HIP7_ARATH
ID HIP7_ARATH Reviewed; 355 AA.
AC Q9C5D3; Q9FMU9; Q9ZRE7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Heavy metal-associated isoprenylated plant protein 7 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP07 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE AltName: Full=Farnesylated protein 3 {ECO:0000303|PubMed:8837031};
DE Short=AtFP3 {ECO:0000303|PubMed:8837031};
DE Flags: Precursor;
GN Name=HIPP07 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN Synonyms=FP3 {ECO:0000303|PubMed:8837031};
GN OrderedLocusNames=At5g63530 {ECO:0000312|Araport:AT5G63530};
GN ORFNames=MLE2.16 {ECO:0000312|EMBL:BAB08818.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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] (ISOFORM 1).
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 [MRNA] OF 60-355.
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 [5]
RP FUNCTION, GENE FAMILY, ALTERNATIVE PRODUCT, ISOPRENYLATION, AND METAL
RP BINDING.
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 [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, 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 zinc, copper and nickel in
CC a reversible manner. {ECO:0000269|PubMed:10561075}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A shorter isoform might be produced by an alternative
CC polyadenylation site usage. {ECO:0000269|PubMed:10561075};
CC Name=1;
CC IsoId=Q9C5D3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5D3-2; Sequence=VSP_058570;
CC -!- PTM: Efficiently farnesylated in vitro. {ECO:0000269|PubMed:10561075}.
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09507.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AB007649; BAB08818.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97763.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97764.1; -; Genomic_DNA.
DR EMBL; AF360327; AAK26037.1; -; mRNA.
DR EMBL; AY056337; AAL07186.1; -; mRNA.
DR EMBL; U64906; AAD09507.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001078790.1; NM_001085321.2. [Q9C5D3-2]
DR RefSeq; NP_568974.1; NM_125748.3. [Q9C5D3-1]
DR AlphaFoldDB; Q9C5D3; -.
DR SMR; Q9C5D3; -.
DR STRING; 3702.AT5G63530.1; -.
DR PaxDb; Q9C5D3; -.
DR PRIDE; Q9C5D3; -.
DR ProteomicsDB; 230366; -. [Q9C5D3-1]
DR EnsemblPlants; AT5G63530.1; AT5G63530.1; AT5G63530. [Q9C5D3-1]
DR EnsemblPlants; AT5G63530.2; AT5G63530.2; AT5G63530. [Q9C5D3-2]
DR GeneID; 836472; -.
DR Gramene; AT5G63530.1; AT5G63530.1; AT5G63530. [Q9C5D3-1]
DR Gramene; AT5G63530.2; AT5G63530.2; AT5G63530. [Q9C5D3-2]
DR KEGG; ath:AT5G63530; -.
DR Araport; AT5G63530; -.
DR TAIR; locus:2167366; AT5G63530.
DR eggNOG; KOG1603; Eukaryota.
DR HOGENOM; CLU_039886_3_0_1; -.
DR InParanoid; Q9C5D3; -.
DR OrthoDB; 1355998at2759; -.
DR PhylomeDB; Q9C5D3; -.
DR PRO; PR:Q9C5D3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5D3; baseline and differential.
DR GO; GO:0046914; F:transition metal ion binding; IDA:TAIR.
DR GO; GO:0046916; P:cellular transition metal ion homeostasis; TAS:TAIR.
DR CDD; cd00371; HMA; 2.
DR InterPro; IPR044577; HIPP4/7/8/17/18/19.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR PANTHER; PTHR46195; PTHR46195; 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; Lipoprotein; Metal-binding; Methylation; Prenylation;
KW Reference proteome; Repeat.
FT CHAIN 1..352
FT /note="Heavy metal-associated isoprenylated plant protein
FT 7"
FT /id="PRO_0000437803"
FT PROPEP 353..355
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437804"
FT DOMAIN 72..136
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 170..234
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 86
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 181
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 184
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 352
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT LIPID 352
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 2)"
FT /id="VSP_058570"
FT CONFLICT 150..152
FT /note="EKK -> GKE (in Ref. 4; AAD09507)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="E -> Q (in Ref. 4; AAD09507)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="S -> F (in Ref. 4; AAD09507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 39279 MW; 26379DE6F1DBFA6D CRC64;
MGEEEKKPEA AEEKKMEEKK PEEKKEGEDK KVDAEKKGED SDKKPQEGES NKDSKEDSAP
AAPEAPAPPP PPQEVVLKVY MHCEGCARKV RRCLKGFEGV EDVMTDCKTG KVVVKGEKAD
PLKVLARVQR KTHRQVQLLS PIPPPPPPPE KKAEEDKPIV EEKKVEPPVV VTVVLKVHMH
CEACATEIKK RIMRMKGVES AESDLKSSQV TVKGVFEPQK LVEYVYKRTG KHAAIMKIDP
PPPPPPEEAA AAAEGEKKEE EKGEGESKGE EGKDDKAKTD EEKKEGDGGK GEGEAADNGG
GEEEGKVVEV RKIENPYYYY YYQPPRVAIP PMEMPPHAYP PQLFSDENPN ACTVM
