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Protein

Osmotin

Gene

AP24

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Pathogenesis-related protein

Keywords - Biological processi

Plant defense, Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Osmotin
Gene namesi
Name:AP24
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

  • Vacuole

  • Note: Vacuolar inclusion body.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Protein family/group databases

Allergomei9618. Nic t Osmotin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 246225OsmotinPRO_0000034043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 225
Disulfide bondi72 ↔ 82
Disulfide bondi87 ↔ 93
Disulfide bondi141 ↔ 213
Disulfide bondi146 ↔ 196
Disulfide bondi154 ↔ 164
Disulfide bondi168 ↔ 177
Disulfide bondi178 ↔ 183

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Highly expressed in roots and flower buds.1 Publication

Inductioni

By salt stress, abscisic acid (ABA), viral infection and wounding.1 Publication

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 286Combined sources
Beta strandi30 – 323Combined sources
Beta strandi34 – 396Combined sources
Turni40 – 423Combined sources
Beta strandi43 – 475Combined sources
Beta strandi52 – 565Combined sources
Beta strandi63 – 7412Combined sources
Beta strandi78 – 858Combined sources
Beta strandi88 – 925Combined sources
Beta strandi103 – 1086Combined sources
Turni110 – 1123Combined sources
Beta strandi113 – 1208Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi129 – 1357Combined sources
Beta strandi144 – 1463Combined sources
Helixi150 – 1534Combined sources
Turni156 – 1583Combined sources
Helixi167 – 1715Combined sources
Helixi174 – 1774Combined sources
Helixi187 – 1959Combined sources
Helixi206 – 2094Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi220 – 2245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PCVX-ray2.30A/B22-226[»]
ProteinModelPortaliP14170.
SMRiP14170. Positions 22-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14170.

Family & Domainsi

Sequence similaritiesi

Belongs to the thaumatin family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.110.10. 1 hit.
InterProiIPR001938. Thaumatin.
IPR017949. Thaumatin_CS.
[Graphical view]
PANTHERiPTHR31048. PTHR31048. 1 hit.
PfamiPF00314. Thaumatin. 1 hit.
[Graphical view]
PIRSFiPIRSF002703. Thaumatin. 1 hit.
PRINTSiPR00347. THAUMATIN.
SMARTiSM00205. THN. 1 hit.
[Graphical view]
SUPFAMiSSF49870. SSF49870. 1 hit.
PROSITEiPS00316. THAUMATIN_1. 1 hit.
PS51367. THAUMATIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNLRSSFVF FLLALVTYTY AATIEVRNNC PYTVWAASTP IGGGRRLDRG
60 70 80 90 100
QTWVINAPRG TKMARVWGRT NCNFNAAGRG TCQTGDCGGV LQCTGWGKPP
110 120 130 140 150
NTLAEYALDQ FSGLDFWDIS LVDGFNIPMT FAPTNPSGGK CHAIHCTANI
160 170 180 190 200
NGECPRELRV PGGCNNPCTT FGGQQYCCTQ GPCGPTFFSK FFKQRCPDAY
210 220 230 240
SYPQDDPTST FTCPGGSTNY RVIFCPNGQA HPNFPLEMPG SDEVAK
Length:246
Mass (Da):26,681
Last modified:October 1, 1996 - v2
Checksum:i3CDBA991ACA2B0B1
GO

Sequence cautioni

The sequence CAA46623.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32GN → EY in CAA64620 (Ref. 5) Curated
Sequence conflicti15 – 151L → F in CAA64620 (Ref. 5) Curated
Sequence conflicti18 – 181Y → C in CAA64620 (Ref. 5) Curated
Sequence conflicti62 – 621K → N in CAA43854 (PubMed:1536937).Curated
Sequence conflicti66 – 661V → I in CAA64620 (Ref. 5) Curated
Sequence conflicti122 – 1221V → L in AAA34089 (PubMed:16666857).Curated
Sequence conflicti129 – 1291M → I in AAA34089 (PubMed:16666857).Curated
Sequence conflicti132 – 1321Missing in AAA34089 (PubMed:16666857).Curated
Sequence conflicti144 – 1452IH → L in AAA34089 (PubMed:16666857).Curated
Sequence conflicti149 – 1491Missing in AAA34089 (PubMed:16666857).Curated
Sequence conflicti151 – 1555NGECP → RRMS in CAA43854 (PubMed:1536937).Curated
Sequence conflicti156 – 1561R → A in AAA34089 (PubMed:16666857).Curated
Sequence conflicti181 – 1811G → R in AAA34089 (PubMed:16666857).Curated
Sequence conflicti221 – 2211R → K in CAA64620 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65700 mRNA. Translation: CAA46622.1.
X65701 Genomic DNA. Translation: CAA46623.1. Different initiation.
S40046 Genomic DNA. Translation: AAB22459.2.
M29279 mRNA. Translation: AAA34089.1.
X61679 mRNA. Translation: CAA43854.1.
X95308 Genomic DNA. Translation: CAA64620.1.
S44889 mRNA. Translation: AAB23375.1.
PIRiS30157.
S34794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65700 mRNA. Translation: CAA46622.1.
X65701 Genomic DNA. Translation: CAA46623.1. Different initiation.
S40046 Genomic DNA. Translation: AAB22459.2.
M29279 mRNA. Translation: AAA34089.1.
X61679 mRNA. Translation: CAA43854.1.
X95308 Genomic DNA. Translation: CAA64620.1.
S44889 mRNA. Translation: AAB23375.1.
PIRiS30157.
S34794.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PCVX-ray2.30A/B22-226[»]
ProteinModelPortaliP14170.
SMRiP14170. Positions 22-226.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei9618. Nic t Osmotin.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP14170.

Family and domain databases

Gene3Di2.60.110.10. 1 hit.
InterProiIPR001938. Thaumatin.
IPR017949. Thaumatin_CS.
[Graphical view]
PANTHERiPTHR31048. PTHR31048. 1 hit.
PfamiPF00314. Thaumatin. 1 hit.
[Graphical view]
PIRSFiPIRSF002703. Thaumatin. 1 hit.
PRINTSiPR00347. THAUMATIN.
SMARTiSM00205. THN. 1 hit.
[Graphical view]
SUPFAMiSSF49870. SSF49870. 1 hit.
PROSITEiPS00316. THAUMATIN_1. 1 hit.
PS51367. THAUMATIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Extracellular targeting of the vacuolar tobacco proteins AP24, chitinase and beta-1,3-glucanase in transgenic plants."
    Melchers L.S., Sela-Buurlage M.B., Vloemans S.A., Woloshuk C.P., van Roekel J.S.C., Pen J., van den Elzen P.J.M., Cornelissen B.J.C.
    Plant Mol. Biol. 21:583-593(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: cv. Samsun NN.
    Tissue: Leaf.
  2. "Analysis of structure and transcriptional activation of an osmotin gene."
    Nelson D.E., Raghothama K.G., Singh N.K., Hasegawa P.M., Bressan R.A.
    Plant Mol. Biol. 19:577-588(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Molecular cloning of osmotin and regulation of its expression by ABA and adaptation to low water potential."
    Singh N.K., Nelson D.E., Kuhn D., Hasegawa P.M., Bressan R.A.
    Plant Physiol. 90:1096-1101(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: cv. Wisconsin 38.
  4. "Nucleotide sequence of an osmotin cDNA from the Nicotiana tabacum cv. white burley generated by the polymerase chain reaction."
    Kumar V., Spencer M.E.
    Plant Mol. Biol. 18:621-622(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. White Burley.
  5. "Comparison of the 5 regulatory regions of homeologous osmotin genes from Nicotiana tabacum."
    Barnard W.M., Neale A.D.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  6. "Chitinase, beta-1,3-glucanase, osmotin, and extensin are expressed in tobacco explants during flower formation."
    Neale A.D., Wahleithner J.A., Lund M., Bonnett H.T., Kelly A., Meeks-Wagner D.R., Peacock W.J., Dennis E.S.
    Plant Cell 2:673-684(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 3-246, INDUCTION, TISSUE SPECIFICITY.
  7. "Pathogen-induced proteins with inhibitory activity toward Phytophthora infestans."
    Woloshuk C.P., Meulenhoff J.S., Sela-Buurlage M., van den Elzen P.J., Cornelissen B.J.
    Plant Cell 3:619-628(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-61.
    Strain: cv. Samsun NN.
  8. "Crystal structure of osmotin, a plant antifungal protein."
    Min K., Ha S.C., Hasegawa P.M., Bressan R.A., Yun D.J., Kim K.K.
    Proteins 54:170-173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-226.

Entry informationi

Entry nameiOSMO_TOBAC
AccessioniPrimary (citable) accession number: P14170
Secondary accession number(s): Q40529, Q6LDD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1996
Last modified: October 14, 2015
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Inhibits the germination and growth of the fungus Phytophthora infestans.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.