RIPM_POLML
ID RIPM_POLML Reviewed; 604 AA.
AC Q9M654;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Ribosome-inactivating protein PMRIPm {ECO:0000303|PubMed:10785398};
DE Contains:
DE RecName: Full=PMRIPm A chain {ECO:0000303|PubMed:10785398};
DE AltName: Full=rRNA N-glycosidase {ECO:0000255|RuleBase:RU004915, ECO:0000303|PubMed:10785398};
DE EC=3.2.2.22 {ECO:0000255|RuleBase:RU004915, ECO:0000269|PubMed:10785398};
DE Contains:
DE RecName: Full=Linker peptide {ECO:0000303|PubMed:10785398};
DE Contains:
DE RecName: Full=PMRIPm B chain {ECO:0000303|PubMed:10785398};
DE Flags: Precursor;
GN Name=RIPm {ECO:0000312|EMBL:AAF37218.1};
OS Polygonatum multiflorum (Solomon's seal).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Nolinoideae; Polygonatum.
OX NCBI_TaxID=45371 {ECO:0000312|EMBL:AAF37218.1};
RN [1] {ECO:0000312|EMBL:AAF37218.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 329-339, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, TISSUE SPECIFICITY, PTM,
RP GLYCOSYLATION, 3D-STRUCTURE MODELING, AND PHYLOGENETIC ANALYSIS.
RC TISSUE=Meristem {ECO:0000303|PubMed:10785398};
RX PubMed=10785398; DOI=10.1046/j.1432-1327.2000.01295.x;
RA Van Damme E.J., Hao Q., Charels D., Barre A., Rouge P., Van Leuven F.,
RA Peumans W.J.;
RT "Characterization and molecular cloning of two different type 2 ribosome-
RT inactivating proteins from the monocotyledonous plant Polygonatum
RT multiflorum.";
RL Eur. J. Biochem. 267:2746-2759(2000).
CC -!- FUNCTION: Gal/GalNAc-specific agglutinin. Behaves as a type-2 ribosome-
CC inactivating protein. Inhibits mammalian ribosomes (PubMed:10785398).
CC The A chain is responsible for inhibiting protein synthesis through the
CC catalytic inactivation of 60S ribosomal subunits by removing adenine
CC from position 4,324 of 28S rRNA (Probable). The B chain binds to cell
CC receptors and probably facilitates the entry into the cell of the A
CC chain; B chains are also responsible for cell agglutination (lectin
CC activity) (Probable). Involved in plant defense against insects (By
CC similarity). Has very low cytotoxic activity against the human tumor
CC cell line Molt4, but higher against CEM (PubMed:10785398).
CC {ECO:0000250|UniProtKB:O22415, ECO:0000269|PubMed:10785398,
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; Evidence={ECO:0000255,
CC ECO:0000255|RuleBase:RU004915, ECO:0000269|PubMed:10785398};
CC -!- ACTIVITY REGULATION: Strongly inhibited by asialofetuin and
CC asialomucin. {ECO:0000269|PubMed:10785398}.
CC -!- SUBUNIT: Disulfide-linked dimer of A and B chains.
CC {ECO:0000269|PubMed:10785398}.
CC -!- TISSUE SPECIFICITY: Expressed in rhizome and abundantly in leaves (at
CC protein level). {ECO:0000269|PubMed:10785398}.
CC -!- DOMAIN: The B-chain consists of six tandemly repeated subdomains. Only
CC subdomains 1-alpha and 2-gamma possess a functional carbohydrate-
CC binding site. {ECO:0000250|UniProtKB:Q41358}.
CC -!- PTM: The precursor is processed in two chains, A and B, that are linked
CC by a disulfide bond. {ECO:0000269|PubMed:10785398}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:10785398}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10785398}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; AF213983; AAF37218.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9M654; -.
DR SMR; Q9M654; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IDA: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; 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Lectin;
KW Plant defense; Protein synthesis inhibitor; Repeat; Signal; Toxin.
FT SIGNAL 1..43
FT /evidence="ECO:0000250|UniProtKB:Q9M653"
FT CHAIN 44..310
FT /note="PMRIPm A chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439025"
FT PEPTIDE 311..328
FT /note="Linker peptide"
FT /evidence="ECO:0000305|PubMed:10785398"
FT /id="PRO_0000439026"
FT CHAIN 329..604
FT /note="PMRIPm B chain"
FT /evidence="ECO:0000305|PubMed:10785398"
FT /id="PRO_0000439027"
FT DOMAIN 335..463
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 345..387
FT /note="1-alpha"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT REPEAT 389..429
FT /note="1-beta"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT REPEAT 432..465
FT /note="1-gamma"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT DOMAIN 466..598
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 477..521
FT /note="2-alpha"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT REPEAT 525..563
FT /note="2-beta"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT REPEAT 566..599
FT /note="2-gamma"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT ACT_SITE 211
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 301..332
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255"
FT DISULFID 348..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 392..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 480..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 331..332
FT /note="KC -> MP (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 67060 MW; 6206C2B25F908D4E CRC64;
MRVVAAILYI NVVVALICGL GIQGGALDLQ DYPSVSFQGD AMQLQDYPSI TFNLKGATWQ
TYRDFIEKLR EIVTRGATTI AGTSIPVLNR VVPDSRRFVY VRLINLDGNV VTIAVDVTSL
YVVAFSANNN GYFFSDSTET ERTNLFVGIP RGDPLGFTGN YNSLENWAGA DRGSIPLGPA
LLNKAIRNLR SNGRDSKAAK SLIVVIQMVS EAARFRRIEE QVRRSIADQD TFTPGSLMIT
MEKKWSKMSQ QVERSVNDQG IFTGIFTRTV QLIDDNLQTL NIDNFNALSL HTMLAILLFR
CRTTTSSHNT LPAASNIVLM GEDYVDKDDE KCTVGEPTRR ISGRAGWCVD VKDGRDNDGN
PIQVLSCGDG QERKQQWTFH RDGTIRSKLG KCMTAYGFKH GEYVMIYDCD TAIAGANKWV
VSIDGTITNP ISGLVLTAPR GATGTTLLVE KNVHAARQCW RVGDDVEPIV TKIVGFQEKC
LEANYLENTN VSRYTKVFLD DCVLDRQQQR WALYSDGTIR ADSDRSLRVT ADGHRSLDSI
IILACKGWGN QRWVFNTDGT ILNPNAKLVM DVKDSDVSLL QIILHQSTGK PNQKWLTVTL
PRTS
