HIP3_ARATH
ID HIP3_ARATH Reviewed; 283 AA.
AC Q9FJH5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Heavy metal-associated isoprenylated plant protein 3 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP03 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIPP3 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Flags: Precursor;
GN Name=HIPP03 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN Synonyms=HIPP3 {ECO:0000303|PubMed:21072340};
GN OrderedLocusNames=At5g60800 {ECO:0000312|Araport:AT5G60800};
GN ORFNames=MAE1.5 {ECO:0000312|EMBL:BAB10101.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NOMENCLATURE, AND GENE FAMILY.
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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF CYS-36;
RP CYS-39; CYS-143 AND CYS-146.
RX PubMed=25913773; DOI=10.1111/nph.13419;
RA Zschiesche W., Barth O., Daniel K., Boehme S., Rausche J., Humbeck K.;
RT "The zinc-binding nuclear protein HIPP3 acts as an upstream regulator of
RT the salicylate-dependent plant immunity pathway and of flowering time in
RT Arabidopsis thaliana.";
RL New Phytol. 207:1084-1096(2015).
CC -!- FUNCTION: Heavy-metal-binding protein. Binds high amounts of zinc. May
CC act as an upstream regulator of the salicylate-dependent pathogen
CC response. Involved in abiotic stress responses, and seed and flower
CC development. {ECO:0000269|PubMed:25913773}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25913773}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:25913773}. Cytoplasm
CC {ECO:0000269|PubMed:25913773}. Note=Weakly expressed in the cytoplasm.
CC {ECO:0000269|PubMed:25913773}.
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=Q9FJH5-1; Sequence=Displayed;
CC -!- INDUCTION: Induced by infection with the bacterial pathogen P. syringae
CC pv. tomato DC3000. Repressed in response to drought and abscisic acid
CC (ABA). {ECO:0000269|PubMed:25913773}.
CC -!- MISCELLANEOUS: Plants over-expressing HIPP3 show delayed growth of
CC inflorescence. {ECO:0000269|PubMed:25913773}.
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
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DR EMBL; AB015472; BAB10101.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97378.1; -; Genomic_DNA.
DR EMBL; BT004613; AAO42859.1; -; mRNA.
DR EMBL; AK227985; BAE99951.1; -; mRNA.
DR RefSeq; NP_200888.2; NM_125473.4. [Q9FJH5-1]
DR AlphaFoldDB; Q9FJH5; -.
DR SMR; Q9FJH5; -.
DR STRING; 3702.AT5G60800.2; -.
DR PaxDb; Q9FJH5; -.
DR PRIDE; Q9FJH5; -.
DR EnsemblPlants; AT5G60800.1; AT5G60800.1; AT5G60800. [Q9FJH5-1]
DR GeneID; 836201; -.
DR Gramene; AT5G60800.1; AT5G60800.1; AT5G60800. [Q9FJH5-1]
DR KEGG; ath:AT5G60800; -.
DR Araport; AT5G60800; -.
DR eggNOG; KOG1603; Eukaryota.
DR HOGENOM; CLU_039886_0_0_1; -.
DR OMA; KTHKNVE; -.
DR PhylomeDB; Q9FJH5; -.
DR PRO; PR:Q9FJH5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJH5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:UniProtKB.
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; Cytoplasm; Lipoprotein; Metal-binding; Methylation;
KW Nucleus; Prenylation; Reference proteome; Repeat; Zinc.
FT CHAIN 1..280
FT /note="Heavy metal-associated isoprenylated plant protein
FT 3"
FT /id="PRO_0000435853"
FT PROPEP 281..283
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435854"
FT DOMAIN 25..88
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 132..195
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:25913773"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:25913773"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:25913773"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000269|PubMed:25913773"
FT MOD_RES 280
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT LIPID 280
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT MUTAGEN 36
FT /note="C->G: Loss of zinc binding; in association with C-
FT 39; C-143 and C-146."
FT /evidence="ECO:0000269|PubMed:25913773"
FT MUTAGEN 39
FT /note="C->G: Loss of zinc binding; in association with C-
FT 36; C-143 and C-146."
FT /evidence="ECO:0000269|PubMed:25913773"
FT MUTAGEN 143
FT /note="C->G: Loss of zinc binding; in association with C-
FT 36; C-39 and C-146."
FT /evidence="ECO:0000269|PubMed:25913773"
FT MUTAGEN 146
FT /note="C->G: Loss of zinc binding; in association with C-
FT 36; C-39 and C-143."
FT /evidence="ECO:0000269|PubMed:25913773"
SQ SEQUENCE 283 AA; 30984 MW; 845E1DBDF5B0107C CRC64;
MGEKKNEGDN KKKGGDNKKK NETPSITVVL KVDMHCEGCA SRIVKCVRSF QGVETVKSES
ATGKLTVTGA LDPVKLREKL EEKTKKKVDL VSPQPKKEKE KENKNKNDED KKKSEEKKKP
DNNDKKPKET PVTTAVLKLN FHCQGCIGKI QKTVTKTKGV NGLTMDKEKN LLTVKGTMDV
KKLVEILSEK LKRAVEIVPP KKEKDKENGN ENGEKKKGGG GDGGGKEKTG NKGGGEGVNM
MEYMAAQPAY GYGYYPGGPY GYPIQAHAPQ IFSDENPNAC VVM
