HIP6_ARATH
ID HIP6_ARATH Reviewed; 392 AA.
AC Q9LZF1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Heavy metal-associated isoprenylated plant protein 6 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP06 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE AltName: Full=Cadmium induced protein CdI19 {ECO:0000303|PubMed:12383082};
DE Flags: Precursor;
GN Name=HIPP06 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN Synonyms=CDI19 {ECO:0000303|PubMed:12383082};
GN OrderedLocusNames=At5g03380 {ECO:0000312|Araport:AT5G03380};
GN ORFNames=F12E4_120 {ECO:0000312|EMBL:CAB83295.1};
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 [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-34; CYS-37; CYS-164; CYS-167
RP AND CYS-389.
RX PubMed=12383082; DOI=10.1046/j.1365-313x.2002.01412.x;
RA Suzuki N., Yamaguchi Y., Koizumi N., Sano H.;
RT "Functional characterization of a heavy metal binding protein CdI19 from
RT Arabidopsis.";
RL Plant J. 32:165-173(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
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 [5]
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 [6]
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. Involved in the maintenance of
CC heavy metal homeostasis and/or in detoxification.
CC {ECO:0000269|PubMed:12383082}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12383082}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9LZF1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in petioles, hypocotyls, peduncles,
CC vascular bundles and root meristems. {ECO:0000269|PubMed:12383082}.
CC -!- INDUCTION: Up-regulated by cadmium, Hg, Fe and Cu, but not by Mn or Co.
CC {ECO:0000269|PubMed:12383082}.
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
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DR EMBL; AF517549; AAM64219.1; -; mRNA.
DR EMBL; AL162751; CAB83295.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90594.1; -; Genomic_DNA.
DR EMBL; AY058875; AAL24262.1; -; mRNA.
DR EMBL; AY103305; AAM65357.1; -; mRNA.
DR PIR; T48360; T48360.
DR RefSeq; NP_195958.1; NM_120417.4. [Q9LZF1-1]
DR AlphaFoldDB; Q9LZF1; -.
DR SMR; Q9LZF1; -.
DR STRING; 3702.AT5G03380.1; -.
DR PaxDb; Q9LZF1; -.
DR PRIDE; Q9LZF1; -.
DR ProteomicsDB; 230243; -. [Q9LZF1-1]
DR EnsemblPlants; AT5G03380.1; AT5G03380.1; AT5G03380. [Q9LZF1-1]
DR GeneID; 831854; -.
DR Gramene; AT5G03380.1; AT5G03380.1; AT5G03380. [Q9LZF1-1]
DR KEGG; ath:AT5G03380; -.
DR Araport; AT5G03380; -.
DR TAIR; locus:2142614; AT5G03380.
DR eggNOG; KOG1603; Eukaryota.
DR InParanoid; Q9LZF1; -.
DR OrthoDB; 1294936at2759; -.
DR PhylomeDB; Q9LZF1; -.
DR PRO; PR:Q9LZF1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZF1; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR CDD; cd00371; HMA; 2.
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 Alternative splicing; Cadmium; Cell membrane; Lipoprotein; Membrane;
KW Metal-binding; Methylation; Prenylation; Reference proteome; Repeat.
FT CHAIN 1..389
FT /note="Heavy metal-associated isoprenylated plant protein
FT 6"
FT /id="PRO_0000437801"
FT PROPEP 390..392
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437802"
FT DOMAIN 23..86
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 153..216
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:12383082"
FT BINDING 37
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:12383082"
FT BINDING 164
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:12383082"
FT BINDING 167
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:12383082"
FT MOD_RES 389
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT LIPID 389
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT MUTAGEN 34
FT /note="C->G: Loss of metal binding; when associated with G-
FT 37; G-164 and G-167."
FT /evidence="ECO:0000269|PubMed:12383082"
FT MUTAGEN 37
FT /note="C->G: Loss of metal binding; when associated with G-
FT 34; G-164 and G-167."
FT /evidence="ECO:0000269|PubMed:12383082"
FT MUTAGEN 164
FT /note="C->G: Loss of metal binding; when associated with G-
FT 34; G-37 and G-167."
FT /evidence="ECO:0000269|PubMed:12383082"
FT MUTAGEN 167
FT /note="C->G: Loss of metal binding; when associated with G-
FT 34; G-37 and G-164."
FT /evidence="ECO:0000269|PubMed:12383082"
FT MUTAGEN 389
FT /note="C->G: Loss of plasma membrane localization."
FT /evidence="ECO:0000269|PubMed:12383082"
SQ SEQUENCE 392 AA; 42263 MW; 712A798F9FDAF7CE CRC64;
MGEKKEETAT KPQGEKKPTD GGITTVVMKL DMHCEGCGKK IKRIFKHFKG VEDVKIDYKS
NKLTVIGNVD PVEVRDKVAD KIKRPVELVS TVAPPKKETP PSSGGAEKKP SPAAEEKPAE
KKPAAVEKPG EKKEEKKKEE GEKKASPPPP PKESTVVLKT KLHCEGCEHK IKRIVNKIKG
VNSVAIDSAK DLVIVKGIID VKQLTPYLNE KLKRTVEVVP AKKDDGAPVA AAAAAPAGGE
KKDKVAGEKK EIKDVGEKKV DGGGEKKKEV AVGGGGGGGG GGGDGGAMDV KKSEYNGYGY
PPQPMYYYPE GQVYGQQHYM MQGQSSQSYV QEPYSNQGYV QESYMNQGYG QGYGQEAPPP
PYMNQQGYAD PYGHMRAPEL FSDENPNGCS VM
