ABRA_ABRPR
ID ABRA_ABRPR Reviewed; 528 AA.
AC P11140; P28589;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Abrin-a;
DE Contains:
DE RecName: Full=Abrin-a A chain;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
DE Contains:
DE RecName: Full=Linker peptide;
DE Contains:
DE RecName: Full=Abrin-a B chain;
DE Flags: Precursor;
OS Abrus precatorius (Indian licorice) (Glycine abrus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Abreae; Abrus.
OX NCBI_TaxID=3816;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8421313; DOI=10.1006/jmbi.1993.1029;
RA Hung C.-H., Lee M.-C., Lee T.-C., Lin J.-Y.;
RT "Primary structure of three distinct isoabrins determined by cDNA
RT sequencing. Conservation and significance.";
RL J. Mol. Biol. 229:263-267(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-251, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Seed;
RA Funatsu G., Taguchi Y., Kamenosono M., Yanaka M.;
RT "The complete amino acid sequence of the A-chain of abrin-a, a toxic
RT protein from the seeds of Abrus precatorius.";
RL Agric. Biol. Chem. 52:1095-1097(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251.
RC TISSUE=Leaf;
RX PubMed=2016300; DOI=10.1016/s0021-9258(20)89578-7;
RA Evensen G., Mathiesen A., Sundan A.;
RT "Direct molecular cloning and expression of two distinct abrin A-chains.";
RL J. Biol. Chem. 266:6848-6852(1991).
RN [4]
RP PROTEIN SEQUENCE OF 262-528.
RX PubMed=1505674; DOI=10.1016/0014-5793(92)81076-x;
RA Chen Y.-L., Chow L.-P., Tsugita A., Lin J.-Y.;
RT "The complete primary structure of abrin-a B chain.";
RL FEBS Lett. 309:115-118(1992).
RN [5]
RP MUTAGENESIS OF ASN-200.
RX PubMed=10636890; DOI=10.1074/jbc.275.3.1897;
RA Liu C.-L., Tsai C.-C., Lin S.-C., Wang L.-I., Hsu C.-I., Hwang M.-J.,
RA Lin J.-Y.;
RT "Primary structure and function analysis of the Abrus precatorius
RT agglutinin A chain by site-directed mutagenesis. Pro(199) Of amphiphilic
RT alpha-helix H impairs protein synthesis inhibitory activity.";
RL J. Biol. Chem. 275:1897-1901(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS).
RX PubMed=7608980; DOI=10.1006/jmbi.1995.0382;
RA Tahirov T.H., Lu T.-H., Liaw Y.-C., Chen Y.-L., Lin J.-Y.;
RT "Crystal structure of abrin-a at 2.14 A.";
RL J. Mol. Biol. 250:354-367(1995).
RN [7]
RP ERRATUM OF PUBMED:7608980.
RA Tahirov T.H., Lu T.-H., Liaw Y.-C., Chen Y.-L., Lin J.-Y.;
RL J. Mol. Biol. 252:154-154(1995).
CC -!- FUNCTION: The A chain is responsible for inhibiting protein synthesis
CC through the catalytic inactivation of 60S ribosomal subunits by
CC removing adenine from position 4,324 of 28S rRNA. Abrin-a is more toxic
CC than ricin.
CC -!- FUNCTION: The B chain is a galactose-specific lectin that facilitates
CC the binding of abrin to the cell membrane that precedes endocytosis.
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 -!- SUBUNIT: Disulfide-linked dimer of A and B chains.
CC -!- DOMAIN: The B chain is composed of two domains, each domain consists of
CC 3 homologous subdomains (alpha, beta, gamma).
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome-
CC inactivating protein family. Type 2 RIP subfamily. {ECO:0000305}.
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DR EMBL; M98344; AAA32624.1; -; mRNA.
DR EMBL; X54872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S32429; TZLSA.
DR PDB; 1ABR; X-ray; 2.14 A; A=2-251, B=262-528.
DR PDB; 5Z37; X-ray; 1.30 A; A=1-251.
DR PDB; 5Z3I; X-ray; 1.65 A; A=1-251.
DR PDB; 5Z3J; X-ray; 1.70 A; A=1-251.
DR PDBsum; 1ABR; -.
DR PDBsum; 5Z37; -.
DR PDBsum; 5Z3I; -.
DR PDBsum; 5Z3J; -.
DR AlphaFoldDB; P11140; -.
DR SMR; P11140; -.
DR UniLectin; P11140; -.
DR ABCD; P11140; 1 sequenced antibody.
DR EvolutionaryTrace; P11140; -.
DR Proteomes; UP000694853; Unplaced.
DR GO; GO:0005534; F:galactose binding; TAS:UniProtKB.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; TAS:UniProtKB.
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; TAS:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; TAS:UniProtKB.
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; Plant defense; Protein synthesis inhibitor;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Toxin.
FT CHAIN 1..251
FT /note="Abrin-a A chain"
FT /id="PRO_0000030729"
FT PEPTIDE 252..261
FT /note="Linker peptide"
FT /evidence="ECO:0000269|PubMed:1505674"
FT /id="PRO_0000030730"
FT CHAIN 262..528
FT /note="Abrin-a B chain"
FT /id="PRO_0000030731"
FT DOMAIN 273..400
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 283..325
FT /note="1-alpha"
FT REPEAT 326..366
FT /note="1-beta"
FT REPEAT 369..401
FT /note="1-gamma"
FT DOMAIN 403..527
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 414..449
FT /note="2-alpha"
FT REPEAT 453..492
FT /note="2-beta"
FT REPEAT 495..528
FT /note="2-gamma"
FT ACT_SITE 164
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.2"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 247..269
FT /note="Interchain (between A and B chains)"
FT DISULFID 286..305
FT DISULFID 329..346
FT DISULFID 417..430
FT DISULFID 456..473
FT MUTAGEN 200
FT /note="N->P: 46-fold less potent protein synthesis
FT inhibition."
FT /evidence="ECO:0000269|PubMed:10636890"
FT CONFLICT 1
FT /note="Q -> E (in Ref. 1; AAA32624)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="N -> Y (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="M -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="T -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="V -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:5Z37"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 148..167
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:5Z37"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:5Z37"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1ABR"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:1ABR"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 452..463
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:1ABR"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:1ABR"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:1ABR"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:1ABR"
SQ SEQUENCE 528 AA; 59244 MW; A1F76BECD5B9A827 CRC64;
QDRPIKFSTE GATSQSYKQF IEALRERLRG GLIHDIPVLP DPTTLQERNR YITVELSNSD
TESIEVGIDV TNAYVVAYRA GTQSYFLRDA PSSASDYLFT GTDQHSLPFY GTYGDLERWA
HQSRQQIPLG LQALTHGISF FRSGGNDNEE KARTLIVIIQ MVAEAARFRY ISNRVRVSIQ
TGTAFQPDAA MISLENNWDN LSRGVQESVQ DTFPNQVTLT NIRNEPVIVD SLSHPTVAVL
ALMLFVCNPP NANQSPLLIR SIVEKSKICS SRYEPTVRIG GRDGMCVDVY DNGYHNGNRI
IMWKCKDRLE ENQLWTLKSD KTIRSNGKCL TTYGYAPGSY VMIYDCTSAV AEATYWEIWD
NGTIINPKSA LVLSAESSSM GGTLTVQTNE YLMRQGWRTG NNTSPFVTSI SGYSDLCMQA
QGSNVWMADC DSNKKEQQWA LYTDGSIRSV QNTNNCLTSK DHKQGSTILL MGCSNGWASQ
RWVFKNDGSI YSLYDDMVMD VKGSDPSLKQ IILWPYTGKP NQIWLTLF
