).
RN [3] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Root {ECO:0000269|PubMed:7772833};
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 [4] {ECO:0000305}
RP GLYCOSYLATION AT ASN-137 AND ASN-180, AND STRUCTURE OF CARBOHYDRATE ON
RP ASN-137 AND ASN-180.
RC TISSUE=Root {ECO:0000269|PubMed:8901119};
RX PubMed=8901119; DOI=10.1271/bbb.60.537;
RA Kimura Y., Yamaguchi K., Funatsu G.;
RT "Structural analysis of N-linked oligosaccharide of mitogenic lectin-B from
RT the roots of pokeweed (Phytolacca americana).";
RL Biosci. Biotechnol. Biochem. 60:537-540(1996).
CC -!- FUNCTION: N-acetyl-D-glucosamine binding lectin. Has high
CC hemagglutinating activity towards human erythrocytes. Shows potent
CC mitogenic activity towards human peripheral blood lymphocytes.
CC {ECO:0000269|PubMed:7772833, ECO:0000303|PubMed:8901119}.
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DR EMBL; AB059241; BAB40792.1; -; mRNA.
DR PIR; JC5559; JC5559.
DR AlphaFoldDB; Q9AVB0; -.
DR SMR; Q9AVB0; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR iPTMnet; Q9AVB0; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; ISS: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; -; 7.
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; 7.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 7.
DR SUPFAM; SSF57016; SSF57016; 7.
DR PROSITE; PS00026; CHIT_BIND_I_1; 2.
DR PROSITE; PS50941; CHIT_BIND_I_2; 7.
PE 1: Evidence at protein level;
KW Chitin-binding; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lectin; Mitogen; Repeat; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..41
FT /note="Removed in mature form"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:9145528"
FT /id="PRO_0000005268"
FT CHAIN 42..336
FT /note="Lectin-B"
FT /evidence="ECO:0000269|PubMed:9145528"
FT /id="PRO_0000005269"
FT PROPEP 337..361
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:9145528"
FT /id="PRO_0000005270"
FT DOMAIN 42..83
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 84..127
FT /note="Chitin-binding type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 128..170
FT /note="Chitin-binding type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 171..211
FT /note="Chitin-binding type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 212..252
FT /note="Chitin-binding type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 253..293
FT /note="Chitin-binding type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 294..335
FT /note="Chitin-binding type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:8901119,
FT ECO:0000269|PubMed:9145528"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:8901119,
FT ECO:0000269|PubMed:9145528"
FT DISULFID 45..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 54..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 59..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 77..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 87..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 96..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 102..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 120..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 131..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 140..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 145..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 163..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 183..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 188..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 206..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 215..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 224..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 229..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 247..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 256..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 265..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 270..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 288..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 297..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 306..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 311..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 329..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT CONFLICT 252
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39132 MW; 463F667183D7E74B CRC64;
MKRISNSIVG MLVVVLSVML LLPVEGHEGH GVVELIMGKL GAPECGREAS GKVCPDDLCC
SVFGHCGVSV QHCGDGCQSQ CVTNWRCGKD FDDRTCPKKL LCCSKDGWCG NTDAHCGEGC
QSQCEQYNWR CGVDFGNRTC PNDLCCSVGG WCGTTDDHCG EGCQSQCEQY NWHCGVDFGN
RTCPNDLCCS EWGWCGITEG YCGEGCQSQC NHQRCGKDFA GRTCLNDLCC SEWGWCGSSE
AHCGQGCQSN CDYNRCGRNF GFRTCPNELC CSSGGWCGSN DAHCGKGCQS QCDYWRCGVD
FSGRVCPQGR CCSAWGWCGD TEEYCEEGCQ SQCKLSSLPS PLSQILAIRK LNATIPTMAV
E
