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Heavy metal-associated isoprenylated plant protein 26 (AtHIP26) (AtHIPP26) (Farnesylated protein 6) (AtFP6)

 HIP26_ARATH             Reviewed;         153 AA.
Q9SZN7; Q8LGG1; Q9ZRE4;
16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
27-SEP-2017, entry version 112.
RecName: Full=Heavy metal-associated isoprenylated plant protein 26 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
Short=AtHIP26 {ECO:0000303|PubMed:23368984};
Short=AtHIPP26 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
AltName: Full=Farnesylated protein 6 {ECO:0000303|PubMed:8837031};
Short=AtFP6 {ECO:0000303|PubMed:8837031};
Flags: Precursor;
Name=HIPP26 {ECO:0000303|PubMed:21072340,
ECO:0000303|PubMed:23368984};
Synonyms=FP6 {ECO:0000303|PubMed:8837031};
OrderedLocusNames=At4g38580 {ECO:0000312|Araport:AT4G38580};
ORFNames=F20M13.140 {ECO:0000312|EMBL:CAB37514.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 38-153.
PubMed=8837031; DOI=10.1007/BF02900363;
Crowell D.N., Biermann B.J., Randall S.K.;
"Identification of cDNAs encoding isoprenylated proteins.";
Mol. Biotechnol. 5:253-258(1996).
[6]
GENE FAMILY.
PubMed=10561075; DOI=10.1023/A:1006367609556;
Dykema P.E., Sipes P.R., Marie A., Biermann B.J., Crowell D.N.,
Randall S.K.;
"A new class of proteins capable of binding transition metals.";
Plant Mol. Biol. 41:139-150(1999).
[7]
FUNCTION, INTERACTION WITH ACBP2, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION BY CADMIUM AND ZINC.
STRAIN=cv. Columbia;
PubMed=18823312; DOI=10.1111/j.1469-8137.2008.02631.x;
Gao W., Xiao S., Li H.Y., Tsao S.W., Chye M.L.;
"Arabidopsis thaliana acyl-CoA-binding protein ACBP2 interacts with
heavy-metal-binding farnesylated protein AtFP6.";
New Phytol. 181:89-102(2009).
[8]
GENE FAMILY, NOMENCLATURE, INTERACTION WITH ZHD11/HB29, INDUCTION BY
COLD; DROUGHT; SALT AND ABSCISIC ACID, SUBCELLULAR LOCATION,
MUTAGENESIS OF CYS-36; CYS-39 AND CYS-150, TISSUE SPECIFICITY,
ISOPRENYLATION AT CYS-150, METHYLATION AT CYS-150, AND DISRUPTION
PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=18974936; DOI=10.1007/s11103-008-9419-0;
Barth O., Vogt S., Uhlemann R., Zschiesche W., Humbeck K.;
"Stress induced and nuclear localized HIPP26 from Arabidopsis thaliana
interacts via its heavy metal associated domain with the drought
stress related zinc finger transcription factor ATHB29.";
Plant Mol. Biol. 69:213-226(2009).
[9]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, GENE FAMILY, AND
NOMENCLATURE.
PubMed=21072340; DOI=10.1039/c003484c;
Tehseen M., Cairns N., Sherson S., Cobbett C.S.;
"Metallochaperone-like genes in Arabidopsis thaliana.";
Metallomics 2:556-564(2010).
[10]
GENE FAMILY, AND NOMENCLATURE.
PubMed=23368984; DOI=10.1111/febs.12159;
de Abreu-Neto J.B., Turchetto-Zolet A.C., de Oliveira L.F.,
Zanettini M.H., Margis-Pinheiro M.;
"Heavy metal-associated isoprenylated plant protein (HIPP):
characterization of a family of proteins exclusive to plants.";
FEBS J. 280:1604-1616(2013).
-!- FUNCTION: Heavy-metal-binding protein. Binds lead, cadmium and
copper. May be involved in heavy-metal transport
(PubMed:18823312). May be involved in cadmium transport and play a
role in cadmium detoxification (PubMed:21072340).
{ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:21072340}.
-!- SUBUNIT: Interacts with ZHD11/HB29 and ACBP2 (via ankyrin
repeats). May also interact with HB21.
{ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:18974936}.
-!- INTERACTION:
Q9STP8:ACBP2; NbExp=5; IntAct=EBI-2008207, EBI-368234;
Q9SEZ1:ZHD11; NbExp=3; IntAct=EBI-2008207, EBI-1806317;
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000269|PubMed:18974936}. Cell membrane
{ECO:0000269|PubMed:18823312}. Note=PubMed:18974936 shows that
isopernylation may be important for a speckle-like nuclear
localization in a heterologous system, while PubMed:18823312 shows
a plasma membrane localization. {ECO:0000269|PubMed:18823312,
ECO:0000269|PubMed:18974936}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems and flowers. Lower
expression in siliques and leaves. Expressed in the vascular
tissues. Detected in lateral roots, shoot apical meristem, petals
of unopened flowers and weak expression in leaf vasculature.
{ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:18974936,
ECO:0000269|PubMed:21072340}.
-!- INDUCTION: Up-regulated by cadmium and zinc, but not by lead or
copper. Up-regulated by cold, drought and salt stress. Not induced
by abscisic acid or by leaf senescence.
{ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:18974936}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Inhibition of HB29-
dependent induction of stress-related target genes.
{ECO:0000269|PubMed:18974936, ECO:0000269|PubMed:21072340}.
-!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL035540; CAB37514.1; -; Genomic_DNA.
EMBL; AL161593; CAB80522.1; -; Genomic_DNA.
EMBL; CP002687; AEE86950.1; -; Genomic_DNA.
EMBL; CP002687; ANM67729.1; -; Genomic_DNA.
EMBL; AF324677; AAG40028.1; -; mRNA.
EMBL; AF326881; AAG41463.1; -; mRNA.
EMBL; AF339701; AAK00383.1; -; mRNA.
EMBL; AF380660; AAK55741.1; -; mRNA.
EMBL; AY056095; AAL06983.1; -; mRNA.
EMBL; AY084288; AAM60879.1; -; mRNA.
EMBL; U64909; AAD09510.1; -; mRNA.
PIR; T05686; T05686.
RefSeq; NP_001320160.1; NM_001342507.1.
RefSeq; NP_195570.1; NM_120019.3.
UniGene; At.21139; -.
UniGene; At.69396; -.
ProteinModelPortal; Q9SZN7; -.
SMR; Q9SZN7; -.
BioGrid; 15295; 3.
IntAct; Q9SZN7; 3.
STRING; 3702.AT4G38580.1; -.
iPTMnet; Q9SZN7; -.
SwissPalm; Q9SZN7; -.
PaxDb; Q9SZN7; -.
PRIDE; Q9SZN7; -.
EnsemblPlants; AT4G38580.1; AT4G38580.1; AT4G38580.
EnsemblPlants; AT4G38580.2; AT4G38580.2; AT4G38580.
GeneID; 830015; -.
Gramene; AT4G38580.1; AT4G38580.1; AT4G38580.
Gramene; AT4G38580.2; AT4G38580.2; AT4G38580.
KEGG; ath:AT4G38580; -.
Araport; AT4G38580; -.
TAIR; locus:2121199; AT4G38580.
eggNOG; KOG1603; Eukaryota.
eggNOG; COG2608; LUCA.
HOGENOM; HOG000234967; -.
InParanoid; Q9SZN7; -.
OMA; ENPAACA; -.
OrthoDB; EOG09360PJ0; -.
PhylomeDB; Q9SZN7; -.
PRO; PR:Q9SZN7; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9SZN7; baseline and differential.
Genevisible; Q9SZN7; AT.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0046870; F:cadmium ion binding; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0032791; F:lead ion binding; IDA:UniProtKB.
GO; GO:0046916; P:cellular transition metal ion homeostasis; IBA:GO_Central.
GO; GO:0010286; P:heat acclimation; IEP:TAIR.
GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
CDD; cd00371; HMA; 1.
InterPro; IPR006121; HMA_dom.
Pfam; PF00403; HMA; 1.
SUPFAM; SSF55008; SSF55008; 1.
1: Evidence at protein level;
Cadmium; Cell membrane; Complete proteome; Lipoprotein; Membrane;
Metal-binding; Methylation; Nucleus; Prenylation; Reference proteome.
CHAIN 1 150 Heavy metal-associated isoprenylated
plant protein 26.
/FTId=PRO_0000417497.
PROPEP 151 153 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000417498.
DOMAIN 26 92 HMA. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 36 36 {ECO:0000255|PROSITE-ProRule:PRU00280}.
METAL 39 39 {ECO:0000255|PROSITE-ProRule:PRU00280}.
MOD_RES 150 150 Cysteine methyl ester.
{ECO:0000305|PubMed:18974936}.
LIPID 150 150 S-farnesyl cysteine.
{ECO:0000305|PubMed:18974936}.
MUTAGEN 36 36 C->G: In HIPP26-4; loss of interaction
with HB29; when associated with G-39.
{ECO:0000269|PubMed:18974936}.
MUTAGEN 39 39 C->G: In HIPP26-4; loss of interaction
with HB29; when associated with G-36.
{ECO:0000269|PubMed:18974936}.
MUTAGEN 150 150 C->G: Loss of prenylation and
localization to membrane.
{ECO:0000269|PubMed:18974936}.
CONFLICT 104 104 A -> T (in Ref. 4; AAM60879).
{ECO:0000305}.
SEQUENCE 153 AA; 17024 MW; 6156E2539E21F2A5 CRC64;
MGVLDHVSEM FDCSHGHKIK KRKQLQTVEI KVKMDCEGCE RKVRRSVEGM KGVSSVTLEP
KAHKVTVVGY VDPNKVVARM SHRTGKKVEL WPYVPYDVVA HPYAAGVYDK KAPSGYVRRV
DDPGVSQLAR ASSTEVRYTT AFSDENPAAC VVM


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