RIP1_SAMNI
ID RIP1_SAMNI Reviewed; 569 AA.
AC P93543;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Ribosome-inactivating protein SNAI';
DE Contains:
DE RecName: Full=SNAI' A chain;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
DE Contains:
DE RecName: Full=Linker peptide;
DE Contains:
DE RecName: Full=SNAI' B chain;
DE Flags: Precursor;
OS Sambucus nigra (European elder).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Dipsacales; Adoxaceae; Sambucus.
OX NCBI_TaxID=4202;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-38 AND 304-309,
RP FUNCTION, AND SUBUNIT.
RC TISSUE=Bark;
RX PubMed=9183001; DOI=10.1111/j.1432-1033.1997.00648.x;
RA van Damme E.J.M., Roy S., Barre A., Citores L., Mostafapous K., Rouge P.,
RA Van Leuven F., Girbes T., Goldstein I.J., Peumans W.J.;
RT "Elderberry (Sambucus nigra) bark contains two structurally different
RT Neu5Ac(alpha2,6)Gal/GalNAc-binding type 2 ribosome-inactivating proteins.";
RL Eur. J. Biochem. 245:648-655(1997).
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. The B chain binds to
CC cell receptors and probably facilitates the entry into the cell of the
CC A chain; B chains are also responsible for cell agglutination (lectin
CC activity). Agglutination is inhibited by Neu5Ac(alpha2,6)lactose, and
CC N-linked glycoproteins such as fetuin and orosomucoid.
CC {ECO:0000269|PubMed:9183001}.
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 -!- SUBUNIT: Disulfide-linked dimer of A and B chains.
CC {ECO:0000269|PubMed:9183001}.
CC -!- DOMAIN: The B chain is composed of two domains, each domain consists of
CC 3 homologous subdomains (alpha, beta, gamma).
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome-
CC inactivating protein family. Type 2 RIP subfamily. {ECO:0000305}.
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DR EMBL; U66191; AAC49754.1; -; mRNA.
DR AlphaFoldDB; P93543; -.
DR SMR; P93543; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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:0008152; P:metabolic process; 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; Glycosidase;
KW Hydrolase; Lectin; Plant defense; Protein synthesis inhibitor; Repeat;
KW Signal; Toxin.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:9183001"
FT CHAIN 29..291
FT /note="SNAI' A chain"
FT /id="PRO_0000030746"
FT PEPTIDE 292..303
FT /note="Linker peptide"
FT /evidence="ECO:0000269|PubMed:9183001"
FT /id="PRO_0000030747"
FT CHAIN 304..569
FT /note="SNAI' B chain"
FT /id="PRO_0000030748"
FT DOMAIN 315..435
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 325..365
FT /note="1-alpha"
FT REPEAT 366..401
FT /note="1-beta"
FT REPEAT 404..436
FT /note="1-gamma"
FT DOMAIN 437..565
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 448..488
FT /note="2-alpha"
FT REPEAT 492..530
FT /note="2-beta"
FT REPEAT 533..566
FT /note="2-gamma"
FT ACT_SITE 201
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..311
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 328..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 369..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 451..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 495..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 569 AA; 62598 MW; 82B9C889A3E1F9AD CRC64;
MKVVATILYL VVLAICGLGI HGAHPTHSAP PTVYPSVSFN LTEANSNEYR HFLQELRGKV
ILGSHRAFDL PVLNPESKVS DSDRFVLVRL TNPSRKKVTL AIDVVTFYVV AFAQNDRSYF
FSGSSEVQRE NLFVDTTQED LNFKGDYTSL EHQVGFGRVY IPLGPKSLAQ SISSLSTYKS
SAGDNKRLAR SLLVVIQMVS EAARFRYIQL RIQASITDAK EFTPDLLMLS MENKWSSMSS
EIQQAQPGGA FAQVVKLLDQ RNHPIDVTNF RRLFQLTSVA VLLHGCPTVT KMPAYIIKMP
VFNGGEDEER CSVVEEVTRR IGGRDGFCAE VKNGDEKDGT PVQLSSCGEQ SNQQWTFSTD
GTIQSLGKCL TTSSSVMIYN CKVVPPESTK WVVSIDGTIT NPRSGLVLTA PKAAEGTLVS
LEKNVHAARQ GWIVGNVEPL VTFIVGYEQM CLETNPGNND VSLGDCSVKS ASKVDQKWAL
YGDGTIRVNN DRSLCVTSEG KSSNEPIIIL KCLGWANQRW VFNTDGTISN PDSKLVMHVD
QNDVPLRKII LSHPSGTSNQ QWIASTHPA
