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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 – 1981By similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. 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 peptide1 PublicationPRO_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 PublicationPROSITE-ProRule annotation
Glycosylationi362 – 3621N-linked (GlcNAc...)1 Publication
Disulfide bondi365 ↔ 3821 PublicationPROSITE-ProRule annotation
Glycosylationi397 – 3971N-linked (GlcNAc...)1 Publication
Glycosylationi437 – 4371N-linked (GlcNAc...)1 Publication
Disulfide bondi453 ↔ 4661 PublicationPROSITE-ProRule annotation
Disulfide bondi492 ↔ 5091 PublicationPROSITE-ProRule annotation

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.3 Publications

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81446.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Contains 2 ricin B-type lectin domains.PROSITE-ProRule annotation

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 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:564
Mass (Da):62,628
Last modified:April 17, 2007 - v3
Checksum:i8BC06110DD458A6E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31G → A in AAR25545. (PubMed:15182350)Curated
Sequence conflicti19 – 202GQ → CL in AAR25545. (PubMed:15182350)Curated
Sequence conflicti37 – 371L → I in AAR25546. (PubMed:15182350)Curated
Sequence conflicti62 – 621S → G AA sequence (PubMed:1450445)Curated
Sequence conflicti83 – 831A → T in AAR25546. (PubMed:15182350)Curated
Sequence conflicti92 – 921T → S in AAR25546. (PubMed:15182350)Curated
Sequence conflicti94 – 941E → Q in AAR25545. (PubMed:15182350)Curated
Sequence conflicti94 – 941E → Q AA sequence (PubMed:8980141)Curated
Sequence conflicti94 – 941E → Q(PubMed:12823544)Curated
Sequence conflicti96 – 961G → Q AA sequence (PubMed:8980141)Curated
Sequence conflicti99 – 991I → V AA sequence (PubMed:8980141)Curated
Sequence conflicti108 – 1081L → A AA sequence (PubMed:8980141)Curated
Sequence conflicti117 – 1171D → N in AAR25546. (PubMed:15182350)Curated
Sequence conflicti141 – 1411S → P in AAR25546. (PubMed:15182350)Curated
Sequence conflicti181 – 1811S → N in AAL87006. (PubMed:15001393)Curated
Sequence conflicti190 – 1901L → I in AAR25545. (PubMed:15182350)Curated
Sequence conflicti190 – 1901L → I in AAR25546. (PubMed:15182350)Curated
Sequence conflicti193 – 1931I → V in AAR25545. (PubMed:15182350)Curated
Sequence conflicti193 – 1931I → V in AAR25546. (PubMed:15182350)Curated
Sequence conflicti209 – 2091A → L in AAR25546. (PubMed:15182350)Curated
Sequence conflicti209 – 2091A → Y AA sequence (PubMed:8980141)Curated
Sequence conflicti241 – 2411Q → H AA sequence (PubMed:8980141)Curated
Sequence conflicti241 – 2411Q → H(PubMed:12823544)Curated
Sequence conflicti244 – 2441D → E in AAL87006. (PubMed:15001393)Curated
Sequence conflicti322 – 3221C → R AA sequence (PubMed:9618256)Curated
Sequence conflicti391 – 3933LWE → IWQ in AAR25545. (PubMed:15182350)Curated
Sequence conflicti391 – 3933LWE → IWQ in AAL87006. (PubMed:15001393)Curated
Sequence conflicti391 – 3933LWE → IWQ AA sequence (PubMed:9618256)Curated
Sequence conflicti396 – 3961G → D AA sequence (PubMed:9618256)Curated
Sequence conflicti408 – 4081V → A in AAL87006. (PubMed:15001393)Curated
Sequence conflicti467 – 4671V → D AA sequence (PubMed:9618256)Curated
Sequence conflicti468 – 4681I → S in AAR25545. (PubMed:15182350)Curated
Sequence conflicti468 – 4681I → S in AAL87006. (PubMed:15001393)Curated
Sequence conflicti468 – 4681I → S AA sequence (PubMed:9618256)Curated
Sequence conflicti471 – 4744QNQR → KNQGK AA sequence (PubMed:9618256)Curated
Sequence conflicti495 – 4951C → S AA sequence (PubMed:9618256)Curated
Sequence conflicti511 – 5155AGSSG → GASGS AA sequence (PubMed:9618256)Curated
Sequence conflicti538 – 5403AQA → KGS in AAL87006. (PubMed:15001393)Curated
Sequence conflicti546 – 5461R → Q in AAL87006. (PubMed:15001393)Curated
Sequence conflicti564 – 5641P → F AA sequence (PubMed:9618256)Curated

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 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: October 29, 2014
This is version 100 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