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 27-MAR-2024, entry version 140. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 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 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 //