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 27-MAR-2024, entry version 98. 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}, SNAIf GN {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 RT Neu5Ac(alpha-2,6)Gal/GalNAc-binding type 2 ribosome-inactivating RT 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF012899; AAC49989.1; -; mRNA. DR AlphaFoldDB; O22415; -. DR SMR; O22415; -. DR GlyCosmos; O22415; 7 sites, No reported glycans. 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; 2.80.10.50; -; 2. DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1. DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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; -; 1. DR PANTHER; PTHR33453:SF34; DUF6598 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00652; Ricin_B_lectin; 2. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR SMART; SM00458; RICIN; 2. DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 2. 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 RNAN-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 RNAN-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 //