ABRB_ABRPR
ID ABRB_ABRPR Reviewed; 527 AA.
AC Q06077; P81374;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Abrin-b;
DE Contains:
DE RecName: Full=Abrin-b 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-b 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 260-527.
RC TISSUE=Seed;
RX PubMed=7763422; DOI=10.1271/bbb.57.166;
RA Kimura M., Sumizawa T., Funatsu G.;
RT "The complete amino acid sequences of the B-chains of abrin-a and abrin-b,
RT toxic proteins from the seeds of Abrus precatorius.";
RL Biosci. Biotechnol. Biochem. 57:166-169(1993).
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; M98345; AAA32625.1; -; mRNA.
DR PIR; S32430; S32430.
DR AlphaFoldDB; Q06077; -.
DR SMR; Q06077; -.
DR Proteomes; UP000694853; Unplaced.
DR GO; GO:0030246; F:carbohydrate 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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Lectin;
KW Plant defense; Protein synthesis inhibitor; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Toxin.
FT CHAIN 1..250
FT /note="Abrin-b A chain"
FT /id="PRO_0000030732"
FT PEPTIDE 251..260
FT /note="Linker peptide"
FT /id="PRO_0000030733"
FT CHAIN 261..527
FT /note="Abrin-b B chain"
FT /id="PRO_0000030734"
FT DOMAIN 272..399
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 282..324
FT /note="1-alpha"
FT REPEAT 325..365
FT /note="1-beta"
FT REPEAT 368..400
FT /note="1-gamma"
FT DOMAIN 402..526
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 413..448
FT /note="2-alpha"
FT REPEAT 452..491
FT /note="2-beta"
FT REPEAT 494..527
FT /note="2-gamma"
FT ACT_SITE 163
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..268
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 285..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 328..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 416..429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 455..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 282
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 350..351
FT /note="AE -> PQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="S -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="L -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="Y -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="N -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="N -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="H -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="R -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="H -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="H -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59115 MW; 3253AE490CE9494A CRC64;
QDQVIKFTTE GATSQSYKQF IEALRQRLTG GLIHGIPVLP DPTTLQERNR YISVELSNSD
TESIEAGIDV SNAYVVAYRA GNRSYFLRDA PTSASRYLFT GTQQYSLRFN GSYIDLERLA
RQTRQQIPLG LQALRHAISF LQSGTDDQEI ARTLIVIIQM ASEAARYRFI SYRVGVSIRT
NTAFQPDAAM ISLENNWDNL SGGVQQSVQD TFPNAVTLRS VNNQPVIVDS LTHQSVAVLA
LMLFVCNPPN ANQSPLLIRS IVEKSKICSS RYEPTVRIGG RNGMCVDVYD DGYHNGNRII
AWKCKDRLEE NQLWTLKSDK TIRSNGKCLT TEGYAPGNYV MIYDCTSAVA EATYWEIWDN
GTIINPKSAL VLSAESSSMG GTLTVQTNEY LMRQGWRTGN NTSPFVTSIS GYSDLCMQAQ
GSNVWLAYCD NNKKEQQWAL YTDGSIRSVQ NTNNCLTSKD HKQGSPIVLM ACSNGWASQR
WLFRNDGSIY NLHDDMVMDV KRSDPSLKEI ILHPYHGKPN QIWLTLF
