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P81446

- ML1_VISAL

UniProt

P81446 - ML1_VISAL

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Protein

Beta-galactoside-specific lectin 1

Gene
N/A
Organism
Viscum album (European mistletoe)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publications

Catalytic activityi

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei198 – 1981 By similarity

GO - Molecular functioni

  1. rRNA N-glycosylase activity Source: UniProtKB-EC

GO - Biological processi

  1. defense response Source: UniProtKB-KW
  2. negative regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Lectin

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactoside-specific lectin 1
Alternative 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
OrganismiViscum album (European mistletoe)
Taxonomic identifieri3972 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeViscum

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33333 PublicationsAdd
BLAST
Chaini34 – 287254Beta-galactoside-specific lectin 1 chain A isoform 1PRO_0000030749Add
BLAST
Propeptidei288 – 30114Connecting peptidePRO_0000030750Add
BLAST
Chaini302 – 564263Beta-galactoside-specific lectin 1 chain BPRO_0000030751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi145 – 1451N-linked (GlcNAc...)1 Publication
Disulfide bondi280 ↔ 306Interchain (between A and B chains)1 Publication
Glycosylationi362 – 3621N-linked (GlcNAc...)1 Publication
Disulfide bondi365 ↔ 3821 Publication
Glycosylationi397 – 3971N-linked (GlcNAc...)1 Publication
Glycosylationi437 – 4371N-linked (GlcNAc...)1 Publication
Disulfide bondi453 ↔ 4661 Publication
Disulfide bondi492 ↔ 5091 Publication

Post-translational modificationi

The A chain of variant MLA' is not glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Disulfide-linked dimer of A and B chains.1 Publication

Protein-protein interaction databases

MINTiMINT-364969.

Structurei

Secondary structure

1
564
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 428
Helixi47 – 6115
Beta strandi62 – 676
Beta strandi70 – 734
Beta strandi80 – 823
Beta strandi85 – 939
Beta strandi98 – 1047
Turni105 – 1073
Beta strandi110 – 1156
Beta strandi118 – 1214
Helixi129 – 1313
Beta strandi137 – 1415
Helixi148 – 1558
Helixi158 – 1603
Helixi165 – 17612
Helixi182 – 19514
Helixi197 – 2015
Helixi203 – 21513
Helixi223 – 24018
Beta strandi246 – 25510
Turni256 – 2583
Beta strandi259 – 2657
Helixi266 – 2683
Turni269 – 2724
Beta strandi315 – 3173
Helixi318 – 3203
Beta strandi322 – 3254
Helixi326 – 3283
Beta strandi335 – 3395
Helixi347 – 3493
Beta strandi351 – 3533
Beta strandi359 – 3613
Beta strandi364 – 3696
Beta strandi376 – 3816
Turni382 – 3843
Helixi387 – 3904
Beta strandi400 – 4023
Turni403 – 4064
Beta strandi407 – 4104
Beta strandi421 – 4233
Helixi429 – 4313
Beta strandi434 – 4374
Beta strandi442 – 4476
Helixi449 – 4513
Beta strandi453 – 4575
Beta strandi460 – 4645
Helixi471 – 4733
Beta strandi475 – 4773
Beta strandi483 – 4853
Beta strandi491 – 4944
Beta strandi505 – 5095
Helixi514 – 5163
Beta strandi518 – 5203
Beta strandi526 – 5283
Turni529 – 5313
Beta strandi534 – 5374
Helixi538 – 5403
Helixi542 – 5443
Beta strandi547 – 5504
Helixi556 – 5583
Beta strandi561 – 5633

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2TX-ray1.89A34-287[»]
B313-564[»]
1ONKX-ray2.10A34-287[»]
B302-563[»]
1OQLX-ray3.00A34-282[»]
B302-564[»]
1PUMX-ray2.30A44-282[»]
B302-564[»]
1PUUX-ray2.30A44-282[»]
B302-564[»]
1SZ6X-ray2.05A44-282[»]
B302-564[»]
2R9KX-ray2.70A34-287[»]
B302-564[»]
2RG9X-ray1.95A44-282[»]
B302-564[»]
3D7WX-ray2.49A34-287[»]
B302-564[»]
3O5WX-ray2.70A34-287[»]
B302-564[»]
4EB2X-ray1.94A44-282[»]
B302-564[»]
4JKXX-ray2.35A34-282[»]
B302-564[»]
ProteinModelPortaliP81446.
SMRiP81446. Positions 34-281, 302-563.

Miscellaneous databases

EvolutionaryTraceiP81446.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini309 – 436128Ricin B-type lectin 1Add
BLAST
Domaini440 – 564125Ricin B-type lectin 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni324 – 3263Galactose binding
Regioni536 – 5383Galactose binding

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. Ribosome_inactivat_prot.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00652. Ricin_B_lectin. 2 hits.
PF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SMARTiSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 2 hits.
SSF56371. SSF56371. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P81446-1 [UniParc]FASTAAdd to Basket

« Hide

MNGHLASRRA WVWYFLMLGQ VFGATVKAET KFSYERLRLR VTHQTTGEEY    50
FRFITLLRDY VSSGSFSNEI PLLRQSTIPV SDAQRFVLVE LTNEGGDSIT 100
AAIDVTNLYV VAYQAGDQSY FLRDAPRGAE THLFTGTTRS SLPFNGSYPD 150
LERYAGHRDQ IPLGIDQLIQ SVTALRFPGG STRTQARSIL ILIQMISEAA 200
RFNPILWRAR QYINSGASFL PDVYMLELET SWGQQSTQVQ QSTDGVFNNP 250
IRLAIPPGNF VTLTNVRDVI ASLAIMLFVC GERPSSSDVR YWPLVIRPVI 300
ADDVTCSASE PTVRIVGRNG MCVDVRDDDF HDGNQIQLWP SKSNNDPNQL 350
WTIKRDGTIR SNGSCLTTYG YTAGVYVMIF DCNTAVREAT LWEIWGNGTI 400
INPRSNLVLA ASSGIKGTTL TVQTLDYTLG QGWLAGNDTA PREVTIYGFR 450
DLCMESNGGS VWVETCVISQ QNQRWALYGD GSIRPKQNQD QCLTCGRDSV 500
STVINIVSCS AGSSGQRWVF TNEGAILNLK NGLAMDVAQA NPKLRRIIIY 550
PATGKPNQMW LPVP 564
Length:564
Mass (Da):62,628
Last modified:April 17, 2007 - v3
Checksum:i8BC06110DD458A6E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481E → D in MLA'. 1 Publication
Natural varianti145 – 1451N → T in MLA'. 1 Publication
Natural varianti149 – 1491P → T in MLA'. 1 Publication
Natural varianti166 – 1672DQ → EE in MLA'.
Natural varianti173 – 1731T → S in MLA'. 1 Publication
Natural varianti177 – 1771F → Y in MLA'. 1 Publication
Natural varianti184 – 1841T → A in MLA'. 1 Publication
Natural varianti212 – 2121Y → D in MLA'. 1 Publication
Natural varianti217 – 2171A → E in MLA'. 1 Publication
Natural varianti223 – 2231V → M in MLA'. 1 Publication
Natural varianti251 – 2511I → F in MLA'. 1 Publication
Natural varianti256 – 2572PP → ST in MLA'.
Natural varianti264 – 2641T → S in MLA'. 1 Publication
Natural varianti268 – 2681D → S in MLA'. 1 Publication
Natural varianti319 – 3191N → S.1 Publication
Natural varianti357 – 3571G → N.1 Publication
Natural varianti458 – 4581G → Q.1 Publication
Natural varianti495 – 4951C → V.1 Publication
Natural varianti524 – 5241G → Y.1 Publication
Natural varianti531 – 5333NGL → KGP.
Natural varianti531 – 5311N → S.1 Publication
Natural varianti531 – 5311N → T.1 Publication
Natural varianti532 – 5354GLAM → SLMV.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31G → A in AAR25545. 1 Publication
Sequence conflicti19 – 202GQ → CL in AAR25545. 1 Publication
Sequence conflicti37 – 371L → I in AAR25546. 1 Publication
Sequence conflicti62 – 621S → G AA sequence 1 Publication
Sequence conflicti83 – 831A → T in AAR25546. 1 Publication
Sequence conflicti92 – 921T → S in AAR25546. 1 Publication
Sequence conflicti94 – 941E → Q in AAR25545. 1 Publication
Sequence conflicti94 – 941E → Q AA sequence 1 Publication
Sequence conflicti94 – 941E → Q1 Publication
Sequence conflicti96 – 961G → Q AA sequence 1 Publication
Sequence conflicti99 – 991I → V AA sequence 1 Publication
Sequence conflicti108 – 1081L → A AA sequence 1 Publication
Sequence conflicti117 – 1171D → N in AAR25546. 1 Publication
Sequence conflicti141 – 1411S → P in AAR25546. 1 Publication
Sequence conflicti181 – 1811S → N in AAL87006. 1 Publication
Sequence conflicti190 – 1901L → I in AAR25545. 1 Publication
Sequence conflicti190 – 1901L → I in AAR25546. 1 Publication
Sequence conflicti193 – 1931I → V in AAR25545. 1 Publication
Sequence conflicti193 – 1931I → V in AAR25546. 1 Publication
Sequence conflicti209 – 2091A → L in AAR25546. 1 Publication
Sequence conflicti209 – 2091A → Y AA sequence 1 Publication
Sequence conflicti241 – 2411Q → H AA sequence 1 Publication
Sequence conflicti241 – 2411Q → H1 Publication
Sequence conflicti244 – 2441D → E in AAL87006. 1 Publication
Sequence conflicti322 – 3221C → R AA sequence 1 Publication
Sequence conflicti391 – 3933LWE → IWQ in AAR25545. 1 Publication
Sequence conflicti391 – 3933LWE → IWQ in AAL87006. 1 Publication
Sequence conflicti391 – 3933LWE → IWQ AA sequence 1 Publication
Sequence conflicti396 – 3961G → D AA sequence 1 Publication
Sequence conflicti408 – 4081V → A in AAL87006. 1 Publication
Sequence conflicti467 – 4671V → D AA sequence 1 Publication
Sequence conflicti468 – 4681I → S in AAR25545. 1 Publication
Sequence conflicti468 – 4681I → S in AAL87006. 1 Publication
Sequence conflicti468 – 4681I → S AA sequence 1 Publication
Sequence conflicti471 – 4744QNQR → KNQGK AA sequence 1 Publication
Sequence conflicti495 – 4951C → S AA sequence 1 Publication
Sequence conflicti511 – 5155AGSSG → GASGS AA sequence 1 Publication
Sequence conflicti538 – 5403AQA → KGS in AAL87006. 1 Publication
Sequence conflicti546 – 5461R → Q in AAL87006. 1 Publication
Sequence conflicti564 – 5641P → F AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY377890 Genomic DNA. Translation: AAR25545.1.
AY377891 mRNA. Translation: AAR25546.1.
AY081149 mRNA. Translation: AAL87006.1.
PIRiJW0090.
PD0018.
PD0019.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
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 44-282 [» ]
B 302-564 [» ]
1PUU X-ray 2.30 A 44-282 [» ]
B 302-564 [» ]
1SZ6 X-ray 2.05 A 44-282 [» ]
B 302-564 [» ]
2R9K X-ray 2.70 A 34-287 [» ]
B 302-564 [» ]
2RG9 X-ray 1.95 A 44-282 [» ]
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 44-282 [» ]
B 302-564 [» ]
4JKX X-ray 2.35 A 34-282 [» ]
B 302-564 [» ]
ProteinModelPortali P81446.
SMRi P81446. Positions 34-281, 302-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-364969.

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P81446.

Family and domain databases

Gene3Di 3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProi IPR001574. Ribosome_inactivat_prot.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00652. Ricin_B_lectin. 2 hits.
PF00161. RIP. 1 hit.
[Graphical view ]
PRINTSi PR00396. SHIGARICIN.
SMARTi SM00458. RICIN. 2 hits.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 2 hits.
SSF56371. SSF56371. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of the genes encoding toxic lectins in mistletoe (Viscum album L)."
    Kourmanova A.G., Soudarkina O.J., Olsnes S., Kozlov J.V.
    Eur. J. Biochem. 271:2350-2360(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
    Tissue: Leaf.
  2. "Purification and characterization of four isoforms of Himalayan mistletoe ribosome-inactivating protein from Viscum album having unique sugar affinity."
    Mishra V., Sharma R.S., Yadav S., Babu C.R., Singh T.P.
    Arch. Biochem. Biophys. 423:288-301(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-564, PROTEIN SEQUENCE OF 34-53, FUNCTION.
    Tissue: Leaf.
  3. "Complete amino acid sequence of the A chain of mistletoe lectin I."
    Soler M.H., Stoeva S., Schwamborn C., Wilhelm S., Stiefel T., Voelter W.
    FEBS Lett. 399:153-157(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-287 (CHAIN A), VARIANTS ASP-48; THR-145; THR-149; 166-GLU-GLU-167; SER-173; TYR-177; ALA-184; ASP-212; GLU-217; MET-223; PHE-251; 256-SER-THR-257; SER-264 AND SER-268.
  4. "Identity of the N-terminal sequences of the three A chains of mistletoe (Viscum album L.) lectins: homology with ricin-like plant toxins and single-chain ribosome-inhibiting proteins."
    Dietrich J.B., Ribereau-Gayon G., Jung M.L., Franz H., Beck J.P., Anton R.
    Anticancer Drugs 3:507-511(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-62, FUNCTION.
  5. "Complete amino acid sequence of the B chain of mistletoe lectin I."
    Soler M.H., Stoeva S., Voelter W.
    Biochem. Biophys. Res. Commun. 246:596-601(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 302-564 (CHAIN B), VARIANTS SER-319; ASN-357; GLN-458; VAL-495; TYR-524; SER-531; THR-531; 531-LYS--PRO-533 AND 532-SER--VAL-535.
  6. "Primary structure and molecular modeling of mistletoe lectin I from Viscum album."
    Eschenburg S., Krauspenhaar R., Mikhailov A., Stoeva S., Betzel C., Voelter W.
    Biochem. Biophys. Res. Commun. 247:367-372(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 34-287 AND 302-564.
  7. "Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution."
    Krauspenhaar R., Rypniewski W., Kalkura N., Moore K., DeLucas L., Stoeva S., Mikhailov A., Voelter W., Betzel C.
    Acta Crystallogr. D 58:1704-1707(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 34-287 AND 302-564 IN COMPLEX WITH AMP.
  8. "Crystal structure at 3 A of mistletoe lectin I, a dimeric type-II ribosome-inactivating protein, complexed with galactose."
    Niwa H., Tonevitsky A.G., Agapov I.I., Saward S., Pfueller U., Palmer R.A.
    Eur. J. Biochem. 270:2739-2749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 34-282 AND 302-564 IN COMPLEX WITH GALACTOSE, SUBUNIT, GLYCOSYLATION AT ASN-145; ASN-362; ASN-397 AND ASN-437, DISULFIDE BONDS.
  9. "Mistletoe lectin I in complex with galactose and lactose reveals distinct sugar-binding properties."
    Mikeska R., Wacker R., Arni R., Singh T.P., Mikhailov A., Gabdoulkhakov A., Voelter W., Betzel C.
    Acta Crystallogr. F 61:17-25(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 34-282 AND 302-564 IN COMPLEX WITH LACTOSE AND GALACTOSE.
  10. "Mistletoe lectin I From Viscum album."
    Gabdoulkhakov A.G., Savoshkina Y., Krauspenhaar R., Stoeva S., Konareva N., Kornilov V., Kornev A.N., Voelter W., Nikonov S.V., Betzel C., Mikhailov A.M.
    Submitted (FEB-2003) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 34-287 AND 302-563.

Entry informationi

Entry nameiML1_VISAL
AccessioniPrimary (citable) accession number: P81446
Secondary accession number(s): P81830
, Q6H270, Q6H271, Q8RXH6, Q9S7D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Several isoforms exist.

Keywords - Technical termi

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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