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Protein

Ribosome-inactivating protein SNAI'

Gene
N/A
Organism
Sambucus nigra (European elder)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Agglutination is inhibited by Neu5Ac(alpha2,6)lactose, and N-linked glycoproteins such as fetuin and orosomucoid.1 Publication

Catalytic activityi

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei201By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Protein synthesis inhibitor, Toxin
Biological processPlant defense
LigandLectin

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-inactivating protein SNAI'
Cleaved into the following 3 chains:
Alternative name(s):
rRNA N-glycosidase
OrganismiSambucus nigra (European elder)
Taxonomic identifieri4202 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsDipsacalesAdoxaceaeSambucus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000003074629 – 291SNAI' A chainAdd BLAST263
PeptideiPRO_0000030747292 – 303Linker peptide1 PublicationAdd BLAST12
ChainiPRO_0000030748304 – 569SNAI' B chainAdd BLAST266

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi286 ↔ 311Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi328 ↔ 347PROSITE-ProRule annotation
Disulfide bondi369 ↔ 381PROSITE-ProRule annotation
Disulfide bondi451 ↔ 466PROSITE-ProRule annotation
Disulfide bondi495 ↔ 512PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP93543

Interactioni

Subunit structurei

Disulfide-linked dimer of A and B chains.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP93543
SMRiP93543
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini315 – 435Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST121
Repeati325 – 3651-alphaAdd BLAST41
Repeati366 – 4011-betaAdd BLAST36
Repeati404 – 4361-gammaAdd BLAST33
Domaini437 – 565Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST129
Repeati448 – 4882-alphaAdd BLAST41
Repeati492 – 5302-betaAdd BLAST39
Repeati533 – 5662-gammaAdd BLAST34

Domaini

The B chain is composed of two domains, each domain consists of 3 homologous subdomains (alpha, beta, gamma).

Sequence similaritiesi

In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

CDDicd00161 RICIN, 2 hits
Gene3Di3.40.420.10, 1 hit
4.10.470.10, 1 hit
InterProiView protein in InterPro
IPR036041 Ribosome-inact_prot_sf
IPR017989 Ribosome_inactivat_1/2
IPR001574 Ribosome_inactivat_prot
IPR017988 Ribosome_inactivat_prot_CS
IPR016138 Ribosome_inactivat_prot_sub1
IPR016139 Ribosome_inactivat_prot_sub2
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PfamiView protein in Pfam
PF00652 Ricin_B_lectin, 2 hits
PF00161 RIP, 1 hit
PRINTSiPR00396 SHIGARICIN
SMARTiView protein in SMART
SM00458 RICIN, 2 hits
SUPFAMiSSF50370 SSF50370, 2 hits
SSF56371 SSF56371, 1 hit
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 2 hits
PS00275 SHIGA_RICIN, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P93543-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVVATILYL VVLAICGLGI HGAHPTHSAP PTVYPSVSFN LTEANSNEYR
60 70 80 90 100
HFLQELRGKV ILGSHRAFDL PVLNPESKVS DSDRFVLVRL TNPSRKKVTL
110 120 130 140 150
AIDVVTFYVV AFAQNDRSYF FSGSSEVQRE NLFVDTTQED LNFKGDYTSL
160 170 180 190 200
EHQVGFGRVY IPLGPKSLAQ SISSLSTYKS SAGDNKRLAR SLLVVIQMVS
210 220 230 240 250
EAARFRYIQL RIQASITDAK EFTPDLLMLS MENKWSSMSS EIQQAQPGGA
260 270 280 290 300
FAQVVKLLDQ RNHPIDVTNF RRLFQLTSVA VLLHGCPTVT KMPAYIIKMP
310 320 330 340 350
VFNGGEDEER CSVVEEVTRR IGGRDGFCAE VKNGDEKDGT PVQLSSCGEQ
360 370 380 390 400
SNQQWTFSTD GTIQSLGKCL TTSSSVMIYN CKVVPPESTK WVVSIDGTIT
410 420 430 440 450
NPRSGLVLTA PKAAEGTLVS LEKNVHAARQ GWIVGNVEPL VTFIVGYEQM
460 470 480 490 500
CLETNPGNND VSLGDCSVKS ASKVDQKWAL YGDGTIRVNN DRSLCVTSEG
510 520 530 540 550
KSSNEPIIIL KCLGWANQRW VFNTDGTISN PDSKLVMHVD QNDVPLRKII
560
LSHPSGTSNQ QWIASTHPA
Length:569
Mass (Da):62,598
Last modified:May 1, 1997 - v1
Checksum:i82B9C889A3E1F9AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66191 mRNA Translation: AAC49754.1

Similar proteinsi

Entry informationi

Entry nameiRIP1_SAMNI
AccessioniPrimary (citable) accession number: P93543
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 1, 1997
Last modified: May 23, 2018
This is version 78 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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