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UniProtKB - P81446 (ML1_VISAL)
Protein
Beta-galactoside-specific lectin 1
Gene
N/A
Organism
Viscum album (European mistletoe)
Status
Functioni
The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.
3 PublicationsMiscellaneous
Several isoforms exist.
Catalytic activityi
- Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. EC:3.2.2.22
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 198 | By similarity | 1 |
GO - Molecular functioni
- carbohydrate binding Source: UniProtKB-KW
- rRNA N-glycosylase activity Source: UniProtKB-EC
- toxin activity Source: UniProtKB-KW
GO - Biological processi
- defense response Source: UniProtKB-KW
- negative regulation of translation Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase, Protein synthesis inhibitor, Toxin |
Biological process | Plant defense |
Ligand | Lectin |
Enzyme and pathway databases
BRENDAi | 3.2.2.22, 6669 |
Protein family/group databases
CAZyi | CBM13, Carbohydrate-Binding Module Family 13 |
UniLectini | P81446 |
Names & Taxonomyi
Protein namesi | Recommended name: Beta-galactoside-specific lectin 1Alternative name(s): Beta-galactoside-specific lectin I Viscumin Cleaved into the following 2 chains: Alternative name(s): Beta-galactoside-specific lectin I chain A isoform 1 ML-I A Short name: MLA rRNA N-glycosidase Alternative name(s): Beta-galactoside-specific lectin I chain B ML-I B Short name: MLB |
Organismi | Viscum album (European mistletoe) |
Taxonomic identifieri | 3972 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › Santalales › Viscaceae › Viscum |
Pathology & Biotechi
Pharmaceutical usei
Due to its immunomodulative effects it is being studied in clinical trials in cancer patients as it may slow the growth of cancer cells and be an effective treatment for solid tumors.
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 33 | 3 PublicationsAdd BLAST | 33 | |
ChainiPRO_0000030749 | 34 – 287 | Beta-galactoside-specific lectin 1 chain A isoform 1Add BLAST | 254 | |
PropeptideiPRO_0000030750 | 288 – 301 | Connecting peptide1 PublicationAdd BLAST | 14 | |
ChainiPRO_0000030751 | 302 – 564 | Beta-galactoside-specific lectin 1 chain BAdd BLAST | 263 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 145 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 280 ↔ 306 | Interchain (between A and B chains)PROSITE-ProRule annotation1 Publication | ||
Glycosylationi | 362 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 365 ↔ 382 | PROSITE-ProRule annotation1 Publication | ||
Glycosylationi | 397 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 437 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 453 ↔ 466 | PROSITE-ProRule annotation1 Publication | ||
Disulfide bondi | 492 ↔ 509 | PROSITE-ProRule annotation1 Publication |
Post-translational modificationi
The A chain of variant MLA' is not glycosylated.1 Publication
Keywords - PTMi
Disulfide bond, GlycoproteinPTM databases
iPTMneti | P81446 |
Interactioni
Subunit structurei
Disulfide-linked dimer of A and B chains.
3 PublicationsStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P81446 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P81446 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 309 – 436 | Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST | 128 | |
Domaini | 440 – 564 | Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST | 125 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 324 – 326 | Galactose binding | 3 | |
Regioni | 536 – 538 | Galactose binding | 3 |
Sequence similaritiesi
Keywords - Domaini
Repeat, SignalFamily and domain databases
CDDi | cd00161, RICIN, 2 hits |
Gene3Di | 3.40.420.10, 1 hit 4.10.470.10, 1 hit |
InterProi | View protein in InterPro IPR036041, Ribosome-inact_prot_sf IPR017989, Ribosome_inactivat_1/2 IPR001574, Ribosome_inactivat_prot IPR016138, Ribosome_inactivat_prot_sub1 IPR016139, Ribosome_inactivat_prot_sub2 IPR035992, Ricin_B-like_lectins IPR000772, Ricin_B_lectin |
PANTHERi | PTHR33453, PTHR33453, 1 hit |
Pfami | View protein in Pfam PF00652, Ricin_B_lectin, 2 hits PF00161, RIP, 1 hit |
PRINTSi | PR00396, SHIGARICIN |
SMARTi | View protein in SMART SM00458, RICIN, 2 hits |
SUPFAMi | SSF50370, SSF50370, 2 hits SSF56371, SSF56371, 1 hit |
PROSITEi | View protein in PROSITE PS50231, RICIN_B_LECTIN, 2 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P81446-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNGHLASRRA WVWYFLMLGQ VFGATVKAET KFSYERLRLR VTHQTTGEEY
60 70 80 90 100
FRFITLLRDY VSSGSFSNEI PLLRQSTIPV SDAQRFVLVE LTNEGGDSIT
110 120 130 140 150
AAIDVTNLYV VAYQAGDQSY FLRDAPRGAE THLFTGTTRS SLPFNGSYPD
160 170 180 190 200
LERYAGHRDQ IPLGIDQLIQ SVTALRFPGG STRTQARSIL ILIQMISEAA
210 220 230 240 250
RFNPILWRAR QYINSGASFL PDVYMLELET SWGQQSTQVQ QSTDGVFNNP
260 270 280 290 300
IRLAIPPGNF VTLTNVRDVI ASLAIMLFVC GERPSSSDVR YWPLVIRPVI
310 320 330 340 350
ADDVTCSASE PTVRIVGRNG MCVDVRDDDF HDGNQIQLWP SKSNNDPNQL
360 370 380 390 400
WTIKRDGTIR SNGSCLTTYG YTAGVYVMIF DCNTAVREAT LWEIWGNGTI
410 420 430 440 450
INPRSNLVLA ASSGIKGTTL TVQTLDYTLG QGWLAGNDTA PREVTIYGFR
460 470 480 490 500
DLCMESNGGS VWVETCVISQ QNQRWALYGD GSIRPKQNQD QCLTCGRDSV
510 520 530 540 550
STVINIVSCS AGSSGQRWVF TNEGAILNLK NGLAMDVAQA NPKLRRIIIY
560
PATGKPNQMW LPVP
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 3 | G → A in AAR25545 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 19 – 20 | GQ → CL in AAR25545 (PubMed:15182350).Curated | 2 | |
Sequence conflicti | 37 | L → I in AAR25546 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 62 | S → G AA sequence (PubMed:1450445).Curated | 1 | |
Sequence conflicti | 83 | A → T in AAR25546 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 92 | T → S in AAR25546 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 94 | E → Q in AAR25545 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 94 | E → Q AA sequence (PubMed:8980141).Curated | 1 | |
Sequence conflicti | 94 | E → Q (PubMed:12823544).Curated | 1 | |
Sequence conflicti | 96 | G → Q AA sequence (PubMed:8980141).Curated | 1 | |
Sequence conflicti | 99 | I → V AA sequence (PubMed:8980141).Curated | 1 | |
Sequence conflicti | 108 | L → A AA sequence (PubMed:8980141).Curated | 1 | |
Sequence conflicti | 117 | D → N in AAR25546 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 141 | S → P in AAR25546 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 181 | S → N in AAL87006 (PubMed:15001393).Curated | 1 | |
Sequence conflicti | 190 | L → I in AAR25545 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 190 | L → I in AAR25546 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 193 | I → V in AAR25545 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 193 | I → V in AAR25546 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 209 | A → L in AAR25546 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 209 | A → Y AA sequence (PubMed:8980141).Curated | 1 | |
Sequence conflicti | 241 | Q → H AA sequence (PubMed:8980141).Curated | 1 | |
Sequence conflicti | 241 | Q → H (PubMed:12823544).Curated | 1 | |
Sequence conflicti | 244 | D → E in AAL87006 (PubMed:15001393).Curated | 1 | |
Sequence conflicti | 322 | C → R AA sequence (PubMed:9618256).Curated | 1 | |
Sequence conflicti | 391 – 393 | LWE → IWQ in AAR25545 (PubMed:15182350).Curated | 3 | |
Sequence conflicti | 391 – 393 | LWE → IWQ in AAL87006 (PubMed:15001393).Curated | 3 | |
Sequence conflicti | 391 – 393 | LWE → IWQ AA sequence (PubMed:9618256).Curated | 3 | |
Sequence conflicti | 396 | G → D AA sequence (PubMed:9618256).Curated | 1 | |
Sequence conflicti | 408 | V → A in AAL87006 (PubMed:15001393).Curated | 1 | |
Sequence conflicti | 467 | V → D AA sequence (PubMed:9618256).Curated | 1 | |
Sequence conflicti | 468 | I → S in AAR25545 (PubMed:15182350).Curated | 1 | |
Sequence conflicti | 468 | I → S in AAL87006 (PubMed:15001393).Curated | 1 | |
Sequence conflicti | 468 | I → S AA sequence (PubMed:9618256).Curated | 1 | |
Sequence conflicti | 471 – 474 | QNQR → KNQGK AA sequence (PubMed:9618256).Curated | 4 | |
Sequence conflicti | 495 | C → S AA sequence (PubMed:9618256).Curated | 1 | |
Sequence conflicti | 511 – 515 | AGSSG → GASGS AA sequence (PubMed:9618256).Curated | 5 | |
Sequence conflicti | 538 – 540 | AQA → KGS in AAL87006 (PubMed:15001393).Curated | 3 | |
Sequence conflicti | 546 | R → Q in AAL87006 (PubMed:15001393).Curated | 1 | |
Sequence conflicti | 564 | P → F AA sequence (PubMed:9618256).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 48 | E → D in MLA'. 1 Publication | 1 | |
Natural varianti | 145 | N → T in MLA'. 1 Publication | 1 | |
Natural varianti | 149 | P → T in MLA'. 1 Publication | 1 | |
Natural varianti | 166 – 167 | DQ → EE in MLA'. | 2 | |
Natural varianti | 173 | T → S in MLA'. 1 Publication | 1 | |
Natural varianti | 177 | F → Y in MLA'. 1 Publication | 1 | |
Natural varianti | 184 | T → A in MLA'. 1 Publication | 1 | |
Natural varianti | 212 | Y → D in MLA'. 1 Publication | 1 | |
Natural varianti | 217 | A → E in MLA'. 1 Publication | 1 | |
Natural varianti | 223 | V → M in MLA'. 1 Publication | 1 | |
Natural varianti | 251 | I → F in MLA'. 1 Publication | 1 | |
Natural varianti | 256 – 257 | PP → ST in MLA'. | 2 | |
Natural varianti | 264 | T → S in MLA'. 1 Publication | 1 | |
Natural varianti | 268 | D → S in MLA'. 1 Publication | 1 | |
Natural varianti | 319 | N → S1 Publication | 1 | |
Natural varianti | 357 | G → N1 Publication | 1 | |
Natural varianti | 458 | G → Q1 Publication | 1 | |
Natural varianti | 495 | C → V1 Publication | 1 | |
Natural varianti | 524 | G → Y1 Publication | 1 | |
Natural varianti | 531 – 533 | NGL → KGP. | 3 | |
Natural varianti | 531 | N → S1 Publication | 1 | |
Natural varianti | 531 | N → T1 Publication | 1 | |
Natural varianti | 532 – 535 | GLAM → SLMV. | 4 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY377890 Genomic DNA Translation: AAR25545.1 AY377891 mRNA Translation: AAR25546.1 AY081149 mRNA Translation: AAL87006.1 |
PIRi | JW0090 PD0018 PD0019 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY377890 Genomic DNA Translation: AAR25545.1 AY377891 mRNA Translation: AAR25546.1 AY081149 mRNA Translation: AAL87006.1 |
PIRi | JW0090 PD0018 PD0019 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1M2T | X-ray | 1.89 | A | 34-287 | [»] | |
B | 313-564 | [»] | ||||
1ONK | X-ray | 2.10 | A | 34-287 | [»] | |
B | 302-563 | [»] | ||||
1OQL | X-ray | 3.00 | A | 34-282 | [»] | |
B | 302-564 | [»] | ||||
1PUM | X-ray | 2.30 | A | 34-282 | [»] | |
B | 302-564 | [»] | ||||
1PUU | X-ray | 2.30 | A | 34-282 | [»] | |
B | 302-564 | [»] | ||||
1SZ6 | X-ray | 2.05 | A | 34-282 | [»] | |
B | 302-564 | [»] | ||||
2R9K | X-ray | 2.70 | A | 34-287 | [»] | |
B | 302-564 | [»] | ||||
2RG9 | X-ray | 1.95 | A | 34-282 | [»] | |
B | 302-564 | [»] | ||||
3D7W | X-ray | 2.49 | A | 34-287 | [»] | |
B | 302-564 | [»] | ||||
3O5W | X-ray | 2.70 | A | 34-287 | [»] | |
B | 302-564 | [»] | ||||
4EB2 | X-ray | 1.94 | A | 34-282 | [»] | |
B | 302-564 | [»] | ||||
4JKX | X-ray | 2.35 | A | 34-282 | [»] | |
B | 302-564 | [»] | ||||
6ELY | X-ray | 2.84 | A | 34-282 | [»] | |
B | 302-564 | [»] | ||||
SMRi | P81446 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
CAZyi | CBM13, Carbohydrate-Binding Module Family 13 |
UniLectini | P81446 |
PTM databases
iPTMneti | P81446 |
Enzyme and pathway databases
BRENDAi | 3.2.2.22, 6669 |
Miscellaneous databases
EvolutionaryTracei | P81446 |
Family and domain databases
CDDi | cd00161, RICIN, 2 hits |
Gene3Di | 3.40.420.10, 1 hit 4.10.470.10, 1 hit |
InterProi | View protein in InterPro IPR036041, Ribosome-inact_prot_sf IPR017989, Ribosome_inactivat_1/2 IPR001574, Ribosome_inactivat_prot IPR016138, Ribosome_inactivat_prot_sub1 IPR016139, Ribosome_inactivat_prot_sub2 IPR035992, Ricin_B-like_lectins IPR000772, Ricin_B_lectin |
PANTHERi | PTHR33453, PTHR33453, 1 hit |
Pfami | View protein in Pfam PF00652, Ricin_B_lectin, 2 hits PF00161, RIP, 1 hit |
PRINTSi | PR00396, SHIGARICIN |
SMARTi | View protein in SMART SM00458, RICIN, 2 hits |
SUPFAMi | SSF50370, SSF50370, 2 hits SSF56371, SSF56371, 1 hit |
PROSITEi | View protein in PROSITE PS50231, RICIN_B_LECTIN, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ML1_VISAL | |
Accessioni | P81446Primary (citable) accession number: P81446 Secondary accession number(s): P81830 Q9S7D0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 15, 1998 |
Last sequence update: | April 17, 2007 | |
Last modified: | June 2, 2021 | |
This is version 127 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, PharmaceuticalDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families