DF195_ARATH
ID DF195_ARATH Reviewed; 89 AA.
AC Q42328; O22865; Q6ZZP6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Defensin-like protein 195;
DE AltName: Full=ATTp;
DE AltName: Full=Trypsin inhibitor ATTI-1;
DE AltName: Full=diDi 4T-1;
DE Flags: Precursor;
GN Name=ATTI1; OrderedLocusNames=At2g43510; ORFNames=T01O24.25;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Herve C., Tremousaygue D., Lescure B.;
RT "Nucleotide sequence of an Arabidopsis cDNA encoding a serine proteinase
RT inhibitor ATTI-2.";
RL (er) Plant Gene Register PGR95-011(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11277426; DOI=10.1094/mpmi.2001.14.3.288;
RA Vercauteren I., van der Schueren E., Van Montagu M., Gheysen G.;
RT "Arabidopsis thaliana genes expressed in the early compatible interaction
RT with root-knot nematodes.";
RL Mol. Plant Microbe Interact. 14:288-299(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Col-1, cv. Cvi-1, cv. Di-0, cv. Fe-1a, cv. Goe-0, cv. Ita-0,
RC cv. Kas-1, cv. Landsberg erecta, cv. Le-0, cv. Nd-1, cv. Nok-0, cv. Rsch-0,
RC cv. Sah-0, cv. Ta-0, cv. Wassilewskija, cv. Wei-0, and cv. Wil-2;
RC TISSUE=Leaf;
RX PubMed=15082560; DOI=10.1534/genetics.166.3.1419;
RA Clauss M.J., Mitchell-Olds T.;
RT "Functional divergence in tandemly duplicated Arabidopsis thaliana trypsin
RT inhibitor genes.";
RL Genetics 166:1419-1436(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP GENE FAMILY.
RX PubMed=15955924; DOI=10.1104/pp.105.060079;
RA Silverstein K.A.T., Graham M.A., Paape T.D., VandenBosch K.A.;
RT "Genome organization of more than 300 defensin-like genes in Arabidopsis.";
RL Plant Physiol. 138:600-610(2005).
RN [8]
RP STRUCTURE BY NMR OF 23-89, AND DISULFIDE BONDS.
RX PubMed=12369816; DOI=10.1021/bi025702a;
RA Zhao Q., Chae Y.K., Markley J.L.;
RT "NMR solution structure of ATTp, an Arabidopsis thaliana trypsin
RT inhibitor.";
RL Biochemistry 41:12284-12296(2002).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEFL family. Protease inhibitor I18
CC (RTI/MTI-2) subfamily. {ECO:0000305}.
CC -!- CAUTION: Was (Ref.1, PubMed:15082560 and PubMed:12369816) thought to be
CC a protease inhibitor. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA86849.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z46816; CAA86849.1; ALT_FRAME; mRNA.
DR EMBL; AJ249958; CAB62548.1; -; mRNA.
DR EMBL; AJ632250; CAG15155.1; -; Genomic_DNA.
DR EMBL; AJ632251; CAG15160.1; -; Genomic_DNA.
DR EMBL; AJ632252; CAG15165.1; -; Genomic_DNA.
DR EMBL; AJ632253; CAG15170.1; -; Genomic_DNA.
DR EMBL; AJ632254; CAG15175.1; -; Genomic_DNA.
DR EMBL; AJ632255; CAG15181.1; -; Genomic_DNA.
DR EMBL; AJ632256; CAG15187.1; -; Genomic_DNA.
DR EMBL; AJ632257; CAG15193.1; -; Genomic_DNA.
DR EMBL; AJ632258; CAG15198.1; -; Genomic_DNA.
DR EMBL; AJ632259; CAG15203.1; -; Genomic_DNA.
DR EMBL; AJ632260; CAG15208.1; -; Genomic_DNA.
DR EMBL; AJ632261; CAG15213.1; -; Genomic_DNA.
DR EMBL; AJ632262; CAG15218.1; -; Genomic_DNA.
DR EMBL; AJ632263; CAG15223.1; -; Genomic_DNA.
DR EMBL; AJ632264; CAG15228.1; -; Genomic_DNA.
DR EMBL; AJ632265; CAG15233.1; -; Genomic_DNA.
DR EMBL; AJ632266; CAG15238.1; -; Genomic_DNA.
DR EMBL; AC002335; AAB64325.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10284.1; -; Genomic_DNA.
DR EMBL; AY050789; AAK92724.1; -; mRNA.
DR EMBL; AY096456; AAM20096.1; -; mRNA.
DR PIR; A84867; A84867.
DR RefSeq; NP_181879.1; NM_129912.4.
DR PDB; 1JXC; NMR; -; A=22-89.
DR PDBsum; 1JXC; -.
DR AlphaFoldDB; Q42328; -.
DR SMR; Q42328; -.
DR BioGRID; 4288; 4.
DR IntAct; Q42328; 7.
DR STRING; 3702.AT2G43510.1; -.
DR MEROPS; I18.001; -.
DR TCDB; 1.C.45.4.1; the plant defensin (plant defensin) family.
DR PaxDb; Q42328; -.
DR PRIDE; Q42328; -.
DR ProteomicsDB; 224625; -.
DR EnsemblPlants; AT2G43510.1; AT2G43510.1; AT2G43510.
DR GeneID; 818952; -.
DR Gramene; AT2G43510.1; AT2G43510.1; AT2G43510.
DR KEGG; ath:AT2G43510; -.
DR Araport; AT2G43510; -.
DR TAIR; locus:2058250; AT2G43510.
DR eggNOG; ENOG502R1PW; Eukaryota.
DR HOGENOM; CLU_181760_0_0_1; -.
DR InParanoid; Q42328; -.
DR OMA; FCAPRIL; -.
DR OrthoDB; 1579135at2759; -.
DR PhylomeDB; Q42328; -.
DR EvolutionaryTrace; Q42328; -.
DR PRO; PR:Q42328; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q42328; baseline and differential.
DR Genevisible; Q42328; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISS:TAIR.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Disulfide bond; Fungicide; Plant defense;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..89
FT /note="Defensin-like protein 195"
FT /id="PRO_0000031093"
FT SITE 48..49
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT DISULFID 32..84
FT /evidence="ECO:0000269|PubMed:12369816"
FT DISULFID 45..69
FT /evidence="ECO:0000269|PubMed:12369816"
FT DISULFID 54..79
FT /evidence="ECO:0000269|PubMed:12369816"
FT DISULFID 58..81
FT /evidence="ECO:0000269|PubMed:12369816"
FT VARIANT 6
FT /note="V -> I (in strain: cv. Goe-0)"
FT CONFLICT 85
FT /note="D -> G (in Ref. 1; CAA86849)"
FT /evidence="ECO:0000305"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1JXC"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:1JXC"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1JXC"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1JXC"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1JXC"
SQ SEQUENCE 89 AA; 9885 MW; C4FA5D0B3ABB03D5 CRC64;
MAKAIVSIFV VFFIFFLVIS DVPEIEAQGN ECLKEYGGDV GFGFCAPRIF PTICYTRCRE
NKGAKGGRCR WGQGSNVKCL CDFCDDTPQ
