HIP5_ARATH
ID HIP5_ARATH Reviewed; 386 AA.
AC Q9SJL2; Q9ZRE8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Heavy metal-associated isoprenylated plant protein 5 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP05 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE AltName: Full=Farnesylated protein 2 {ECO:0000303|PubMed:8837031};
DE Short=AtFP2 {ECO:0000303|PubMed:8837031};
DE Flags: Precursor;
GN Name=HIPP05 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN Synonyms=FP2 {ECO:0000303|PubMed:8837031};
GN OrderedLocusNames=At2g36950 {ECO:0000312|Araport:AT2G36950};
GN ORFNames=T1J8.13 {ECO:0000312|EMBL:AAD31580.2};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 142-386.
RX PubMed=8837031; DOI=10.1007/bf02900363;
RA Crowell D.N., Biermann B.J., Randall S.K.;
RT "Identification of cDNAs encoding isoprenylated proteins.";
RL Mol. Biotechnol. 5:253-258(1996).
RN [4]
RP GENE FAMILY, AND ISOPRENYLATION.
RX PubMed=10561075; DOI=10.1023/a:1006367609556;
RA Dykema P.E., Sipes P.R., Marie A., Biermann B.J., Crowell D.N.,
RA Randall S.K.;
RT "A new class of proteins capable of binding transition metals.";
RL Plant Mol. Biol. 41:139-150(1999).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12684538; DOI=10.1073/pnas.0737574100;
RA Cooper B., Clarke J.D., Budworth P., Kreps J., Hutchison D., Park S.,
RA Guimil S., Dunn M., Luginbuehl P., Ellero C., Goff S.A., Glazebrook J.;
RT "A network of rice genes associated with stress response and seed
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4945-4950(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21072340; DOI=10.1039/c003484c;
RA Tehseen M., Cairns N., Sherson S., Cobbett C.S.;
RT "Metallochaperone-like genes in Arabidopsis thaliana.";
RL Metallomics 2:556-564(2010).
RN [7]
RP GENE FAMILY, NOMENCLATURE, AND INDUCTION BY CADMIUM.
RX PubMed=23368984; DOI=10.1111/febs.12159;
RA de Abreu-Neto J.B., Turchetto-Zolet A.C., de Oliveira L.F., Zanettini M.H.,
RA Margis-Pinheiro M.;
RT "Heavy metal-associated isoprenylated plant protein (HIPP):
RT characterization of a family of proteins exclusive to plants.";
RL FEBS J. 280:1604-1616(2013).
CC -!- FUNCTION: Heavy-metal-binding protein (By similarity). Involved in
CC disease resistance (PubMed:12684538). {ECO:0000250|UniProtKB:Q9LZF1,
CC ECO:0000269|PubMed:12684538}.
CC -!- INDUCTION: Up-regulated by cadmium. {ECO:0000303|PubMed:23368984}.
CC -!- PTM: Efficiently farnesylated in vitro. {ECO:0000269|PubMed:10561075}.
CC -!- DISRUPTION PHENOTYPE: Strongly increased bacterial disease
CC susceptibility. {ECO:0000269|PubMed:12684538}.
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09506.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AC006922; AAD31580.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09325.1; -; Genomic_DNA.
DR EMBL; U64905; AAD09506.1; ALT_SEQ; mRNA.
DR PIR; F84786; F84786.
DR RefSeq; NP_565855.1; NM_129251.3.
DR AlphaFoldDB; Q9SJL2; -.
DR SMR; Q9SJL2; -.
DR IntAct; Q9SJL2; 1.
DR STRING; 3702.AT2G36950.1; -.
DR PaxDb; Q9SJL2; -.
DR PRIDE; Q9SJL2; -.
DR ProteomicsDB; 230195; -.
DR EnsemblPlants; AT2G36950.1; AT2G36950.1; AT2G36950.
DR GeneID; 818269; -.
DR Gramene; AT2G36950.1; AT2G36950.1; AT2G36950.
DR KEGG; ath:AT2G36950; -.
DR Araport; AT2G36950; -.
DR TAIR; locus:2057951; AT2G36950.
DR eggNOG; KOG1603; Eukaryota.
DR HOGENOM; CLU_039886_0_0_1; -.
DR InParanoid; Q9SJL2; -.
DR OMA; NAPGMFS; -.
DR OrthoDB; 1294936at2759; -.
DR PhylomeDB; Q9SJL2; -.
DR PRO; PR:Q9SJL2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJL2; baseline and differential.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR CDD; cd00371; HMA; 1.
DR InterPro; IPR044594; HIP01/3/5/6.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR PANTHER; PTHR46413; PTHR46413; 1.
DR Pfam; PF00403; HMA; 2.
DR SUPFAM; SSF55008; SSF55008; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 1: Evidence at protein level;
KW Lipoprotein; Metal-binding; Methylation; Prenylation; Reference proteome;
KW Repeat.
FT CHAIN 1..383
FT /note="Heavy metal-associated isoprenylated plant protein
FT 5"
FT /id="PRO_0000437799"
FT PROPEP 384..386
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437800"
FT DOMAIN 49..112
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 153..220
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 63
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 164
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 167
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MOD_RES 383
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT LIPID 383
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT CONFLICT 150
FT /note="A -> T (in Ref. 3; AAD09506)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..236
FT /note="NKKTEA -> IRRTER (in Ref. 3; AAD09506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 40357 MW; 1BC6BAFEC7C1414E CRC64;
MGEVQEGPKV EQEKKPAATV VPVETTDGKP KSGGGDSAAA AAPPVAAVVS AFVYKVDMHC
EGCAKKIKRM VKHFDGVKDV TADTGGNKLL VVGKIDPVKL QEKLEEKTKR KVVLANPPPK
VEGPVAAAVG EKKADGGDKE AAPPAPAPAA PKESVVPLKI RLHCEGCIQK IKKIILKIKG
VETVAIDGAK DVVTVKGTID VKELVPLLTK KLKRTVEPLV PAKKDDGAAE NKKTEAAAPD
AKKEAPSAGV NEAKKEGSDG GEKKKEVGDG GEKKKEGGDG GEKKKEAGDG GEKKKDGGGV
PAPVAMVNKM DYYGYSAYPT APMHWQEGHV YGQSYSMTGQ NYPVGGQSYP GSGYNYASES
YVPYAQPNVN APGMFSDENP NGCSVM
