RIP_CUCMO
ID RIP_CUCMO Reviewed; 244 AA.
AC P84531; B7SK17;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Ribosome-inactivating protein cucurmosin {ECO:0000303|PubMed:18652900};
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase {ECO:0000303|PubMed:18652900};
OS Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var.
OS moschata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3662;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABY47624.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236, PROTEIN SEQUENCE OF 1-27, X-RAY
RP CRYSTALLOGRAPHY (1.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP GLYCOSYLATION AT ASN-225, AND ACTIVE SITES.
RC TISSUE=Mesocarp {ECO:0000269|PubMed:18652900};
RX PubMed=18652900; DOI=10.1016/j.jsb.2008.06.011;
RA Hou X., Meehan E.J., Xie J., Huang M., Chen M., Chen L.;
RT "Atomic resolution structure of cucurmosin, a novel type 1 ribosome-
RT inactivating protein from the sarcocarp of Cucurbita moschata.";
RL J. Struct. Biol. 164:81-87(2008).
CC -!- FUNCTION: Has cytotoxic activity towards cancer cells, but not normal
CC cells. Inhibits the growth of the human leukemia cell line K562, the
CC murine melanoma cell line B16 and the lung adenocarcinoma cell line
CC A549 with IC(50) values of 88.1 nM, 63.4 nM and 359.3 nM respectively.
CC {ECO:0000269|PubMed:18652900}.
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:0000269|PubMed:18652900};
CC -!- PTM: The N-linked glycan consists of GlcNAc2Man3Xyl.
CC {ECO:0000269|PubMed:18652900}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC RIP subfamily. {ECO:0000255}.
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DR EMBL; EU309692; ABY47624.1; -; Genomic_DNA.
DR PDB; 3BWH; X-ray; 1.00 A; A=1-244.
DR PDBsum; 3BWH; -.
DR AlphaFoldDB; P84531; -.
DR SMR; P84531; -.
DR iPTMnet; P84531; -.
DR EvolutionaryTrace; P84531; -.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
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 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 PANTHER; PTHR33453; PTHR33453; 1.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SUPFAM; SSF56371; SSF56371; 1.
DR PROSITE; PS00275; SHIGA_RICIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Plant defense; Protein synthesis inhibitor; Toxin.
FT CHAIN 1..244
FT /note="Ribosome-inactivating protein cucurmosin"
FT /id="PRO_0000221398"
FT ACT_SITE 70
FT /evidence="ECO:0000269|PubMed:18652900"
FT ACT_SITE 109
FT /evidence="ECO:0000269|PubMed:18652900"
FT ACT_SITE 158
FT /evidence="ECO:0000269|PubMed:18652900"
FT ACT_SITE 161
FT /evidence="ECO:0000269|PubMed:18652900"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18652900"
SQ SEQUENCE 244 AA; 27008 MW; EC055E4EA8AFB38C CRC64;
NVRFDLSSAT SSSYKTFIKN LREALPKDGK VYDIPVLLST VMDSRRFILI DLVNYDGQSI
TAAIDVLNVY IVAYSTGTVS YFFQQVPAQA PKLLFKGTQQ RTLPYTGNYE NLQTAAKKLR
ENIELGLPAL DSAITTLFHY NAEAAASALL VLIQTTSEAA RFRYIELQIA NNVGTKFKPS
QTIISLENNW SALSKQIQIA KNKNGQFETP VILIDPQGNR VQITNVTSNV VTQNIQLLLN
IGAT