HIP46_ARATH
ID HIP46_ARATH Reviewed; 181 AA.
AC Q5PNZ7; Q84WQ2; Q9LK84; Q9ZRE5;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Heavy metal-associated isoprenylated plant protein 46 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP46 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE AltName: Full=Farnesylated protein 5 {ECO:0000303|PubMed:8837031};
DE Short=AtFP5 {ECO:0000303|PubMed:8837031};
DE Flags: Precursor;
GN Name=HIPP46 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN Synonyms=FP5 {ECO:0000303|PubMed:8837031};
GN OrderedLocusNames=At5g48290 {ECO:0000312|Araport:AT5G48290};
GN ORFNames=K23F3.1 {ECO:0000312|EMBL:BAA98186.1};
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 {ECO:0000312|EMBL:AAV84521.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-181.
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 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 [8]
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: Probable heavy-metal-binding protein.
CC {ECO:0000250|UniProtKB:Q9LZF1}.
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=Q5PNZ7-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
CC -!- CAUTION: Contains an apparent HMA-like domain but lacks the core
CC conserved Cys-X-X-Cys motif. {ECO:0000305|PubMed:21072340}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA98186.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000372; BAA98186.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95646.1; -; Genomic_DNA.
DR EMBL; BT002909; AAO22725.1; -; mRNA.
DR EMBL; BT020300; AAV84521.1; -; mRNA.
DR EMBL; BT020469; AAW38970.1; -; mRNA.
DR EMBL; U64908; AAD09509.1; -; mRNA.
DR RefSeq; NP_568695.1; NM_124204.4. [Q5PNZ7-1]
DR AlphaFoldDB; Q5PNZ7; -.
DR SMR; Q5PNZ7; -.
DR PaxDb; Q5PNZ7; -.
DR EnsemblPlants; AT5G48290.1; AT5G48290.1; AT5G48290. [Q5PNZ7-1]
DR GeneID; 834882; -.
DR Gramene; AT5G48290.1; AT5G48290.1; AT5G48290. [Q5PNZ7-1]
DR KEGG; ath:AT5G48290; -.
DR Araport; AT5G48290; -.
DR TAIR; locus:2156253; AT5G48290.
DR HOGENOM; CLU_1680331_0_0_1; -.
DR InParanoid; Q5PNZ7; -.
DR OMA; TEVDMIG; -.
DR PhylomeDB; Q5PNZ7; -.
DR PRO; PR:Q5PNZ7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5PNZ7; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR044296; HIPP16/46/47.
DR PANTHER; PTHR46371; PTHR46371; 2.
DR PROSITE; PS50846; HMA_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Lipoprotein; Metal-binding; Methylation; Prenylation;
KW Reference proteome.
FT CHAIN 1..178
FT /note="Heavy metal-associated isoprenylated plant protein
FT 46"
FT /id="PRO_0000437864"
FT PROPEP 179..181
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437865"
FT DOMAIN 2..71
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 74..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT LIPID 178
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT CONFLICT 21
FT /note="M -> I (in Ref. 3; AAO22725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 19761 MW; 5BE05A06197EE38B CRC64;
MKQKILIRVT MTDDKTRAKA MTKAVQFKGV SAVEIKGDHR NQIEVTGVEV DMIPLIQILR
KKVAFAELVS VTKVEPPKKE DEKKGGDGKG AEGKGGDQKG GDKKGPDDKE PPEPKPVPCY
PWPLQGYGVP SSFPHQGYGV PSTFPQGDGV PSSFPYPCHP AHPYNDIGEP VYNHEPNCKI
M
