AGGL_ABRPR
ID AGGL_ABRPR Reviewed; 547 AA.
AC Q9M6E9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Agglutinin-1;
DE AltName: Full=Agglutinin I;
DE Contains:
DE RecName: Full=Agglutinin-1 chain A;
DE EC=3.2.2.22;
DE AltName: Full=AAG-A;
DE Contains:
DE RecName: Full=Agglutinin-1 chain B;
DE AltName: Full=AAG-B;
DE Flags: Precursor;
GN Name=AAG {ECO:0000312|EMBL:AAF28309.1};
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:0000305, ECO:0000312|EMBL:AAF28309.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-278 AND 281-543,
RP FUNCTION, AND MUTAGENESIS OF PRO-219.
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 [2] {ECO:0000305}
RP IMMUNOMODULATORY ROLE.
RX PubMed=15474989; DOI=10.1016/j.biocel.2004.07.015;
RA Tripathi S., Maiti T.K.;
RT "Immunomodulatory role of native and heat denatured agglutinin from Abrus
RT precatorius.";
RL Int. J. Biochem. Cell Biol. 37:451-462(2005).
RN [3] {ECO:0000305}
RP SUBUNIT, AND 3D-STRUCTURE MODELING.
RX PubMed=16772301; DOI=10.1074/jbc.m601777200;
RA Bagaria A., Surendranath K., Ramagopal U.A., Ramakumar S., Karande A.A.;
RT "Structure-function analysis and insights into the reduced toxicity of
RT Abrus precatorius agglutinin I in relation to abrin.";
RL J. Biol. Chem. 281:34465-34474(2006).
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 (By similarity). Less
CC toxic than abrin-a. {ECO:0000250|UniProtKB:P28590,
CC ECO:0000269|PubMed:10636890}.
CC -!- FUNCTION: The B chain is a galactose-specific lectin that facilitates
CC the binding to the cell membrane that precedes endocytosis.
CC {ECO:0000250|UniProtKB:P28590}.
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:0000250|UniProtKB:P11140};
CC -!- SUBUNIT: Heterotetramer of two A and two B chains.
CC {ECO:0000269|PubMed:16772301}.
CC -!- DOMAIN: The B chain is composed of two domains, each domain consists of
CC 3 homologous subdomains (alpha, beta, gamma). {ECO:0000255}.
CC -!- MISCELLANEOUS: Induces cytokine production and proliferation of
CC splenocytes and thymocytes in mice. {ECO:0000269|PubMed:15474989}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome-
CC inactivating protein family. Type 2 RIP subfamily. {ECO:0000255}.
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; AF190173; AAF28309.1; -; mRNA.
DR PDB; 2Q3N; X-ray; 3.50 A; A=21-280, B=281-547.
DR PDB; 2ZR1; X-ray; 2.60 A; A/C=21-278, B/D=281-547.
DR PDBsum; 2Q3N; -.
DR PDBsum; 2ZR1; -.
DR AlphaFoldDB; Q9M6E9; -.
DR SMR; Q9M6E9; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR UniLectin; Q9M6E9; -.
DR EvolutionaryTrace; Q9M6E9; -.
DR Proteomes; UP000694853; Unplaced.
DR GO; GO:0030246; F:carbohydrate binding; TAS:UniProtKB.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; NAS:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0044533; P:positive regulation of apoptotic process in another organism; IDA:UniProtKB.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lectin; Plant defense; Protein synthesis inhibitor;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:10636890"
FT CHAIN 21..278
FT /note="Agglutinin-1 chain A"
FT /id="PRO_0000248489"
FT PROPEP 279..280
FT /note="Linker peptide"
FT /evidence="ECO:0000269|PubMed:10636890"
FT /id="PRO_0000248490"
FT CHAIN 281..547
FT /note="Agglutinin-1 chain B"
FT /id="PRO_0000248491"
FT DOMAIN 292..419
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 302..344
FT /note="1-alpha"
FT /evidence="ECO:0000255"
FT REPEAT 345..385
FT /note="1-beta"
FT /evidence="ECO:0000255"
FT REPEAT 388..420
FT /note="1-gamma"
FT /evidence="ECO:0000255"
FT DOMAIN 422..546
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 433..468
FT /note="2-alpha"
FT /evidence="ECO:0000255"
FT REPEAT 472..511
FT /note="2-beta"
FT /evidence="ECO:0000255"
FT REPEAT 514..547
FT /note="2-gamma"
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /evidence="ECO:0000250|UniProtKB:P11140"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P28590"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 266..288
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 305..324
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 348..365
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 436..449
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 475..492
FT /evidence="ECO:0000250|UniProtKB:P11140,
FT ECO:0000255|PROSITE-ProRule:PRU00174"
FT MUTAGEN 219
FT /note="P->N: 7-fold more potent in protein synthesis
FT inhibition in vitro."
FT /evidence="ECO:0000269|PubMed:10636890"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:2ZR1"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 208..226
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2Q3N"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:2ZR1"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:2ZR1"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 474..482
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:2ZR1"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:2ZR1"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:2ZR1"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:2ZR1"
SQ SEQUENCE 547 AA; 61248 MW; 355A325C2354A1BD CRC64;
MKFETTKNKL HGNAYYQAQF QDPIKFTTGS ATPASYNQFI DALRERLTGG LIYGIPVLRD
PSTVEKPNQY VTVELSYSDT VSIQLGIDLT NAYVVAYRAG SESFFFRNAP ASASTYLFTG
TQQYSLPFDG NYDDLEKWAH QSRQRISLGL EALRQGIKFL RSGASDDEEI ARTLIVIIQM
VAEAARFRYV SKLVVISLSN RAAFQPDPSM LSLENTWEPL SRAVQHTVQD TFPQNVTLIN
VRQERVVVSS LSHPSVSALA LMLFVCNPLN ATQSPLLIRS VVEQSKICSS HYEPTVRIGG
RDGLCVDVSD NAYNNGNPII LWKCKDQLEV NQLWTLKSDK TIRSKGKCLT TYGYAPGNYV
MIYDCSSAVA EATYWDIWDN GTIINPKSGL VLSAESSSMG GTLTVQKNDY RMRQGWRTGN
DTSPFVTSIA GFFKLCMEAH GNSMWLDVCD ITKEEQQWAV YPDGSIRPVQ NTNNCLTCEE
HKQGATIVMM GCSNAWASQR WVFKSDGTIY NLYDDMVMDV KSSDPSLKQI ILWPYTGNAN
QMWATLF
