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OSMO_TOBAC
ID   OSMO_TOBAC              Reviewed;         246 AA.
AC   P14170; Q40529; Q6LDD7;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Osmotin;
DE   Flags: Precursor;
GN   Name=AP24;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Samsun NN; TISSUE=Leaf;
RX   PubMed=8448358; DOI=10.1007/bf00014542;
RA   Melchers L.S., Sela-Buurlage M.B., Vloemans S.A., Woloshuk C.P.,
RA   van Roekel J.S.C., Pen J., van den Elzen P.J.M., Cornelissen B.J.C.;
RT   "Extracellular targeting of the vacuolar tobacco proteins AP24, chitinase
RT   and beta-1,3-glucanase in transgenic plants.";
RL   Plant Mol. Biol. 21:583-593(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1385735; DOI=10.1007/bf00026784;
RA   Nelson D.E., Raghothama K.G., Singh N.K., Hasegawa P.M., Bressan R.A.;
RT   "Analysis of structure and transcriptional activation of an osmotin gene.";
RL   Plant Mol. Biol. 19:577-588(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Wisconsin 38;
RX   PubMed=16666857; DOI=10.1104/pp.90.3.1096;
RA   Singh N.K., Nelson D.E., Kuhn D., Hasegawa P.M., Bressan R.A.;
RT   "Molecular cloning of osmotin and regulation of its expression by ABA and
RT   adaptation to low water potential.";
RL   Plant Physiol. 90:1096-1101(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. White Burley;
RX   PubMed=1536937; DOI=10.1007/bf00040683;
RA   Kumar V., Spencer M.E.;
RT   "Nucleotide sequence of an osmotin cDNA from the Nicotiana tabacum cv.
RT   white burley generated by the polymerase chain reaction.";
RL   Plant Mol. Biol. 18:621-622(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Barnard W.M., Neale A.D.;
RT   "Comparison of the 5 regulatory regions of homeologous osmotin genes from
RT   Nicotiana tabacum.";
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE OF 3-246, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=2152343; DOI=10.2307/3869130;
RA   Neale A.D., Wahleithner J.A., Lund M., Bonnett H.T., Kelly A.,
RA   Meeks-Wagner D.R., Peacock W.J., Dennis E.S.;
RT   "Chitinase, beta-1,3-glucanase, osmotin, and extensin are expressed in
RT   tobacco explants during flower formation.";
RL   Plant Cell 2:673-684(1990).
RN   [7]
RP   PROTEIN SEQUENCE OF 22-61.
RC   STRAIN=cv. Samsun NN;
RX   PubMed=1841721; DOI=10.2307/3869190;
RA   Woloshuk C.P., Meulenhoff J.S., Sela-Buurlage M., van den Elzen P.J.,
RA   Cornelissen B.J.;
RT   "Pathogen-induced proteins with inhibitory activity toward Phytophthora
RT   infestans.";
RL   Plant Cell 3:619-628(1991).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-226.
RX   PubMed=14705035; DOI=10.1002/prot.10571;
RA   Min K., Ha S.C., Hasegawa P.M., Bressan R.A., Yun D.J., Kim K.K.;
RT   "Crystal structure of osmotin, a plant antifungal protein.";
RL   Proteins 54:170-173(2004).
CC   -!- SUBCELLULAR LOCATION: Vacuole. Note=Vacuolar inclusion body.
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots and flower buds.
CC       {ECO:0000269|PubMed:2152343}.
CC   -!- INDUCTION: By salt stress, abscisic acid (ABA), viral infection and
CC       wounding. {ECO:0000269|PubMed:2152343}.
CC   -!- MISCELLANEOUS: Inhibits the germination and growth of the fungus
CC       Phytophthora infestans.
CC   -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00699}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA46623.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X65700; CAA46622.1; -; mRNA.
DR   EMBL; X65701; CAA46623.1; ALT_INIT; Genomic_DNA.
DR   EMBL; S40046; AAB22459.2; -; Genomic_DNA.
DR   EMBL; M29279; AAA34089.1; -; mRNA.
DR   EMBL; X61679; CAA43854.1; -; mRNA.
DR   EMBL; X95308; CAA64620.1; -; Genomic_DNA.
DR   EMBL; S44889; AAB23375.1; -; mRNA.
DR   PIR; S30157; S30157.
DR   PIR; S34794; S34794.
DR   RefSeq; NP_001312374.1; NM_001325445.1.
DR   RefSeq; XP_016464912.1; XM_016609426.1.
DR   PDB; 1PCV; X-ray; 2.30 A; A/B=22-226.
DR   PDBsum; 1PCV; -.
DR   AlphaFoldDB; P14170; -.
DR   SMR; P14170; -.
DR   Allergome; 9618; Nic t Osmotin.
DR   GeneID; 107787819; -.
DR   KEGG; nta:107787819; -.
DR   OrthoDB; 1135904at2759; -.
DR   EvolutionaryTrace; P14170; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.110.10; -; 1.
DR   InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR   InterPro; IPR001938; Thaumatin.
DR   InterPro; IPR017949; Thaumatin_CS.
DR   PANTHER; PTHR31048; PTHR31048; 1.
DR   Pfam; PF00314; Thaumatin; 1.
DR   PIRSF; PIRSF002703; Thaumatin; 1.
DR   PRINTS; PR00347; THAUMATIN.
DR   SMART; SM00205; THN; 1.
DR   SUPFAM; SSF49870; SSF49870; 1.
DR   PROSITE; PS00316; THAUMATIN_1; 1.
DR   PROSITE; PS51367; THAUMATIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Pathogenesis-related protein; Plant defense; Reference proteome; Signal;
KW   Stress response; Vacuole.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:1841721"
FT   CHAIN           22..246
FT                   /note="Osmotin"
FT                   /id="PRO_0000034043"
FT   DISULFID        30..225
FT   DISULFID        72..82
FT   DISULFID        87..93
FT   DISULFID        141..213
FT   DISULFID        146..196
FT   DISULFID        154..164
FT   DISULFID        168..177
FT   DISULFID        178..183
FT   CONFLICT        2..3
FT                   /note="GN -> EY (in Ref. 5; CAA64620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="L -> F (in Ref. 5; CAA64620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="Y -> C (in Ref. 5; CAA64620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="K -> N (in Ref. 4; CAA43854)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="V -> I (in Ref. 5; CAA64620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="V -> L (in Ref. 3; AAA34089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="M -> I (in Ref. 3; AAA34089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="Missing (in Ref. 3; AAA34089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144..145
FT                   /note="IH -> L (in Ref. 3; AAA34089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="Missing (in Ref. 3; AAA34089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151..155
FT                   /note="NGECP -> RRMS (in Ref. 4; CAA43854)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="R -> A (in Ref. 3; AAA34089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="G -> R (in Ref. 3; AAA34089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="R -> K (in Ref. 5; CAA64620)"
FT                   /evidence="ECO:0000305"
FT   STRAND          23..28
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          34..39
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          52..56
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          63..74
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          78..85
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          88..92
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          113..120
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   HELIX           167..171
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   HELIX           174..177
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   HELIX           187..195
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   HELIX           206..209
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          211..214
FT                   /evidence="ECO:0007829|PDB:1PCV"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:1PCV"
SQ   SEQUENCE   246 AA;  26681 MW;  3CDBA991ACA2B0B1 CRC64;
     MGNLRSSFVF FLLALVTYTY AATIEVRNNC PYTVWAASTP IGGGRRLDRG QTWVINAPRG
     TKMARVWGRT NCNFNAAGRG TCQTGDCGGV LQCTGWGKPP NTLAEYALDQ FSGLDFWDIS
     LVDGFNIPMT FAPTNPSGGK CHAIHCTANI NGECPRELRV PGGCNNPCTT FGGQQYCCTQ
     GPCGPTFFSK FFKQRCPDAY SYPQDDPTST FTCPGGSTNY RVIFCPNGQA HPNFPLEMPG
     SDEVAK
 
 
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