ML2_VISAL
ID ML2_VISAL Reviewed; 567 AA.
AC Q6H266; Q6H265; Q6H267;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Beta-galactoside-specific lectin 2;
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 2 chain A;
DE EC=3.2.2.22;
DE AltName: Full=Beta-galactoside-specific lectin II chain A;
DE AltName: Full=ML-2 A;
DE AltName: Full=ML-II A;
DE AltName: Full=rRNA N-glycosidase;
DE Contains:
DE RecName: Full=Beta-galactoside-specific lectin 2 chain B;
DE AltName: Full=Beta-galactoside-specific lectin II chain B;
DE AltName: Full=ML-2B;
DE AltName: Full=ML-II 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] {ECO:0000305, ECO:0000312|EMBL:AAR25550.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC TISSUE=Leaf {ECO:0000312|EMBL:AAR25550.1};
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).
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). {ECO:0000250|UniProtKB:P81446, 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 Evidence={ECO:0000250|UniProtKB:P81446};
CC -!- SUBUNIT: Disulfide-linked dimer of A and B chains.
CC {ECO:0000250|UniProtKB:P81446}.
CC -!- MISCELLANEOUS: Several isoforms exist. {ECO:0000269|PubMed:15182350}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2
CC RIP subfamily. {ECO:0000255}.
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DR EMBL; AY377894; AAR25549.1; -; Genomic_DNA.
DR EMBL; AY377895; AAR25550.1; -; Genomic_DNA.
DR EMBL; AY377896; AAR25551.1; -; mRNA.
DR AlphaFoldDB; Q6H266; -.
DR SMR; Q6H266; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
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; 1.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lectin; Plant defense;
KW Protein synthesis inhibitor; Repeat; Signal; Toxin.
FT SIGNAL 1..33
FT /evidence="ECO:0000255, ECO:0000312|EMBL:AAR25550.1"
FT CHAIN 34..287
FT /note="Beta-galactoside-specific lectin 2 chain A"
FT /id="PRO_5000092109"
FT PROPEP 288..301
FT /note="Connecting peptide"
FT /evidence="ECO:0000250|UniProtKB:P81446"
FT /id="PRO_0000284728"
FT CHAIN 302..567
FT /note="Beta-galactoside-specific lectin 2 chain B"
FT /id="PRO_5000092110"
FT DOMAIN 309..439
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 443..566
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 198
FT /evidence="ECO:0000250|UniProtKB:Q6ITZ3"
FT BINDING 324..326
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000250|UniProtKB:P81446"
FT BINDING 539..541
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000250|UniProtKB:P81446"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..306
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250|UniProtKB:P81446,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 322..341
FT /evidence="ECO:0000250|UniProtKB:Q6ITZ3,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 365..382
FT /evidence="ECO:0000250|UniProtKB:P81446,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 456..469
FT /evidence="ECO:0000250|UniProtKB:P81446,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 495..512
FT /evidence="ECO:0000250|UniProtKB:P81446,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 18
FT /note="V -> L (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="A -> T (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="S -> T (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="K -> E (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="I -> M (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="W -> G (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="H -> D (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> V (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="V -> I (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="V -> A (in Ref. 1; AAR25551)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="R -> Q (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="R -> H (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 364..365
FT /note="SC -> RF (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="Q -> L (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="D -> Y (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="T -> I (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="S -> T (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="S -> F (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="S -> N (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="V -> M (in Ref. 1; AAR25549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 63410 MW; 5FC57D56848F741F CRC64;
MNARLASSRA WVWCFLMVGL VCGATAKAES KINYRRISLR VTDKTTGDEY FRFITILRDY
VSIGSFSNDI PLLRQSTIPV SDAQRFVLVE LTNQWGDSIT AAIDVTNLYV VAYQAAGQSY
YLRDAPHGAE RHLFTGTTRS SLPFNGSYAD LERYAGHRDR IPLGREPLLR SVSALHYPGG
STRAQASSII IVIQMISEAA RFNPILWRAR QYINRGVSFL PDVYMLELET SWGRQSTQVQ
QSTDGVFNNP IRLGISTGNF VTLSNVRDVI PSLAIMVFVC RDRSSSSDVH NWPLVIRPVM
VDDVTCTTSE PTVRIVGRNG MCLDVRDSDY RDGSRIQLWP CKSNSDPNQL WTIRRDGTIR
SNGSCLTTYG YTAGSYIMMY DCNRAGWDLT TWQIRGNGII FNPRSKMVIG TPSGSRGTRG
TTFTLQTLDD SLGQSWLASN DTAPREVTIY GFRDLCMETS GGRVWVESCV SSKQNQRWAL
YGDGSIRPKP YQDQCLTSQG DSVRSVINLF SCTAGSPRQR WVFTNKGTIL NLKNGLALDV
RESNPSLRQI IIFSVSGNPN QMWLPVP
