LECA_ARTIN
ID LECA_ARTIN Reviewed; 133 AA.
AC P18670; P80023; Q9S788;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Agglutinin alpha chain;
DE AltName: Full=Jacalin alpha chain;
OS Artocarpus integer (Jack fruit) (Artocarpus integrifolia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Artocarpus.
OX NCBI_TaxID=3490;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=2037053; DOI=10.1016/0014-5793(91)80518-8;
RA Young N.M., Johnston R.A.Z., Watson D.C.;
RT "The amino acid sequences of jacalin and the Maclura pomifera agglutinin.";
RL FEBS Lett. 282:382-384(1991).
RN [2]
RP PROTEIN SEQUENCE.
RC TISSUE=Fruit;
RX PubMed=1599414; DOI=10.1042/bj2840095;
RA Mahanta S.K., Sanker S., Prasad Rao N.V.S.A.V., Swamy M.J., Surolia A.;
RT "Primary structure of a Thomsen-Friedenreich-antigen-specific lectin,
RT jacalin [Artocarpus integrifolia (jack fruit) agglutinin]. Evidence for the
RT presence of an internal repeat.";
RL Biochem. J. 284:95-101(1992).
RN [3]
RP PROTEIN SEQUENCE, VARIANTS ILE-31; THR-45 AND VAL-66, GLYCOSYLATION AT
RP ASN-43 (VARIANT THR-45), GLYCOSYLATION AT ASN-74, AND SUBUNIT.
RC TISSUE=Seed;
RX PubMed=1520261; DOI=10.1042/bj2860131;
RA Ruffet E., Paquet N., Frutiger S., Hughes G.J., Jaton J.-C.;
RT "Structural and electron-microscopic studies of jacalin from jackfruit
RT (Artocarpus integrifolia) show that this lectin is a 65 kDa tetramer.";
RL Biochem. J. 286:131-134(1992).
RN [4]
RP PROTEIN SEQUENCE OF 1-33.
RC TISSUE=Seed;
RX PubMed=2705782; DOI=10.1016/0003-9861(89)90542-0;
RA Young N.M., Johnston R.A.Z., Szabo A.G., Watson D.C.;
RT "Homology of the D-galactose-specific lectins from Artocarpus integrifolia
RT and Maclura pomifera and the role of an unusual small polypeptide
RT subunit.";
RL Arch. Biochem. Biophys. 270:596-603(1989).
RN [5]
RP PROTEIN SEQUENCE OF 1-29 AND 68-89.
RC TISSUE=Seed;
RX PubMed=8431469; DOI=10.1016/0167-4838(93)90213-b;
RA Kabir S., Aebersold R., Daar A.S.;
RT "Identification of a novel 4 kDa immunoglobulin-A-binding peptide obtained
RT by the limited proteolysis of jacalin.";
RL Biochim. Biophys. Acta 1161:194-200(1993).
RN [6]
RP PROTEIN SEQUENCE OF 1-27.
RX PubMed=8427879; DOI=10.1016/0304-4165(93)90139-y;
RA Ngoc L.D., Brillard M., Hoebeke J.;
RT "The alpha- and beta-subunits of the jacalins are cleavage products from a
RT 17-kDa precursor.";
RL Biochim. Biophys. Acta 1156:219-222(1993).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS).
RX PubMed=8673603; DOI=10.1038/nsb0796-596;
RA Sakaranarayanan R., Sekar S., Banerjee R., Sharma V., Surolia A.,
RA Vijayan M.;
RT "A novel mode of carbohydrate recognition in jacalin, a Moraceae plant
RT lectin with a beta-prism fold.";
RL Nat. Struct. Biol. 3:596-603(1996).
CC -!- FUNCTION: D-galactose-specific lectin, binds the T-antigen structure
CC Gal-beta1,3-GalNAc (Thomsen-Friedenreich-antigen-specific lectin).
CC Potent and selective stimulant of distinct T- and B-cell functions.
CC Shows a unique ability to specifically recognize IgA-1 from human
CC serum.
CC -!- SUBUNIT: Tetramer of four alpha chains associated with two or four beta
CC chains. {ECO:0000269|PubMed:1520261}.
CC -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01088, ECO:0000305}.
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DR PIR; S29641; S29641.
DR PDB; 1JAC; X-ray; 2.43 A; A/C/E/G=1-133.
DR PDB; 1KU8; X-ray; 1.75 A; A/C/E/G=1-133.
DR PDB; 1KUJ; X-ray; 2.00 A; A/C/E/G=1-133.
DR PDB; 1M26; X-ray; 1.62 A; A/C/E/G=1-133.
DR PDB; 1PXD; X-ray; 1.80 A; A=1-133.
DR PDB; 1TOQ; X-ray; 2.50 A; A/C/E/G=1-133.
DR PDB; 1TP8; X-ray; 3.00 A; A/C/E/G=1-133.
DR PDB; 1UGW; X-ray; 1.70 A; A/C/E/G=1-133.
DR PDB; 1UGX; X-ray; 1.60 A; A=1-133.
DR PDB; 1UGY; X-ray; 2.40 A; A/C/E/G=1-133.
DR PDB; 1UH0; X-ray; 2.80 A; A/C/E/G=1-133.
DR PDB; 1UH1; X-ray; 2.80 A; A/C/E/G=1-133.
DR PDB; 1WS4; X-ray; 1.90 A; A/C/E/G=1-133.
DR PDB; 1WS5; X-ray; 1.90 A; A/C/E/G=1-133.
DR PDB; 4AK4; X-ray; 1.65 A; A/C/E/G/I/K/M/O=1-133.
DR PDB; 4AKB; X-ray; 1.95 A; A/C/E/G=1-133.
DR PDB; 4AKC; X-ray; 2.30 A; A/C/E/G=1-133.
DR PDB; 4R6N; X-ray; 1.67 A; A/C/E/G=1-133.
DR PDB; 4R6O; X-ray; 1.60 A; A/C/E/G=1-133.
DR PDB; 4R6P; X-ray; 1.70 A; A/C/E/G=1-133.
DR PDB; 4R6Q; X-ray; 1.60 A; A/C/E/G=1-133.
DR PDB; 4R6R; X-ray; 1.38 A; A/C/E/G=1-133.
DR PDB; 5J4T; X-ray; 1.94 A; A/C/E/G=1-133.
DR PDB; 5J4X; X-ray; 1.65 A; A/C/E/G=1-133.
DR PDB; 5J50; X-ray; 2.05 A; A/C/E/G=1-133.
DR PDB; 5J51; X-ray; 1.67 A; A/C/E/G=1-133.
DR PDB; 5JM1; X-ray; 1.95 A; A/C/E/G=1-133.
DR PDBsum; 1JAC; -.
DR PDBsum; 1KU8; -.
DR PDBsum; 1KUJ; -.
DR PDBsum; 1M26; -.
DR PDBsum; 1PXD; -.
DR PDBsum; 1TOQ; -.
DR PDBsum; 1TP8; -.
DR PDBsum; 1UGW; -.
DR PDBsum; 1UGX; -.
DR PDBsum; 1UGY; -.
DR PDBsum; 1UH0; -.
DR PDBsum; 1UH1; -.
DR PDBsum; 1WS4; -.
DR PDBsum; 1WS5; -.
DR PDBsum; 4AK4; -.
DR PDBsum; 4AKB; -.
DR PDBsum; 4AKC; -.
DR PDBsum; 4R6N; -.
DR PDBsum; 4R6O; -.
DR PDBsum; 4R6P; -.
DR PDBsum; 4R6Q; -.
DR PDBsum; 4R6R; -.
DR PDBsum; 5J4T; -.
DR PDBsum; 5J4X; -.
DR PDBsum; 5J50; -.
DR PDBsum; 5J51; -.
DR PDBsum; 5JM1; -.
DR AlphaFoldDB; P18670; -.
DR SMR; P18670; -.
DR UniLectin; P18670; -.
DR iPTMnet; P18670; -.
DR EvolutionaryTrace; P18670; -.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0019862; F:IgA binding; IDA:UniProtKB.
DR CDD; cd09612; Jacalin; 1.
DR Gene3D; 2.100.10.30; -; 1.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR033734; Jacalin-like_lectin_dom_plant.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR Pfam; PF01419; Jacalin; 1.
DR SMART; SM00915; Jacalin; 1.
DR SUPFAM; SSF51101; SSF51101; 1.
DR PROSITE; PS51752; JACALIN_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; IgA-binding protein;
KW Lectin; Repeat.
FT CHAIN 1..133
FT /note="Agglutinin alpha chain"
FT /id="PRO_0000072798"
FT DOMAIN 1..133
FT /note="Jacalin-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REPEAT 7..64
FT REPEAT 76..130
FT REGION 68..89
FT /note="IgA-binding"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine; when associated
FT with variant T-45; partial"
FT /evidence="ECO:0000269|PubMed:1520261"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:1520261"
FT VARIANT 31
FT /note="V -> I"
FT /evidence="ECO:0000269|PubMed:1520261"
FT VARIANT 34
FT /note="L -> G"
FT VARIANT 45
FT /note="K -> L"
FT VARIANT 45
FT /note="K -> T"
FT /evidence="ECO:0000269|PubMed:1520261"
FT VARIANT 66
FT /note="M -> D"
FT VARIANT 66
FT /note="M -> V"
FT /evidence="ECO:0000269|PubMed:1520261"
FT VARIANT 67
FT /note="E -> M"
FT VARIANT 72
FT /note="T -> I"
FT VARIANT 74
FT /note="N -> K"
FT VARIANT 102
FT /note="T -> D"
FT VARIANT 113
FT /note="I -> V"
FT VARIANT 131
FT /note="L -> N"
FT CONFLICT 19
FT /note="Y -> I (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="V -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 10..19
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1KU8"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:4R6R"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:4R6R"
FT STRAND 112..132
FT /evidence="ECO:0007829|PDB:4R6R"
SQ SEQUENCE 133 AA; 14663 MW; FF10513379CB2E10 CRC64;
GKAFDDGAFT GIREINLSYN KETAIGDFQV VYDLNGSPYV GQNHKSFITG FTPVKISLDF
PSEYIMEVSG YTGNVSGYVV VRSLTFKTNK KTYGPYGVTS GTPFNLPIEN GLIVGFKGSI
GYWLDYFSMY LSL
