Reviewed, UniProtKB/Swiss-Prot Q06076 (ABRD_ABRPR)

Names and origin

Protein names	Recommended name:     Abrin-d Cleaved into the following 3 chains:     1- Recommended name:             Abrin-d A chain               EC=3.2.2.22         Alternative name(s):             rRNA N-glycosidase     2- Recommended name:             Linker peptide     3- Recommended name:             Abrin-d B chain
Organism	Abrus precatorius (Indian licorice) (Crab's eye)
Taxonomic identifier	3816 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Abreae › Abrus

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain is a galactose-specific lectin that facilitates the binding of abrin to the cell membrane that precedes endocytosis.
Catalytic activity	Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Subunit structure	Disulfide-linked dimer of A and B chains.
Domain	The B chain is composed of two domains, each domain consists of 3 homologous subdomains (alpha, beta, gamma).
Sequence similarities	In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily. Contains 2 ricin B-type lectin domains.

Ontologies

Keywords
Biological process	Plant defense
Domain	Repeat
Ligand	Lectin
Molecular function	Hydrolase Protein synthesis inhibitor Toxin
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Gene Ontology (GO)
Biological process	defense response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	rRNA N-glycosylase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 251	251	Abrin-d A chain By similarity UniProtKB P11140		PRO_0000030738
	Peptide	252 – 261	10	Linker peptide By similarity UniProtKB P11140		PRO_0000030739
	Chain	262 – 528	267	Abrin-d B chain By similarity UniProtKB P11140		PRO_0000030740
Regions
	Domain	273 – 400	128	Ricin B-type lectin 1
	Repeat	283 – 325	43	1-alpha UniProtKB P11140
	Repeat	326 – 366	41	1-beta UniProtKB P11140
	Repeat	369 – 401	33	1-gamma UniProtKB P11140
	Domain	403 – 527	125	Ricin B-type lectin 2
	Repeat	414 – 449	36	2-alpha UniProtKB P11140
	Repeat	453 – 492	40	2-beta UniProtKB P11140
	Repeat	495 – 528	34	2-gamma UniProtKB P11140
Sites
	Active site	164	1	By similarity UniProtKB P02879
Amino acid modifications
	Modified residue	1	1	Pyrrolidone carboxylic acid By similarity UniProtKB P11140
	Glycosylation	200	1	N-linked (GlcNAc...) Potential
	Glycosylation	361	1	N-linked (GlcNAc...) Potential
	Glycosylation	401	1	N-linked (GlcNAc...) Potential
	Disulfide bond	247 ↔ 269		Interchain (between A and B chains) By similarity UniProtKB P11140
	Disulfide bond	286 ↔ 305		By similarity UniProtKB P11140
	Disulfide bond	329 ↔ 346		By similarity UniProtKB P11140
	Disulfide bond	417 ↔ 430		By similarity UniProtKB P11140
	Disulfide bond	456 ↔ 473		By similarity UniProtKB P11140

Sequences

	Sequence		Length	Mass (Da)
	Q06076-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 62ED42FB8FFE60F8	FASTA	528	58,870
	10 20 30 40 50 60 QDQVIKFTTE GATSQSYKQF IEALRQRLTG GLIHDIPVLP DPTTVEERNR YITVELSNSE 70 80 90 100 110 120 RESIEVGIDV TNAYVVAYRA GSQSYFLRDA PASASTYLFP GTQRYSLRFD GSYGDLERWA 130 140 150 160 170 180 HQTREEISLG LQALTHAISF LRSGASNDEE KARTLIVIIQ MASEAARYRC ISNRVGVSIR 190 200 210 220 230 240 TGTAFQPDPA MLSLENNWDN LSGGVQQSVQ DAFPNNVILS SINRQPVVVD SLSHPTVAVL 250 260 270 280 290 300 ALMLFVCNPP NANQSPLLIR SIVEESKICS SRYEPTVRIG GRDGMCVDVY DDGYHNGNRI 310 320 330 340 350 360 IAWKCKDRLE ENQLWTLKSD LTIRSNGKCL TTEGYAPGNY VMIYDCTSAV AEATYWEIWD 370 380 390 400 410 420 NGTIINPKSA LVLSAESSSM GGTLTVQTNE YLMRQGWRTG NNTSPFVTSI SGYSDLCMQA 430 440 450 460 470 480 QGSNVWLADC DNNKKEQQWA LYTDGSIRSV QNTNNCLTSK DHKQGSPIVL MACSNGWASQ 490 500 510 520 RWLFKNDGSI YSLYDDMVMD VKGSDPSLKQ IILWPYTGKP NQIWLTLF

References

[1]	"Primary structure of three distinct isoabrins determined by cDNA sequencing. Conservation and significance." Hung C.-H., Lee M.-C., Lee T.-C., Lin J.-Y. J. Mol. Biol. 229:263-267(1993) [PubMed: 8421313] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Endosperm.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M98346 mRNA. Translation: AAA32626.1.
PIR	S32431.
3D structure databases
HSSP	HSSP built from PDB template 1ABR based on UniProtKB P11140.
SMR	Q06076. Positions 1-251, 262-528.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.2.2.22. 273549.
Family and domain databases
InterPro	IPR001574. Ribosome_inactivat_prot. IPR017988. Ribosome_inactivat_prot_CS. IPR016138. Ribosome_inactivat_prot_sub1. IPR016139. Ribosome_inactivat_prot_sub2. IPR017989. Ribosome_inactivat_prot_subgr. IPR000772. Ricin_B_lectin. [Graphical view]
Gene3D	G3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit. G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 1 hit.
Pfam	PF00652. Ricin_B_lectin. 2 hits. PF00161. RIP. 1 hit. [Graphical view]
PRINTS	PR00396. SHIGARICIN.
SMART	SM00458. RICIN. 2 hits. [Graphical view]
PROSITE	PS50231. RICIN_B_LECTIN. 2 hits. PS00275. SHIGA_RICIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ABRD_ABRPR

Accession

Primary (citable) accession number: Q06076

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)