ABRD_ABRPR
ID ABRD_ABRPR Reviewed; 528 AA.
AC Q06076;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Abrin-d;
DE Contains:
DE RecName: Full=Abrin-d 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-d 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] {ECO:0000312|EMBL:AAA32626.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endosperm {ECO:0000269|PubMed:8421313};
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).
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. {ECO:0000305}.
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:0000305}.
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 Evidence={ECO:0000255|RuleBase:RU003711};
CC -!- SUBUNIT: Disulfide-linked dimer of A and B chains. {ECO:0000305}.
CC -!- DOMAIN: The B chain is composed of two domains, each domain consists of
CC 3 homologous subdomains (alpha, beta, gamma). {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome-
CC inactivating protein family. Type 2 RIP subfamily. {ECO:0000255}.
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DR EMBL; M98346; AAA32626.1; -; mRNA.
DR PIR; S32431; S32431.
DR AlphaFoldDB; Q06076; -.
DR SMR; Q06076; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lectin; Plant defense;
KW Protein synthesis inhibitor; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Toxin.
FT CHAIN 1..251
FT /note="Abrin-d A chain"
FT /evidence="ECO:0000250|UniProtKB:P11140"
FT /id="PRO_0000030738"
FT PEPTIDE 252..261
FT /note="Linker peptide"
FT /evidence="ECO:0000250|UniProtKB:P11140"
FT /id="PRO_0000030739"
FT CHAIN 262..528
FT /note="Abrin-d B chain"
FT /evidence="ECO:0000250|UniProtKB:P11140"
FT /id="PRO_0000030740"
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 /evidence="ECO:0000250|UniProtKB:P11140"
FT REPEAT 326..366
FT /note="1-beta"
FT /evidence="ECO:0000250|UniProtKB:P11140"
FT REPEAT 369..401
FT /note="1-gamma"
FT /evidence="ECO:0000250|UniProtKB:P11140"
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 /evidence="ECO:0000250|UniProtKB:P11140"
FT REPEAT 453..492
FT /note="2-beta"
FT /evidence="ECO:0000250|UniProtKB:P11140"
FT REPEAT 495..528
FT /note="2-gamma"
FT /evidence="ECO:0000250|UniProtKB:P11140"
FT ACT_SITE 164
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P11140"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 247..269
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 286..305
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 329..346
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 417..430
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 456..473
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 528 AA; 58870 MW; 62ED42FB8FFE60F8 CRC64;
QDQVIKFTTE GATSQSYKQF IEALRQRLTG GLIHDIPVLP DPTTVEERNR YITVELSNSE
RESIEVGIDV TNAYVVAYRA GSQSYFLRDA PASASTYLFP GTQRYSLRFD GSYGDLERWA
HQTREEISLG LQALTHAISF LRSGASNDEE KARTLIVIIQ MASEAARYRC ISNRVGVSIR
TGTAFQPDPA MLSLENNWDN LSGGVQQSVQ DAFPNNVILS SINRQPVVVD SLSHPTVAVL
ALMLFVCNPP NANQSPLLIR SIVEESKICS SRYEPTVRIG GRDGMCVDVY DDGYHNGNRI
IAWKCKDRLE ENQLWTLKSD LTIRSNGKCL TTEGYAPGNY VMIYDCTSAV AEATYWEIWD
NGTIINPKSA LVLSAESSSM GGTLTVQTNE YLMRQGWRTG NNTSPFVTSI SGYSDLCMQA
QGSNVWLADC DNNKKEQQWA LYTDGSIRSV QNTNNCLTSK DHKQGSPIVL MACSNGWASQ
RWLFKNDGSI YSLYDDMVMD VKGSDPSLKQ IILWPYTGKP NQIWLTLF
