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Ribosome-inactivating protein PMRIPt [Cleaved into: PMRIPt A chain (rRNA N-glycosidase) (EC 3.2.2.22); Linker peptide; PMRIPt B chain]

 RIPT_POLML              Reviewed;         603 AA.
Q9M653;
15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 80.
RecName: Full=Ribosome-inactivating protein PMRIPt {ECO:0000303|PubMed:10785398};
Contains:
RecName: Full=PMRIPt A chain {ECO:0000303|PubMed:10785398};
AltName: Full=rRNA N-glycosidase {ECO:0000255|RuleBase:RU004915, ECO:0000303|PubMed:10785398};
EC=3.2.2.22 {ECO:0000255|RuleBase:RU004915, ECO:0000269|PubMed:10785398};
Contains:
RecName: Full=Linker peptide {ECO:0000303|PubMed:10785398};
Contains:
RecName: Full=PMRIPt B chain {ECO:0000303|PubMed:10785398};
Flags: Precursor;
Name=RIPt {ECO:0000312|EMBL:AAF37219.1};
Polygonatum multiflorum (Solomon's seal).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
Nolinoideae; Polygonatum.
NCBI_TaxID=45371 {ECO:0000312|EMBL:AAF37219.1};
[1] {ECO:0000312|EMBL:AAF37219.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-55 AND
332-342, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT,
TISSUE SPECIFICITY, PTM, GLYCOSYLATION, 3D-STRUCTURE MODELING, AND
PHYLOGENETIC ANALYSIS.
TISSUE=Meristem {ECO:0000303|PubMed:10785398};
PubMed=10785398; DOI=10.1046/j.1432-1327.2000.01295.x;
Van Damme E.J., Hao Q., Charels D., Barre A., Rouge P., Van Leuven F.,
Peumans W.J.;
"Characterization and molecular cloning of two different type 2
ribosome-inactivating proteins from the monocotyledonous plant
Polygonatum multiflorum.";
Eur. J. Biochem. 267:2746-2759(2000).
-!- FUNCTION: GalNAc-specific agglutinin. Behaves as a type-2
ribosome-inactivating protein. Inhibits mammalian ribosomes
(PubMed:10785398). 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 (Probable). The B chain binds to cell receptors and probably
facilitates the entry into the cell of the A chain; B chains are
also responsible for cell agglutination (lectin activity)
(Probable). Involved in plant defense against insects (By
similarity). Has very low cytotoxic activity against the human
tumor cell lines CEM and Molt4 (PubMed:10785398).
{ECO:0000250|UniProtKB:O22415, ECO:0000269|PubMed:10785398,
ECO:0000305}.
-!- CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one
specific adenosine on the 28S rRNA.
{ECO:0000255|RuleBase:RU004915, ECO:0000255|SAAS:SAAS00357228,
ECO:0000269|PubMed:10785398}.
-!- ENZYME REGULATION: Strongly inhibited by asialofetuin and
asialomucin. {ECO:0000269|PubMed:10785398}.
-!- SUBUNIT: Tetramer of four pairs of disulfide bound A-B chains.
{ECO:0000269|PubMed:10785398}.
-!- TISSUE SPECIFICITY: Expressed in rhizome and more abundantly in
leaves (at protein level). {ECO:0000269|PubMed:10785398}.
-!- DOMAIN: The B-chain consists of six tandemly repeated subdomains.
Only subdomains 1-alpha and 2-gamma possess a functional
carbohydrate-binding site. {ECO:0000250|UniProtKB:Q41358}.
-!- PTM: The precursor is processed in two chains, A and B, that are
linked by a disulfide bond. {ECO:0000269|PubMed:10785398}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:10785398}.
-!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
Type 2 RIP subfamily. {ECO:0000305}.
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EMBL; AF213984; AAF37219.1; -; Genomic_DNA.
ProteinModelPortal; Q9M653; -.
SMR; Q9M653; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0030598; F:rRNA N-glycosylase activity; IDA:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
CDD; cd00161; RICIN; 2.
Gene3D; 3.40.420.10; -; 1.
Gene3D; 4.10.470.10; -; 1.
InterPro; IPR036041; Ribosome-inact_prot_sf.
InterPro; IPR017989; Ribosome_inactivat_1/2.
InterPro; IPR001574; Ribosome_inactivat_prot.
InterPro; IPR017988; Ribosome_inactivat_prot_CS.
InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00652; Ricin_B_lectin; 2.
Pfam; PF00161; RIP; 1.
PRINTS; PR00396; SHIGARICIN.
SMART; SM00458; RICIN; 2.
SUPFAM; SSF50370; SSF50370; 2.
SUPFAM; SSF56371; SSF56371; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 2.
PROSITE; PS00275; SHIGA_RICIN; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Lectin; Plant defense; Protein synthesis inhibitor; Repeat; Signal;
Toxin.
SIGNAL 1 39 {ECO:0000269|PubMed:10785398}.
CHAIN 40 311 PMRIPt A chain.
{ECO:0000305|PubMed:10785398}.
/FTId=PRO_0000439022.
PEPTIDE 312 331 Linker peptide.
{ECO:0000305|PubMed:10785398}.
/FTId=PRO_0000439023.
CHAIN 332 603 PMRIPt B chain.
{ECO:0000305|PubMed:10785398}.
/FTId=PRO_0000439024.
DOMAIN 338 466 Ricin B-type lectin 1.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REPEAT 348 388 1-alpha. {ECO:0000250|UniProtKB:Q41358}.
REPEAT 389 430 1-beta. {ECO:0000250|UniProtKB:Q41358}.
REPEAT 433 466 1-gamma. {ECO:0000250|UniProtKB:Q41358}.
DOMAIN 467 593 Ricin B-type lectin 2.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REPEAT 478 516 2-alpha. {ECO:0000250|UniProtKB:Q41358}.
REPEAT 520 558 2-beta. {ECO:0000250|UniProtKB:Q41358}.
REPEAT 561 597 2-gamma. {ECO:0000250|UniProtKB:Q41358}.
ACT_SITE 208 208 {ECO:0000250|UniProtKB:P02879}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 297 335 Interchain (between A and B chains).
{ECO:0000255}.
DISULFID 351 370 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 392 409 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 481 497 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 523 540 {ECO:0000255|PROSITE-ProRule:PRU00174}.
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


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