RIPT_POLML
ID RIPT_POLML Reviewed; 603 AA.
AC Q9M653;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Ribosome-inactivating protein PMRIPt {ECO:0000303|PubMed:10785398};
DE Contains:
DE RecName: Full=PMRIPt 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=PMRIPt B chain {ECO:0000303|PubMed:10785398};
DE Flags: Precursor;
GN Name=RIPt {ECO:0000312|EMBL:AAF37219.1};
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:AAF37219.1};
RN [1] {ECO:0000312|EMBL:AAF37219.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-55 AND 332-342,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, TISSUE
RP SPECIFICITY, PTM, GLYCOSYLATION, 3D-STRUCTURE MODELING, AND PHYLOGENETIC
RP 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: 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 lines CEM and Molt4 (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: Tetramer of four pairs of disulfide bound A-B chains.
CC {ECO:0000269|PubMed:10785398}.
CC -!- TISSUE SPECIFICITY: Expressed in rhizome and more abundantly in leaves
CC (at 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 -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; AF213984; AAF37219.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9M653; -.
DR SMR; Q9M653; -.
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..39
FT /evidence="ECO:0000269|PubMed:10785398"
FT CHAIN 40..311
FT /note="PMRIPt A chain"
FT /evidence="ECO:0000305|PubMed:10785398"
FT /id="PRO_0000439022"
FT PEPTIDE 312..331
FT /note="Linker peptide"
FT /evidence="ECO:0000305|PubMed:10785398"
FT /id="PRO_0000439023"
FT CHAIN 332..603
FT /note="PMRIPt B chain"
FT /evidence="ECO:0000305|PubMed:10785398"
FT /id="PRO_0000439024"
FT DOMAIN 338..466
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 348..388
FT /note="1-alpha"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT REPEAT 389..430
FT /note="1-beta"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT REPEAT 433..466
FT /note="1-gamma"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT DOMAIN 467..593
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 478..516
FT /note="2-alpha"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT REPEAT 520..558
FT /note="2-beta"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT REPEAT 561..597
FT /note="2-gamma"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT ACT_SITE 208
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 297..335
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255"
FT DISULFID 351..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 392..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 481..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 523..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 603 AA; 66734 MW; 88B61C17CA431B1E CRC64;
MRVVAGILYI VVMAICGLGI QGGTLQDYPS VYFQDSTLQQ DFPTIFFNIL AGETYGDFIA
DLREIVTRTA DTKNGSIPVL LNPAHPVPVR ERFVKVHLTG RNGKTVILAL DVTNLYVAAF
SANNVAYFFR DFSALERENL FSGMLTIRLS FTSNYVSLEH KAGVGRENIS LGPTPLDEAC
TKSLWSGTTV TEASIAKALL VVIQMVSEAA RFRHIEERVR RSFTAADHDQ LTFRPDGLML
SMENEWPSMS LEVQRSIEGG IFIGVVQLQD ESFQPLRVDN FNTLSRYTMV ALLLFRCGHP
RATAGTSSTT PAAAQIIRMP VDVLAGEEYY DEETCTVGEP TRRISGLDGL CMDVRNESNN
DGIPIQLWPC GAQRNQQWTF HTDGTIQSMG KCMTSNGYHP GDYVMIFNCS TAPVPDATKW
VVSIDGSITN PHSGLVLTAP QAAQTTILLV VRNTHSAKQG RSVGDDVEPI VTYIVGFKYM
CLQGNNENNT RVWLEDCAVD RPQQWWALYS DGTIRVDSDR SLCVTSDGHS SRDAIIILTC
DGGINQRLVF NTDGTILNPN AQLVMDVRQS NVALRQIILY QPTGNPNQQW MTMITRTRPS
LTS
