ID ABRC_ABRPR Reviewed; 562 AA.
AC P28590;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Abrin-c;
DE Contains:
DE RecName: Full=Abrin-c 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-c 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 [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=2050149; DOI=10.1111/j.1432-1033.1991.tb16072.x;
RA Wood K.A., Lord J.M., Wawrzynczak E.J., Piatak M.;
RT "Preproabrin: genomic cloning, characterisation and the expression of the
RT A-chain in Escherichia coli.";
RL Eur. J. Biochem. 198:723-732(1991).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC STRAIN=GIS04; TISSUE=Seed;
RA Ingale A.G.;
RT "Detection and partial characterization of lectin from Abrus
RT precatorius.L.";
RL Submitted (APR-2009) to UniProtKB.
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. {ECO:0000269|Ref.2}.
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 {ECO:0000269|Ref.2}.
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; X55667; CAA39202.1; -; Genomic_DNA.
DR PIR; S16022; S16022.
DR AlphaFoldDB; P28590; -.
DR SMR; P28590; -.
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; 2.80.10.50; -; 2.
DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1.
DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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; -; 1.
DR PANTHER; PTHR33453:SF34; DUF6598 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 2.
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; Signal; Toxin.
FT SIGNAL 1..34
FT /evidence="ECO:0000250"
FT CHAIN 35..285
FT /note="Abrin-c A chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030735"
FT PEPTIDE 286..295
FT /note="Linker peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030736"
FT CHAIN 296..562
FT /note="Abrin-c B chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030737"
FT DOMAIN 307..434
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 317..359
FT /note="1-alpha"
FT REPEAT 360..400
FT /note="1-beta"
FT REPEAT 403..435
FT /note="1-gamma"
FT DOMAIN 437..561
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 448..483
FT /note="2-alpha"
FT REPEAT 487..526
FT /note="2-beta"
FT REPEAT 529..562
FT /note="2-gamma"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 281..303
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 320..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 363..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 451..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 490..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 562 AA; 62818 MW; 1FD0ABC7D7BA6278 CRC64;
MDKTLKLLIL CLAWTCSFSA LRCAARTYPP VATNQDQVIK FTTEGATSQS YKQFIEALRQ
RLTGGLIHDI PVLPDPTTVE ERNRYITVEL SNSERESIEV GIDVTNAYVV AYRAGSQSYF
LRDAPASAST YLFPGTQRYS LRFDGSYGDL ERWAHQTREE ISLGLQALTH AISFLRSGAS
NDEEKARTLI VIIQMASEAA RYRYISNRVG VSIRTGTAFQ PDPAMLSLEN NWDNLSGGVQ
QSVQDTFPNN VILSSINRQP VVVDSLSHPT VAVLALMLFV CNPPNANQSP LLIRSIVEES
KICSSRYEPT VRIGGRDGMC VDVYDDGYHN GNRIIAWKCK DRLEENQLWT LKSDKTIRSN
GKCLTTEGYA PGNYVMIYDC TSAVAEATYW EIWDNGTIIN PKSALVLSAE SSSMGGTLTV
QTNEYLMRQG WRTGNNTSPF VTSISGYSDL CMQAQGSNVW LADCDNNKKE QQWALYTDGS
IRSVQNTNNC LTSKDHKQGS PIVLMACSNG WASQRWLFKN DGSIYNLHDD MVMDVKRSDP
SLKEIILHPY HGKPNQIWLT LF
//
