PIMP1_CAPAN
ID PIMP1_CAPAN Reviewed; 166 AA.
AC A1XGB4; A1XGB3;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=CASP-like protein PIMP1;
DE AltName: Full=CASP-like protein 4D1;
DE Short=CaCASPL4D1;
DE AltName: Full=Pathogen-induced membrane protein 1;
DE Short=CaPIMP1;
GN Name=PIMP1;
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION BY
RP XANTHOMONAS CAMPESTRIS, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Hanbyul; TISSUE=Leaf;
RX PubMed=18506481; DOI=10.1007/s00425-008-0752-y;
RA Hong J.K., Choi D.S., Kim S.H., Yi S.Y., Kim Y.J., Hwang B.K.;
RT "Distinct roles of the pepper pathogen-induced membrane protein gene
RT CaPIMP1 in bacterial disease resistance and oomycete disease
RT susceptibility.";
RL Planta 228:485-497(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION BY BIOTIC AND
RP ABIOTIC STRESSES.
RC STRAIN=cv. Hanbyul; TISSUE=Leaf;
RX PubMed=18936963; DOI=10.1007/s00425-008-0824-z;
RA Hong J.K., Hwang B.K.;
RT "The promoter of the pepper pathogen-induced membrane protein gene CaPIMP1
RT mediates environmental stress responses in plants.";
RL Planta 229:249-259(2009).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24920445; DOI=10.1104/pp.114.239137;
RA Roppolo D., Boeckmann B., Pfister A., Boutet E., Rubio M.C.,
RA Denervaud-Tendon V., Vermeer J.E., Gheyselinck J., Xenarios I., Geldner N.;
RT "Functional and evolutionary analysis of the CASPARIAN STRIP MEMBRANE
RT DOMAIN PROTEIN family.";
RL Plant Physiol. 165:1709-1722(2014).
CC -!- FUNCTION: Required for defense response to Xanthomonas campestris pv.
CC vesicatoria (Xcv). In heterologous systems, confers resistance to
CC bacterial pathogens such as Pseudomonas syringae pv. tomato but
CC susceptibility to pathogenic oomycetes such as Hylaloperonospora
CC parasitica when expressed in Arabidopsis thaliana. May be involved in
CC the regulation of responses to bitoic and abiotic stresses.
CC {ECO:0000269|PubMed:18506481, ECO:0000269|PubMed:18936963}.
CC -!- SUBUNIT: Homodimer and heterodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18506481};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18506481}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems and flowers.
CC {ECO:0000269|PubMed:18506481}.
CC -!- INDUCTION: In leaves by X.campestris pv. vesicatoria, faster during
CC compatible than incompatible interactions. Induced in leaves by
CC treatments with ethylene, methyl jasmonate (MeJA), abscisic acid (ABA),
CC beta-amino-n-butyric acid (BABA), NaCl, mechanical wounding, and low
CC temperature, but not with salicylic acid (SA).
CC {ECO:0000269|PubMed:18506481, ECO:0000269|PubMed:18936963}.
CC -!- MISCELLANEOUS: Susceptibility to X.campestris pv. vesicatoria is
CC enhanced upon virus induced gene silencing (VIGS).
CC -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ356278; ABC79684.1; -; mRNA.
DR EMBL; DQ356279; ABC86980.1; -; Genomic_DNA.
DR RefSeq; XP_016572144.1; XM_016716658.1.
DR AlphaFoldDB; A1XGB4; -.
DR TCDB; 9.B.56.1.1; the bacterial disease resistance and oomycete disease susceptibility protein, pimp1 (pimp1) family.
DR EnsemblPlants; PHT80901; PHT80901; T459_13916.
DR GeneID; 107870211; -.
DR Gramene; PHT80901; PHT80901; T459_13916.
DR KEGG; cann:107870211; -.
DR OrthoDB; 1520625at2759; -.
DR Proteomes; UP000189700; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR InterPro; IPR006702; CASP_dom.
DR Pfam; PF04535; DUF588; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Plant defense; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..166
FT /note="CASP-like protein PIMP1"
FT /id="PRO_0000391511"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 7
FT /note="S -> T (in Ref. 1; ABC79684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 166 AA; 18155 MW; F0003F11D9913713 CRC64;
MTPPPTSTVP PYVSLIVRIL TLICLLISFI VIATNNQTVS TVAGDVKIKF KDFYAYRYLI
ATVIIGMAYT LLQIAFSISL LTTGNRIGGE GFLLFDFYGD KFISYFLVTG AAASFGMTQD
LKQLEGSDNY SKFLNTSNAA ASLCLIGFFF AVASSIFSSY NLPKRI
