SNAIB_SAMNI
ID SNAIB_SAMNI Reviewed; 570 AA.
AC Q41358;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Ribosome-inactivating protein SNAI {ECO:0000303|PubMed:8631319};
DE AltName: Full=Agglutinin I;
DE Contains:
DE RecName: Full=SNAI-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=SNAI-B chain {ECO:0000303|PubMed:9541002};
DE Contains:
DE RecName: Full=TrSNAI {ECO:0000303|PubMed:9541002};
DE Flags: Precursor;
GN Name=SNA-I {ECO:0000303|PubMed:9541002};
GN Synonyms=LECSNAI {ECO:0000303|PubMed:8631319},
GN SNAI {ECO:0000303|PubMed:8631319};
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, PROTEIN SEQUENCE OF 29-39 AND
RP 309-319, 3D-STRUCTURE MODELING, SUBUNIT, DOMAIN, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Bark;
RX PubMed=8631319; DOI=10.1111/j.1432-1033.1996.00128.x;
RA Van Damme E.J., Barre A., Rouge P., Van Leuven F., Peumans W.J.;
RT "The NeuAc(alpha-2,6)-Gal/GalNAc-binding lectin from elderberry (Sambucus
RT nigra) bark, a type-2 ribosome-inactivating protein with an unusual
RT specificity and structure.";
RL Eur. J. Biochem. 235:128-137(1996).
RN [2]
RP FUNCTION (TRSNAI), PROTEOLYTIC PROCESSING, PROTEIN SEQUENCE OF 434-453, AND
RP 3D-STRUCTURE MODELING.
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 [3]
RP FUNCTION.
RX PubMed=3805045; DOI=10.1016/s0021-9258(19)75677-4;
RA Shibuya N., Goldstein I.J., Broekaert W.F., Nsimba-Lubaki M., Peeters B.,
RA Peumans W.J.;
RT "The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha
RT 2-6)Gal/GalNAc sequence.";
RL J. Biol. Chem. 262:1596-1601(1987).
RN [4]
RP GLYCOSYLATION AT ASN-40; ASN-62; ASN-144; ASN-260; ASN-492 AND ASN-526.
RX PubMed=27384337; DOI=10.1007/s10719-016-9698-7;
RA Gnanesh Kumar B.S., Surolia A.;
RT "Site specific N-glycan profiling of NeuAc(alpha2-6)-Gal/GalNAc-binding
RT bark Sambucus nigra agglutinin using LC-MS(n) revealed differential
RT glycosylation.";
RL Glycoconj. J. 33:907-915(2016).
CC -!- FUNCTION: Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin
CC (PubMed:3805045). Behaves as a type-2 ribosome-inactivating protein
CC (PubMed:8631319). Strongly inhibits mammalian but not plant ribosomes
CC (PubMed:8631319). 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 (By similarity). {ECO:0000250|UniProtKB:O22415,
CC ECO:0000269|PubMed:3805045, ECO:0000269|PubMed:8631319, ECO:0000305}.
CC -!- FUNCTION: [TrSNAI]: 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:8631319}.
CC -!- TISSUE SPECIFICITY: Expressed in bark. {ECO:0000269|PubMed:8631319}.
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:0000305|PubMed:8631319}.
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, TrSNAI, can also be produced (PubMed:9541002).
CC {ECO:0000269|PubMed:9541002}.
CC -!- PTM: Glycosylated (PubMed:8631319, PubMed:27384337). N-glycans of
CC subunit A are (Man)2-3(Xyl)(GlcNAc)2(Fuc) at Asn-40, (GlcNAc)0-
CC 2(Man)3(Xyl)(GlcNAc)2(Fuc) or (Man)1-2(GlcNAc)2 at Asn-62,
CC (Man)3(Xyl)(GlcNAc)2(Fuc)0-1 at Asn-144 and (GlcNAc)0-
CC 1(Man)3(Xyl)(GlcNAc)2(Fuc) at Asn-260 (PubMed:27384337). N-glycans of
CC subunit B are (Man)3(Xyl)(GlcNAc)2(Fuc) at Asn-492 and (Man)6-
CC 9(GlcNAc)2 at Asn-526 (PubMed:27384337). {ECO:0000269|PubMed:27384337,
CC ECO:0000269|PubMed:8631319}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; U27122; AAC49158.1; -; mRNA.
DR PIR; S62627; S62627.
DR AlphaFoldDB; Q41358; -.
DR SMR; Q41358; -.
DR iPTMnet; Q41358; -.
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:0000269|PubMed:8631319"
FT CHAIN 29..289
FT /note="SNAI-A chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437971"
FT PEPTIDE 290..308
FT /note="Linker peptide"
FT /evidence="ECO:0000250|UniProtKB:P93543"
FT /id="PRO_0000437972"
FT CHAIN 309..570
FT /note="SNAI-B chain"
FT /evidence="ECO:0000305|PubMed:8631319"
FT /id="PRO_0000437973"
FT CHAIN 434..570
FT /note="TrSNAI"
FT /evidence="ECO:0000305|PubMed:9541002"
FT /id="PRO_0000437974"
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:8631319"
FT REPEAT 370..405
FT /note="1-beta"
FT /evidence="ECO:0000305|PubMed:8631319"
FT REPEAT 408..440
FT /note="1-gamma"
FT /evidence="ECO:0000305|PubMed:8631319"
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:8631319"
FT REPEAT 493..531
FT /note="2-beta"
FT /evidence="ECO:0000305|PubMed:8631319"
FT REPEAT 534..567
FT /note="2-gamma"
FT /evidence="ECO:0000305|PubMed:8631319"
FT ACT_SITE 199
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27384337"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27384337"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27384337"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27384337"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27384337"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27384337"
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:0000305|PubMed:8631319"
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"
SQ SEQUENCE 570 AA; 63102 MW; A059E2A3E868B868 CRC64;
MRLVAKLLYL AVLAICGLGI HGALTHPRVT PPVYPSVSFN LTGADTYEPF LRALQEKVIL
GNHTAFDLPV LNPESQVSDS NRFVLVPLTN PSGDTVTLAI DVVNLYVVAF SSNGKSYFFS
GSTAVQRDNL FVDTTQEELN FTGNYTSLER QVGFGRVYIP LGPKSLDQAI SSLRTYTLTA
GDTKPLARGL LVVIQMVSEA ARFRYIELRI RTSITDASEF TPDLLMLSME NNWSSMSSEI
QQAQPGGIFA GVVQLRDERN NSIEVTNFRR LFELTYIAVL LYGCAPVTSS SYSNNAIDAQ
IIKMPVFRGG EYEKVCSVVE VTRRISGWDG LCVDVRYGHY IDGNPVQLRP CGNECNQLWT
FRTDGTIRWL GKCLTASSSV MIYDCNTVPP EATKWVVSID GTITNPHSGL VLTAPQAAEG
TALSLENNIH AARQGWTVGD VEPLVTFIVG YKQMCLRENG ENNFVWLEDC VLNRVQQEWA
LYGDGTIRVN SNRSLCVTSE DHEPSDLIVI LKCEGSGNQR WVFNTNGTIS NPNAKLLMDV
AQRDVSLRKI ILYRPTGNPN QQWITTTHPA
