ML4_VISAL
ID ML4_VISAL Reviewed; 520 AA.
AC Q6ITZ3; Q9S7D0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Beta-galactoside-specific lectin 4;
DE AltName: Full=Beta-galactoside-specific lectin IV;
DE Contains:
DE RecName: Full=Beta-galactoside-specific lectin 4 chain A;
DE EC=3.2.2.22;
DE AltName: Full=Beta-galactoside-specific lectin IV chain A;
DE AltName: Full=ML-4 A;
DE AltName: Full=ML-IV A;
DE AltName: Full=rRNA N-glycosidase;
DE Contains:
DE RecName: Full=Beta-galactoside-specific lectin 4 chain B;
DE AltName: Full=Beta-galactoside-specific lectin IV chain B;
DE AltName: Full=ML-4B;
DE AltName: Full=ML-IV 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:AAT37532.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20, AND FUNCTION.
RC TISSUE=Leaf {ECO:0000269|PubMed:15001393};
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 [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-29, 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 [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-240 AND 266-520, SUBUNIT, AND
RP GLYCOSYLATION AT ASN-107; ASN-357 AND ASN-397.
RX PubMed=10198229; DOI=10.1006/bbrc.1999.0470;
RA Krauspenhaar R., Eschenburg S., Perbandt M., Kornilov V., Konareva N.,
RA Mikailova I., Stoeva S., Wacker R., Maier T., Singh T.P., Mikhailov A.,
RA Voelter W., Betzel C.;
RT "Crystal structure of mistletoe lectin I from Viscum album.";
RL Biochem. Biophys. Res. Commun. 257:418-424(1999).
RN [4] {ECO:0000305, ECO:0000312|PDB:1PC8}
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-240 AND 266-520, SUBUNIT, ACTIVE
RP SITE, AND DISULFIDE BONDS.
RX PubMed=15583377; DOI=10.1107/s0907444904023534;
RA Mishra V., Ethayathulla A.S., Sharma R.S., Yadav S., Krauspenhaar R.,
RA Betzel C., Babu C.R., Singh T.P.;
RT "Structure of a novel ribosome-inactivating protein from a hemi-parasitic
RT plant inhabiting the northwestern Himalayas.";
RL Acta Crystallogr. D 60:2295-2304(2004).
RN [5] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-240 AND 266-520.
RA Mishra V., Bilgrami S., Sharma R.S., Kaur P., Yadav S., Krauspenhaar R.,
RA Betzel C., Voelter W., Babu C.R., Singh T.P.;
RT "Crystal structure of Himalayan mistletoe rip reveals the presence of a
RT natural inhibitor and a new functionally active sugar-binding site.";
RL Submitted (DEC-2004) to the PDB data bank.
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:0000250|UniProtKB:P81446, ECO:0000269|PubMed:1450445,
CC ECO:0000269|PubMed:15001393}.
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:0000269|PubMed:10198229, ECO:0000269|PubMed:15583377}.
CC -!- MISCELLANEOUS: Several isoforms exist. {ECO:0000269|PubMed:15001393}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2
CC RIP subfamily. {ECO:0000255}.
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DR EMBL; AY625281; AAT37532.1; -; mRNA.
DR PDB; 1CE7; X-ray; 2.70 A; A=1-240, B=266-519.
DR PDB; 1PC8; X-ray; 3.80 A; A=1-240, B=266-520.
DR PDB; 1TFM; X-ray; 2.80 A; A=1-240, B=266-520.
DR PDB; 1YF8; X-ray; 2.80 A; A=1-240, B=266-520.
DR PDB; 2MLL; X-ray; 2.70 A; A=1-240, B=266-519.
DR PDBsum; 1CE7; -.
DR PDBsum; 1PC8; -.
DR PDBsum; 1TFM; -.
DR PDBsum; 1YF8; -.
DR PDBsum; 2MLL; -.
DR AlphaFoldDB; Q6ITZ3; -.
DR SMR; Q6ITZ3; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR UniLectin; Q6ITZ3; -.
DR iPTMnet; Q6ITZ3; -.
DR EvolutionaryTrace; Q6ITZ3; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lectin; Plant defense; Protein synthesis inhibitor; Repeat;
KW Toxin.
FT CHAIN 1..240
FT /note="Beta-galactoside-specific lectin 4 chain A"
FT /id="PRO_5000093497"
FT PROPEP 241..265
FT /note="Connecting peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000284730"
FT CHAIN 266..520
FT /note="Beta-galactoside-specific lectin 4 chain B"
FT /id="PRO_5000093498"
FT DOMAIN 269..396
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 400..520
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 159
FT /evidence="ECO:0000269|PubMed:15583377"
FT BINDING 284..286
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000250|UniProtKB:P81446"
FT BINDING 494..496
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000250|UniProtKB:P81446"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10198229"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10198229"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10198229"
FT DISULFID 240..266
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:10198229, ECO:0000269|PubMed:15583377"
FT DISULFID 325..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15583377"
FT DISULFID 413..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15583377"
FT DISULFID 451..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15583377"
FT CONFLICT 5
FT /note="D -> R (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="D -> R (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="S -> H (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="S -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1TFM"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1CE7"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1TFM"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 204..214
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1CE7"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1TFM"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1TFM"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:1CE7"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1CE7"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:1CE7"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:1TFM"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:1TFM"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:1CE7"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:1CE7"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:1CE7"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:1CE7"
SQ SEQUENCE 520 AA; 56957 MW; 4F9561A0BD92A915 CRC64;
YERLDLDVTS QTTGEEYFRF ITLLRDYVSS GSFSNEIPLL RQSGGGVEAA RFVLVELTNE
GGDSITAAID VTNLYVVAYQ AGSQSYFLSG PGTHLFTGTT RSSLPFNGSY PDLEQYAGHR
KQIPLGIDQL IQSVTALRFP GNTRTQARSI LILIQMISEA ARFNPILWRA RQYINSGASF
LPDVYMLELE TSWGQQSTQV QQSTEGVFNN PIRLAIPGNF VTLTNVRDVI ASLAIMLFVC
GERPSSSDVR YWPLVIRPVI ADDVTCSASE PTVRIVGRNG MNVDVRDDDF HDGNQIQLWP
SKSNNDPNQL WTIKRDGTIR SNGSCLTTYG YTAGVYVMIF DCNTAVREAT IWQIWGNGTI
INPRSNLALA ASSGIKGTTL TVQTLDYTLG QGWLAGNDTA PREVTIYGFN DLCMESNGGS
VWVETCVSQQ NDRWALYGDG SIRPEQNQDQ CLTSGRDSVA GINIVSCSGG SSGQRWVFTN
EGAILNLKNG LAMDVANPGL GQIIIYPATG KPNQMWLPVP
