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Protein

Agglutinin alpha chain

Gene
N/A
Organism
Artocarpus integer (Jack fruit) (Artocarpus integrifolia)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc (Thomsen-Friedenreich-antigen-specific lectin). Potent and selective stimulant of distinct T- and B-cell functions. Shows a unique ability to specifically recognize IgA-1 from human serum.

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • IgA binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

IgA-binding protein, Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Agglutinin alpha chain
Alternative name(s):
Jacalin alpha chain
OrganismiArtocarpus integer (Jack fruit) (Artocarpus integrifolia)
Taxonomic identifieri3490 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesMoraceaeArtocarpus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 133133Agglutinin alpha chainPRO_0000072798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...); when associated with variant T-45; partial1 Publication
Glycosylationi74 – 741N-linked (GlcNAc...); partial1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Tetramer of four alpha chains associated with two or four beta chains.1 Publication

Structurei

Secondary structure

1
133
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi10 – 1910Combined sources
Beta strandi21 – 233Combined sources
Beta strandi25 – 3410Combined sources
Beta strandi37 – 404Combined sources
Beta strandi52 – 576Combined sources
Turni60 – 623Combined sources
Beta strandi65 – 7511Combined sources
Beta strandi78 – 9013Combined sources
Beta strandi92 – 976Combined sources
Beta strandi101 – 11010Combined sources
Beta strandi112 – 13221Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JACX-ray2.43A/C/E/G1-133[»]
1KU8X-ray1.75A/C/E/G1-133[»]
1KUJX-ray2.00A/C/E/G1-133[»]
1M26X-ray1.62A/C/E/G1-133[»]
1PXDX-ray1.80A1-133[»]
1TOQX-ray2.50A/C/E/G1-133[»]
1TP8X-ray3.00A/C/E/G1-133[»]
1UGWX-ray1.70A/C/E/G1-133[»]
1UGXX-ray1.60A1-133[»]
1UGYX-ray2.40A/C/E/G1-133[»]
1UH0X-ray2.80A/C/E/G1-133[»]
1UH1X-ray2.80A/C/E/G1-133[»]
1WS4X-ray1.90A/C/E/G1-133[»]
1WS5X-ray1.90A/C/E/G1-133[»]
4AK4X-ray1.65A/C/E/G/I/K/M/O1-133[»]
4AKBX-ray1.95A/C/E/G1-133[»]
4AKCX-ray2.30A/C/E/G1-133[»]
4R6NX-ray1.67A/C/E/G1-133[»]
4R6OX-ray1.60A/C/E/G1-133[»]
4R6PX-ray1.70A/C/E/G1-133[»]
4R6QX-ray1.60A/C/E/G1-133[»]
4R6RX-ray1.38A/C/E/G1-133[»]
ProteinModelPortaliP18670.
SMRiP18670. Positions 1-133.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18670.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 133133Jacalin-type lectinPROSITE-ProRule annotationAdd
BLAST
Repeati7 – 6458Add
BLAST
Repeati76 – 13055Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 8922IgA-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the jacalin lectin family.PROSITE-ProRule annotationCurated
Contains 1 jacalin-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.100.10.30. 1 hit.
InterProiIPR001229. Jacalin-like_lectin_dom.
[Graphical view]
PfamiPF01419. Jacalin. 1 hit.
[Graphical view]
SMARTiSM00915. Jacalin. 1 hit.
[Graphical view]
SUPFAMiSSF51101. SSF51101. 1 hit.
PROSITEiPS51752. JACALIN_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18670-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GKAFDDGAFT GIREINLSYN KETAIGDFQV VYDLNGSPYV GQNHKSFITG
60 70 80 90 100
FTPVKISLDF PSEYIMEVSG YTGNVSGYVV VRSLTFKTNK KTYGPYGVTS
110 120 130
GTPFNLPIEN GLIVGFKGSI GYWLDYFSMY LSL
Length:133
Mass (Da):14,663
Last modified:August 1, 1991 - v2
Checksum:iFF10513379CB2E10
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191Y → I AA sequence (PubMed:8427879).Curated
Sequence conflicti75 – 751V → Y AA sequence (PubMed:1599414).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311V → I.1 Publication
Natural varianti34 – 341L → G.
Natural varianti45 – 451K → L.
Natural varianti45 – 451K → T.1 Publication
Natural varianti66 – 661M → D.
Natural varianti66 – 661M → V.1 Publication
Natural varianti67 – 671E → M.
Natural varianti72 – 721T → I.
Natural varianti74 – 741N → K.
Natural varianti102 – 1021T → D.
Natural varianti113 – 1131I → V.
Natural varianti131 – 1311L → N.

Sequence databases

PIRiS29641.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

PIRiS29641.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JACX-ray2.43A/C/E/G1-133[»]
1KU8X-ray1.75A/C/E/G1-133[»]
1KUJX-ray2.00A/C/E/G1-133[»]
1M26X-ray1.62A/C/E/G1-133[»]
1PXDX-ray1.80A1-133[»]
1TOQX-ray2.50A/C/E/G1-133[»]
1TP8X-ray3.00A/C/E/G1-133[»]
1UGWX-ray1.70A/C/E/G1-133[»]
1UGXX-ray1.60A1-133[»]
1UGYX-ray2.40A/C/E/G1-133[»]
1UH0X-ray2.80A/C/E/G1-133[»]
1UH1X-ray2.80A/C/E/G1-133[»]
1WS4X-ray1.90A/C/E/G1-133[»]
1WS5X-ray1.90A/C/E/G1-133[»]
4AK4X-ray1.65A/C/E/G/I/K/M/O1-133[»]
4AKBX-ray1.95A/C/E/G1-133[»]
4AKCX-ray2.30A/C/E/G1-133[»]
4R6NX-ray1.67A/C/E/G1-133[»]
4R6OX-ray1.60A/C/E/G1-133[»]
4R6PX-ray1.70A/C/E/G1-133[»]
4R6QX-ray1.60A/C/E/G1-133[»]
4R6RX-ray1.38A/C/E/G1-133[»]
ProteinModelPortaliP18670.
SMRiP18670. Positions 1-133.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP18670.

Family and domain databases

Gene3Di2.100.10.30. 1 hit.
InterProiIPR001229. Jacalin-like_lectin_dom.
[Graphical view]
PfamiPF01419. Jacalin. 1 hit.
[Graphical view]
SMARTiSM00915. Jacalin. 1 hit.
[Graphical view]
SUPFAMiSSF51101. SSF51101. 1 hit.
PROSITEiPS51752. JACALIN_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The amino acid sequences of jacalin and the Maclura pomifera agglutinin."
    Young N.M., Johnston R.A.Z., Watson D.C.
    FEBS Lett. 282:382-384(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Seed.
  2. "Primary structure of a Thomsen-Friedenreich-antigen-specific lectin, jacalin [Artocarpus integrifolia (jack fruit) agglutinin]. Evidence for the presence of an internal repeat."
    Mahanta S.K., Sanker S., Prasad Rao N.V.S.A.V., Swamy M.J., Surolia A.
    Biochem. J. 284:95-101(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Fruit.
  3. "Structural and electron-microscopic studies of jacalin from jackfruit (Artocarpus integrifolia) show that this lectin is a 65 kDa tetramer."
    Ruffet E., Paquet N., Frutiger S., Hughes G.J., Jaton J.-C.
    Biochem. J. 286:131-134(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, VARIANTS ILE-31; THR-45 AND VAL-66, GLYCOSYLATION AT ASN-43 AND ASN-74, SUBUNIT.
    Tissue: Seed.
  4. "Homology of the D-galactose-specific lectins from Artocarpus integrifolia and Maclura pomifera and the role of an unusual small polypeptide subunit."
    Young N.M., Johnston R.A.Z., Szabo A.G., Watson D.C.
    Arch. Biochem. Biophys. 270:596-603(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-33.
    Tissue: Seed.
  5. "Identification of a novel 4 kDa immunoglobulin-A-binding peptide obtained by the limited proteolysis of jacalin."
    Kabir S., Aebersold R., Daar A.S.
    Biochim. Biophys. Acta 1161:194-200(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-29 AND 68-89.
    Tissue: Seed.
  6. "The alpha- and beta-subunits of the jacalins are cleavage products from a 17-kDa precursor."
    Ngoc L.D., Brillard M., Hoebeke J.
    Biochim. Biophys. Acta 1156:219-222(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-27.
  7. "A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold."
    Sakaranarayanan R., Sekar S., Banerjee R., Sharma V., Surolia A., Vijayan M.
    Nat. Struct. Biol. 3:596-603(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS).

Entry informationi

Entry nameiLECA_ARTIN
AccessioniPrimary (citable) accession number: P18670
Secondary accession number(s): P80023, Q9S788
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 1, 1991
Last modified: May 27, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.