HIP26_ARATH
ID HIP26_ARATH Reviewed; 153 AA.
AC Q9SZN7; Q8LGG1; Q9ZRE4;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Heavy metal-associated isoprenylated plant protein 26 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP26 {ECO:0000303|PubMed:23368984};
DE Short=AtHIPP26 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE AltName: Full=Farnesylated protein 6 {ECO:0000303|PubMed:8837031};
DE Short=AtFP6 {ECO:0000303|PubMed:8837031};
DE Flags: Precursor;
GN Name=HIPP26 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN Synonyms=FP6 {ECO:0000303|PubMed:8837031};
GN OrderedLocusNames=At4g38580 {ECO:0000312|Araport:AT4G38580};
GN ORFNames=F20M13.140 {ECO:0000312|EMBL:CAB37514.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 [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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-153.
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 [6]
RP GENE FAMILY.
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 [7]
RP FUNCTION, INTERACTION WITH ACBP2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY CADMIUM AND ZINC.
RC STRAIN=cv. Columbia;
RX PubMed=18823312; DOI=10.1111/j.1469-8137.2008.02631.x;
RA Gao W., Xiao S., Li H.Y., Tsao S.W., Chye M.L.;
RT "Arabidopsis thaliana acyl-CoA-binding protein ACBP2 interacts with heavy-
RT metal-binding farnesylated protein AtFP6.";
RL New Phytol. 181:89-102(2009).
RN [8]
RP GENE FAMILY, NOMENCLATURE, INTERACTION WITH ZHD11/HB29, INDUCTION BY COLD;
RP DROUGHT; SALT AND ABSCISIC ACID, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP CYS-36; CYS-39 AND CYS-150, TISSUE SPECIFICITY, ISOPRENYLATION AT CYS-150,
RP METHYLATION AT CYS-150, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18974936; DOI=10.1007/s11103-008-9419-0;
RA Barth O., Vogt S., Uhlemann R., Zschiesche W., Humbeck K.;
RT "Stress induced and nuclear localized HIPP26 from Arabidopsis thaliana
RT interacts via its heavy metal associated domain with the drought stress
RT related zinc finger transcription factor ATHB29.";
RL Plant Mol. Biol. 69:213-226(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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 [10]
RP GENE FAMILY, AND NOMENCLATURE.
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. Binds lead, cadmium and copper.
CC May be involved in heavy-metal transport (PubMed:18823312). May be
CC involved in cadmium transport and play a role in cadmium detoxification
CC (PubMed:21072340). {ECO:0000269|PubMed:18823312,
CC ECO:0000269|PubMed:21072340}.
CC -!- SUBUNIT: Interacts with ZHD11/HB29 and ACBP2 (via ankyrin repeats). May
CC also interact with HB21. {ECO:0000269|PubMed:18823312,
CC ECO:0000269|PubMed:18974936}.
CC -!- INTERACTION:
CC Q9SZN7; Q9STP8: ACBP2; NbExp=5; IntAct=EBI-2008207, EBI-368234;
CC Q9SZN7; Q9SQR3: D14; NbExp=3; IntAct=EBI-2008207, EBI-25530219;
CC Q9SZN7; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-2008207, EBI-25519488;
CC Q9SZN7; Q9SEZ1: ZHD11; NbExp=3; IntAct=EBI-2008207, EBI-1806317;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18974936}.
CC Cell membrane {ECO:0000269|PubMed:18823312}. Note=PubMed:18974936 shows
CC that isopernylation may be important for a speckle-like nuclear
CC localization in a heterologous system, while PubMed:18823312 shows a
CC plasma membrane localization. {ECO:0000269|PubMed:18823312,
CC ECO:0000269|PubMed:18974936}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and flowers. Lower
CC expression in siliques and leaves. Expressed in the vascular tissues.
CC Detected in lateral roots, shoot apical meristem, petals of unopened
CC flowers and weak expression in leaf vasculature.
CC {ECO:0000269|PubMed:18823312, ECO:0000269|PubMed:18974936,
CC ECO:0000269|PubMed:21072340}.
CC -!- INDUCTION: Up-regulated by cadmium and zinc, but not by lead or copper.
CC Up-regulated by cold, drought and salt stress. Not induced by abscisic
CC acid or by leaf senescence. {ECO:0000269|PubMed:18823312,
CC ECO:0000269|PubMed:18974936}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Inhibition of HB29-
CC dependent induction of stress-related target genes.
CC {ECO:0000269|PubMed:18974936, ECO:0000269|PubMed:21072340}.
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
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DR EMBL; AL035540; CAB37514.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80522.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86950.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67729.1; -; Genomic_DNA.
DR EMBL; AF324677; AAG40028.1; -; mRNA.
DR EMBL; AF326881; AAG41463.1; -; mRNA.
DR EMBL; AF339701; AAK00383.1; -; mRNA.
DR EMBL; AF380660; AAK55741.1; -; mRNA.
DR EMBL; AY056095; AAL06983.1; -; mRNA.
DR EMBL; AY084288; AAM60879.1; -; mRNA.
DR EMBL; U64909; AAD09510.1; -; mRNA.
DR PIR; T05686; T05686.
DR RefSeq; NP_001320160.1; NM_001342507.1.
DR RefSeq; NP_195570.1; NM_120019.3.
DR AlphaFoldDB; Q9SZN7; -.
DR SMR; Q9SZN7; -.
DR BioGRID; 15295; 5.
DR IntAct; Q9SZN7; 5.
DR STRING; 3702.AT4G38580.1; -.
DR iPTMnet; Q9SZN7; -.
DR SwissPalm; Q9SZN7; -.
DR PaxDb; Q9SZN7; -.
DR PRIDE; Q9SZN7; -.
DR ProteomicsDB; 230190; -.
DR EnsemblPlants; AT4G38580.1; AT4G38580.1; AT4G38580.
DR EnsemblPlants; AT4G38580.2; AT4G38580.2; AT4G38580.
DR GeneID; 830015; -.
DR Gramene; AT4G38580.1; AT4G38580.1; AT4G38580.
DR Gramene; AT4G38580.2; AT4G38580.2; AT4G38580.
DR KEGG; ath:AT4G38580; -.
DR Araport; AT4G38580; -.
DR TAIR; locus:2121199; AT4G38580.
DR eggNOG; KOG1603; Eukaryota.
DR HOGENOM; CLU_100095_1_0_1; -.
DR InParanoid; Q9SZN7; -.
DR OMA; LDHISDM; -.
DR OrthoDB; 1406686at2759; -.
DR PhylomeDB; Q9SZN7; -.
DR PRO; PR:Q9SZN7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZN7; baseline and differential.
DR Genevisible; Q9SZN7; AT.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0046870; F:cadmium ion binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0032791; F:lead ion binding; IDA:UniProtKB.
DR GO; GO:0010286; P:heat acclimation; IEP:TAIR.
DR CDD; cd00371; HMA; 1.
DR InterPro; IPR045181; HIPP/ATX1-like.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR PANTHER; PTHR22814; PTHR22814; 1.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW Cadmium; Cell membrane; Lipoprotein; Membrane; Metal-binding; Methylation;
KW Nucleus; Prenylation; Reference proteome.
FT CHAIN 1..150
FT /note="Heavy metal-associated isoprenylated plant protein
FT 26"
FT /id="PRO_0000417497"
FT PROPEP 151..153
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000417498"
FT DOMAIN 25..89
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 36
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 39
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MOD_RES 150
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305|PubMed:18974936"
FT LIPID 150
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000305|PubMed:18974936"
FT MUTAGEN 36
FT /note="C->G: In HIPP26-4; loss of interaction with HB29;
FT when associated with G-39."
FT /evidence="ECO:0000269|PubMed:18974936"
FT MUTAGEN 39
FT /note="C->G: In HIPP26-4; loss of interaction with HB29;
FT when associated with G-36."
FT /evidence="ECO:0000269|PubMed:18974936"
FT MUTAGEN 150
FT /note="C->G: Loss of prenylation and localization to
FT membrane."
FT /evidence="ECO:0000269|PubMed:18974936"
FT CONFLICT 104
FT /note="A -> T (in Ref. 4; AAM60879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 17024 MW; 6156E2539E21F2A5 CRC64;
MGVLDHVSEM FDCSHGHKIK KRKQLQTVEI KVKMDCEGCE RKVRRSVEGM KGVSSVTLEP
KAHKVTVVGY VDPNKVVARM SHRTGKKVEL WPYVPYDVVA HPYAAGVYDK KAPSGYVRRV
DDPGVSQLAR ASSTEVRYTT AFSDENPAAC VVM
