ML3_VISAL
ID ML3_VISAL Reviewed; 569 AA.
AC P82683; P87800; Q6H268; Q6H269; Q8RXH7; Q9S7D0;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Beta-galactoside-specific lectin 3;
DE AltName: Full=Beta-galactoside-specific lectin II;
DE AltName: Full=Beta-galactoside-specific lectin III;
DE Contains:
DE RecName: Full=Beta-galactoside-specific lectin 3 chain A isoform 1;
DE EC=3.2.2.22;
DE AltName: Full=Beta-galactoside-specific lectin III chain A isoform 1;
DE AltName: Full=Lectin chain A isoform 2;
DE AltName: Full=ML-3 A;
DE AltName: Full=ML-III A;
DE AltName: Full=rRNA N-glycosidase;
DE Contains:
DE RecName: Full=Beta-galactoside-specific lectin 3 chain B;
DE AltName: Full=Beta-galactoside-specific lectin III chain B;
DE AltName: Full=ML-3 B;
DE AltName: Full=ML-III B;
DE Flags: Precursor;
OS Viscum album (European mistletoe).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Santalales; Viscaceae; Viscum.
OX NCBI_TaxID=3972;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC TISSUE=Leaf;
RX PubMed=15182350; DOI=10.1111/j.1432-1033.2004.04153.x;
RA Kourmanova A.G., Soudarkina O.J., Olsnes S., Kozlov J.V.;
RT "Cloning and characterization of the genes encoding toxic lectins in
RT mistletoe (Viscum album L).";
RL Eur. J. Biochem. 271:2350-2360(2004).
RN [2]
RP PROTEIN SEQUENCE OF 34-287, AND VARIANTS ARG-127; THR-131 AND ALA-138.
RX PubMed=15113086; DOI=10.1002/psc.505;
RA Wacker R., Stoeva S., Pfuller K., Pfuller U., Voelter W.;
RT "Complete structure determination of the A chain of mistletoe lectin III
RT from Viscum album L. ssp. album.";
RL J. Pept. Sci. 10:138-148(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-282, PROTEIN SEQUENCE OF 34-53, AND
RP FUNCTION.
RC TISSUE=Leaf;
RX PubMed=15001393; DOI=10.1016/j.abb.2003.12.033;
RA Mishra V., Sharma R.S., Yadav S., Babu C.R., Singh T.P.;
RT "Purification and characterization of four isoforms of Himalayan mistletoe
RT ribosome-inactivating protein from Viscum album having unique sugar
RT affinity.";
RL Arch. Biochem. Biophys. 423:288-301(2004).
RN [4]
RP PROTEIN SEQUENCE OF 34-62, AND FUNCTION.
RX PubMed=1450445; DOI=10.1097/00001813-199210000-00010;
RA Dietrich J.B., Ribereau-Gayon G., Jung M.L., Franz H., Beck J.P., Anton R.;
RT "Identity of the N-terminal sequences of the three A chains of mistletoe
RT (Viscum album L.) lectins: homology with ricin-like plant toxins and
RT single-chain ribosome-inhibiting proteins.";
RL Anticancer Drugs 3:507-511(1992).
RN [5]
RP PROTEIN SEQUENCE OF 308-569, VARIANTS PHE-358; LEU-430 AND PHE-569, AND
RP GLYCOSYLATION AT ASN-402 AND ASN-442.
RC TISSUE=Leaf;
RX PubMed=15635663; DOI=10.1002/psc.627;
RA Wacker R., Stoeva S., Betzel C., Voelter W.;
RT "Complete structure determination of N-acetyl-D-galactosamine-binding
RT mistletoe lectin-3 from Viscum album L. album.";
RL J. Pept. Sci. 11:289-302(2005).
CC -!- FUNCTION: The A chain is responsible for inhibiting protein synthesis
CC through the catalytic inactivation of 60S ribosomal subunits by
CC removing adenine from position 4,324 of 28S rRNA. The B chain binds to
CC cell receptors and probably facilitates the entry into the cell of the
CC A chain; B chains are also responsible for cell agglutination (lectin
CC activity). Inhibits growth of the human tumor cell line Molt4.
CC {ECO:0000269|PubMed:1450445, ECO:0000269|PubMed:15001393,
CC ECO:0000269|PubMed:15182350}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC adenosine on the 28S rRNA.; EC=3.2.2.22;
CC -!- SUBUNIT: Disulfide-linked dimer of A and B chains.
CC -!- MISCELLANEOUS: Several isoforms exist.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; AY377892; AAR25547.1; -; Genomic_DNA.
DR EMBL; AY377893; AAR25548.1; -; mRNA.
DR EMBL; AY081148; AAL87005.1; -; mRNA.
DR AlphaFoldDB; P82683; -.
DR SMR; P82683; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR iPTMnet; P82683; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 3.40.420.10; -; 1.
DR Gene3D; 4.10.470.10; -; 1.
DR InterPro; IPR036041; Ribosome-inact_prot_sf.
DR InterPro; IPR017989; Ribosome_inactivat_1/2.
DR InterPro; IPR001574; Ribosome_inactivat_prot.
DR InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR33453; PTHR33453; 2.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF50370; SSF50370; 2.
DR SUPFAM; SSF56371; SSF56371; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Lectin;
KW Plant defense; Protein synthesis inhibitor; Repeat; Signal; Toxin.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:1450445,
FT ECO:0000269|PubMed:15001393, ECO:0000269|PubMed:15113086"
FT CHAIN 34..287
FT /note="Beta-galactoside-specific lectin 3 chain A isoform
FT 1"
FT /id="PRO_0000221393"
FT PROPEP 288..307
FT /note="Connecting peptide"
FT /evidence="ECO:0000269|PubMed:15635663"
FT /id="PRO_0000284729"
FT CHAIN 308..569
FT /note="Beta-galactoside-specific lectin 3 chain B"
FT /id="PRO_0000221394"
FT DOMAIN 314..441
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 445..568
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT BINDING 329..331
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT BINDING 541..543
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15635663"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15635663"
FT DISULFID 280..311
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000305"
FT DISULFID 327..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 370..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 458..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 497..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VARIANT 127
FT /note="D -> R"
FT /evidence="ECO:0000269|PubMed:15113086"
FT VARIANT 131
FT /note="R -> T"
FT /evidence="ECO:0000269|PubMed:15113086"
FT VARIANT 138
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:15113086"
FT VARIANT 358
FT /note="I -> F"
FT /evidence="ECO:0000269|PubMed:15635663"
FT VARIANT 430
FT /note="Q -> L"
FT /evidence="ECO:0000269|PubMed:15635663"
FT VARIANT 569
FT /note="P -> F"
FT /evidence="ECO:0000269|PubMed:15635663"
FT CONFLICT 9
FT /note="G -> R (in Ref. 1; AAR25548)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="I -> M (in Ref. 1; AAR25548)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="A -> R (in Ref. 1; AAR25548)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="D -> E (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="Q -> E (in Ref. 3; AAL87005)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="I -> V (in Ref. 1; AAR25548)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> Y (in Ref. 1; AAR25548)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..282
FT /note="RD -> GE (in Ref. 2; AA sequence and 3; AAL87005)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="T -> K (in Ref. 1; AAR25548 and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="C -> S (in Ref. 1; AAR25548)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="A -> S (in Ref. 1; AAR25548 and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="N -> K (in Ref. 1; AAR25548)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="V -> L (in Ref. 1; AAR25548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 62686 MW; 7860722EA6425D3E CRC64;
MNAVMDSRGA WVSCFLILGL VFGATVKAET KFSYERLRLR VTHQTTGDEY FRFITLLRDY
VSSGSFSNEI PLLRQSTIPV SDAQRFVLVE LTNQGGDSIT AAIDVTNLYV VAYQAGDQSY
FLRDAPDGAE RHLFTGTTRS SLPFTGSYTD LERYAGHRDQ IPLGIEELIQ SVSALRYPGG
STRAQARSII ILIQMISEAA RFNPIFWRVR QDINSGESFL PDMYMLELET SWGQQSTQVQ
QSTDGVFNNP FRLAISTGNF VTLSNVRDVI ASLAIMLFVC RDRPSSSEVR YWPLVIRPVL
ENSGAVDDVT CTASEPTVRI VGRDGLCVDV RDGKFHNGNP IQLSPCKSNT DPNQLWTIRR
DGTIRSNGRC LTTYGYTAGV YVMIFDCNTA VREATLWQIW GNGTIINPRS NLVLGAASGS
SGTTLTVQTQ VYSLGQGWLA GNDTAPREVT IYGFRDLCME ANGASVWVET CGSSTENQNW
ALYGDGSIRP KQNQDQCLTC QGDSVATVIN IVSCSAGSSG QRWVFTNEGT ILNLNNGLVM
DVAQSNPSLR RIIIYPATGN PNQMWLPVP
