AGGL_RICCO
ID AGGL_RICCO Reviewed; 564 AA.
AC P06750;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Agglutinin;
DE AltName: Full=RCA;
DE Contains:
DE RecName: Full=Agglutinin A chain;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
DE Contains:
DE RecName: Full=Agglutinin B chain;
DE Flags: Precursor;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2999130; DOI=10.1016/s0021-9258(17)36312-3;
RA Roberts L.M., Lamb F.I., Pappin D.J.C., Lord J.M.;
RT "The primary sequence of Ricinus communis agglutinin. Comparison with
RT ricin.";
RL J. Biol. Chem. 260:15682-15686(1985).
RN [2]
RP PROTEIN SEQUENCE OF 303-564.
RC TISSUE=Seed;
RA Araki T., Yoshioka Y., Funatsu G.;
RT "The complete amino acid sequence of the B-chain of the Ricinus communis
RT agglutinin isolated from large-grain castor bean seeds.";
RL Biochim. Biophys. Acta 872:277-285(1986).
RN [3]
RP PROTEIN SEQUENCE OF 303-337.
RX PubMed=6768555; DOI=10.1111/j.1432-1033.1980.tb04520.x;
RA Lin T.T.-S., Li S.S.-L.;
RT "Purification and physicochemical properties of ricins and agglutinins from
RT Ricinus communis.";
RL Eur. J. Biochem. 105:453-459(1980).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 25-286 AND 303-564 IN COMPLEX
RP WITH GALACTOSE, AND DISULFIDE BONDS.
RA Gabdoulkhakov A.G., Savochkina Y., Konareva N., Krauspenhaar R., Stoeva S.,
RA Nikonov S.V., Voelter W., Betzel C., Mikhailov A.M.;
RT "Structure-function investigation complex of agglutinin from Ricinus
RT communis with galactose.";
RL Submitted (DEC-2003) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC adenosine on the 28S rRNA.; EC=3.2.2.22;
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome-
CC inactivating protein family. Type 2 RIP subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=RCA;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_pla_other_420";
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DR EMBL; M12089; AAA33869.1; -; mRNA.
DR EMBL; S40368; AAB22584.1; -; mRNA.
DR PIR; A24261; RLCSAG.
DR PDB; 1RZO; X-ray; 2.63 A; A/C=25-286, B/D=303-564.
DR PDBsum; 1RZO; -.
DR AlphaFoldDB; P06750; -.
DR SMR; P06750; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR UniLectin; P06750; -.
DR GlyConnect; 10; 3 N-Linked glycans.
DR eggNOG; ENOG502QUVN; Eukaryota.
DR EvolutionaryTrace; P06750; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 3.40.420.10; -; 1.
DR Gene3D; 4.10.470.10; -; 1.
DR InterPro; IPR036041; Ribosome-inact_prot_sf.
DR InterPro; IPR017989; Ribosome_inactivat_1/2.
DR InterPro; IPR001574; Ribosome_inactivat_prot.
DR InterPro; IPR017988; Ribosome_inactivat_prot_CS.
DR InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR33453; PTHR33453; 1.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF50370; SSF50370; 2.
DR SUPFAM; SSF56371; SSF56371; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
DR PROSITE; PS00275; SHIGA_RICIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lectin; Nucleotide-binding; Plant defense;
KW Protein synthesis inhibitor; Repeat; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..290
FT /note="Agglutinin A chain"
FT /id="PRO_0000030726"
FT PROPEP 291..302
FT /note="Linker peptide"
FT /evidence="ECO:0000269|PubMed:6768555, ECO:0000269|Ref.2"
FT /id="PRO_0000030727"
FT CHAIN 303..564
FT /note="Agglutinin B chain"
FT /evidence="ECO:0000269|PubMed:2999130"
FT /id="PRO_0000030728"
FT DOMAIN 309..436
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 319..361
FT /note="1-alpha"
FT REPEAT 362..402
FT /note="1-beta"
FT REPEAT 405..437
FT /note="1-gamma"
FT DOMAIN 439..563
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 450..485
FT /note="2-alpha"
FT REPEAT 489..528
FT /note="2-beta"
FT REPEAT 531..558
FT /note="2-gamma"
FT ACT_SITE 104
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 147
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 200
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 203
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT BINDING 32..34
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1RZO"
FT BINDING 104..105
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 145..147
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /ligand_label="3"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1RZO"
FT BINDING 324..328
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1RZO"
FT BINDING 337
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1RZO"
FT BINDING 342
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1RZO"
FT BINDING 348
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1RZO"
FT BINDING 437
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /ligand_label="3"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1RZO"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 282..306
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|Ref.4"
FT DISULFID 322..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|Ref.4"
FT DISULFID 365..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|Ref.4"
FT DISULFID 453..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|Ref.4"
FT DISULFID 492..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|Ref.4"
FT CONFLICT 331
FT /note="F -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="R -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="R -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="F -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1RZO"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 184..203
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 205..217
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 245..256
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1RZO"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:1RZO"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:1RZO"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:1RZO"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:1RZO"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:1RZO"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:1RZO"
SQ SEQUENCE 564 AA; 62851 MW; D455F2A72F609759 CRC64;
MYAVATWLCF GSTSGWSFTL EDNNIFPKQY PIINFTTADA TVESYTNFIR AVRSHLTTGA
DVRHEIPVLP NRVGLPISQR FILVELSNHA ELSVTLALDV TNAYVVGCRA GNSAYFFHPD
NQEDAEAITH LFTDVQNSFT FAFGGNYDRL EQLGGLRENI ELGTGPLEDA ISALYYYSTC
GTQIPTLARS FMVCIQMISE AARFQYIEGE MRTRIRYNRR SAPDPSVITL ENSWGRLSTA
IQESNQGAFA SPIQLQRRNG SKFNVYDVSI LIPIIALMVY RCAPPPSSQF SLLIRPVVPN
FNADVCMDPE PIVRIVGRNG LCVDVTGEEF FDGNPIQLWP CKSNTDWNQL WTLRKDSTIR
SNGKCLTISK SSPRQQVVIY NCSTATVGAT RWQIWDNRTI INPRSGLVLA ATSGNSGTKL
TVQTNIYAVS QGWLPTNNTQ PFVTTIVGLY GMCLQANSGK VWLEDCTSEK AEQQWALYAD
GSIRPQQNRD NCLTTDANIK GTVVKILSCG PASSGQRWMF KNDGTILNLY NGLVLDVRRS
DPSLKQIIVH PFHGNLNQIW LPLF
