SNAIF_SAMNI
ID SNAIF_SAMNI Reviewed; 570 AA.
AC O22415;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Ribosome-inactivating protein SNAIf {ECO:0000303|PubMed:9541002};
DE AltName: Full=Agglutinin I;
DE Contains:
DE RecName: Full=SNAIf-A chain {ECO:0000303|PubMed:9541002};
DE EC=3.2.2.22 {ECO:0000255|RuleBase:RU004915};
DE AltName: Full=rRNA N-glycosidase {ECO:0000255|RuleBase:RU004915};
DE Contains:
DE RecName: Full=Linker peptide;
DE Contains:
DE RecName: Full=SNAIf-B chain {ECO:0000303|PubMed:9541002};
DE Contains:
DE RecName: Full=TrSNAIf {ECO:0000303|PubMed:9541002};
DE Flags: Precursor;
GN Name=SNA-If {ECO:0000303|PubMed:12023903};
GN Synonyms=LECSNA-If {ECO:0000303|PubMed:9541002},
GN SNAIf {ECO:0000303|PubMed:9541002};
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], FUNCTION (TRSNAIF), TISSUE SPECIFICITY,
RP PROTEOLYTIC PROCESSING, PROTEIN SEQUENCE OF 424-442, AND 3D-STRUCTURE
RP MODELING.
RC TISSUE=Fruit;
RX PubMed=9541002; DOI=10.1016/s0014-5793(98)00193-8;
RA Peumans W.J., Roy S., Barre A., Rouge P., van Leuven F., van Damme E.J.;
RT "Elderberry (Sambucus nigra) contains truncated Neu5Ac(alpha-
RT 2,6)Gal/GalNAc-binding type 2 ribosome-inactivating proteins.";
RL FEBS Lett. 425:35-39(1998).
RN [2]
RP FUNCTION, DOMAIN, MUTAGENESIS OF ASN-356 AND ASP-539, AND 3D-STRUCTURE
RP MODELING.
RX PubMed=12023903; DOI=10.1042/bj20020006;
RA Chen Y., Rouge P., Peumans W.J., van Damme E.J.;
RT "Mutational analysis of the carbohydrate-binding activity of the
RT NeuAc(alpha-2,6)Gal/GalNAc-specific type 2 ribosome-inactivating protein
RT from elderberry (Sambucus nigra) fruits.";
RL Biochem. J. 364:587-592(2002).
RN [3]
RP FUNCTION.
RX PubMed=18951590; DOI=10.1016/j.phytochem.2008.09.012;
RA Shahidi-Noghabi S., Van Damme E.J., Smagghe G.;
RT "Carbohydrate-binding activity of the type-2 ribosome-inactivating protein
RT SNA-I from elderberry (Sambucus nigra) is a determining factor for its
RT insecticidal activity.";
RL Phytochemistry 69:2972-2978(2008).
CC -!- FUNCTION: Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin
CC (PubMed:12023903). Behaves as a type-2 ribosome-inactivating protein
CC (PubMed:12023903). Strongly inhibits mammalian but not plant ribosomes
CC (PubMed:12023903). The A chain is responsible for inhibiting protein
CC synthesis through the catalytic inactivation of 60S ribosomal subunits
CC by removing adenine from position 4,324 of 28S rRNA (Probable). The B
CC chain binds to cell receptors and probably facilitates the entry into
CC the cell of the A chain; B chains are also responsible for cell
CC agglutination (lectin activity) (Probable). Involved in plant defense
CC against insects (PubMed:18951590). {ECO:0000269|PubMed:12023903,
CC ECO:0000269|PubMed:18951590, ECO:0000305}.
CC -!- FUNCTION: [TrSNAIf]: Binds Neu5Ac(alpha2-6)Gal/GalNAc but has no clear
CC agglutination activity. {ECO:0000269|PubMed:9541002}.
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:0000255|RuleBase:RU004915};
CC -!- SUBUNIT: Tetramer of four pairs of disulfide bound A-B chains.
CC {ECO:0000305|PubMed:12023903}.
CC -!- TISSUE SPECIFICITY: Expressed in fruits. {ECO:0000269|PubMed:9541002}.
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:0000269|PubMed:12023903}.
CC -!- PTM: The precursor is processed in two chains, A and B, that are linked
CC by a disulfide bond (PubMed:9541002). A small truncated form
CC corresponding roughly to the second ricin B-type lectin domain of the B
CC chain, TrSNAIf, can also be produced (PubMed:9541002).
CC {ECO:0000269|PubMed:9541002}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q41358}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; AF012899; AAC49989.1; -; mRNA.
DR AlphaFoldDB; O22415; -.
DR SMR; O22415; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide 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: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; 2.
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 Nucleotide-binding; Plant defense; Protein synthesis inhibitor; Repeat;
KW Signal; Toxin.
FT SIGNAL 1..28
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT CHAIN 29..289
FT /note="SNAIf-A chain"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT /id="PRO_0000437975"
FT PEPTIDE 290..308
FT /note="Linker peptide"
FT /evidence="ECO:0000250|UniProtKB:P93543"
FT /id="PRO_0000437976"
FT CHAIN 309..570
FT /note="SNAIf-B chain"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT /id="PRO_0000437977"
FT CHAIN 424..570
FT /note="TrSNAIf"
FT /evidence="ECO:0000305|PubMed:9541002"
FT /id="PRO_0000437978"
FT DOMAIN 319..439
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 329..369
FT /note="1-alpha"
FT /evidence="ECO:0000305|PubMed:12023903"
FT REPEAT 370..405
FT /note="1-beta"
FT /evidence="ECO:0000305|PubMed:12023903"
FT REPEAT 408..440
FT /note="1-gamma"
FT /evidence="ECO:0000305|PubMed:12023903"
FT DOMAIN 441..566
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 452..489
FT /note="2-alpha"
FT /evidence="ECO:0000305|PubMed:12023903"
FT REPEAT 493..531
FT /note="2-beta"
FT /evidence="ECO:0000305|PubMed:12023903"
FT REPEAT 534..567
FT /note="2-gamma"
FT /evidence="ECO:0000305|PubMed:12023903"
FT ACT_SITE 199
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 284..316
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 332..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 355
FT /note="Interchain (between two adjacent B chains)"
FT /evidence="ECO:0000250|UniProtKB:Q41358"
FT DISULFID 373..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 455..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 496..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT MUTAGEN 356
FT /note="N->S: In SNA-If-M2; loss of carbohydrate-binding
FT activity but no effect on RNA N-glycosylase activity; when
FT associated with E-539."
FT /evidence="ECO:0000269|PubMed:12023903"
FT MUTAGEN 539
FT /note="D->E: In SNA-If-M1; strongly reduced lectin activity
FT but no effect on RNA N-glycosylase activity."
FT /evidence="ECO:0000269|PubMed:12023903"
SQ SEQUENCE 570 AA; 62752 MW; 7D799D3A20764BA6 CRC64;
MRVVTKLLYL VVLAICGLGI HGALTHTRVT PPVYPSVSFN LTGADTYGPF LRALQEKVIL
GNHTAFDLPV LNPESQVSDS NRFVLVPLTN PSGDTVTLAI DVVNLYVVAF SSNGRSYFFS
GSTAVQRDNL FVDTTQEELN FTGNYISLER QVGFGRVYIP LGPKSLAQAI SSLRTYTLSA
GDTKPLARGL LVVIQMVSEA ARFRYIELRI RTSITDASEF TPDLLMLSME NNWSSMSSEI
QQAQPGGIFP GVVQLRDERN NPIEVTNFRR LFELTYIAVL LYGCAPVTSN SYTNNAIDAQ
IIKMPVFRGG GYEKVCSVVE VTRRISGWDG LCVDVRDGHY IDGNTVQLGP CGNECNQLWT
FRTDGTIRWL GKCLTTSSSV MIYDCNTVPP EATKWVVSTD GTITNPRSGL VLTAPQAAEG
TALSLENNIH AARQGWTVGD VEPLVTFIVG YKQMCLTENG ENNFVWLEDC VLNRVEQEWA
LYGDGTIRVN SNRSLCVTSE DHEPSDLIVI LKCEGSGNQR WVFNTNGTIS NPNAKLVMDV
AQSNVSLRKI ILYPPTGNPN QQWITTTQPA
