HIP9_ARATH
ID HIP9_ARATH Reviewed; 319 AA.
AC Q9FLU5;
DT 02-NOV-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 9 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP09 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Flags: Precursor;
GN Name=HIPP09 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN OrderedLocusNames=At5g24580 {ECO:0000312|Araport:AT5G24580};
GN ORFNames=K18P6.11 {ECO:0000312|EMBL:BAB11210.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(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 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 [5]
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. {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=Q9FLU5-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
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DR EMBL; AB010068; BAB11210.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93327.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70314.1; -; Genomic_DNA.
DR EMBL; AY072071; AAL59894.1; -; mRNA.
DR EMBL; AY133835; AAM91769.1; -; mRNA.
DR RefSeq; NP_001331936.1; NM_001343881.1. [Q9FLU5-1]
DR RefSeq; NP_568449.1; NM_122366.4. [Q9FLU5-1]
DR AlphaFoldDB; Q9FLU5; -.
DR SMR; Q9FLU5; -.
DR STRING; 3702.AT5G24580.1; -.
DR PaxDb; Q9FLU5; -.
DR PRIDE; Q9FLU5; -.
DR EnsemblPlants; AT5G24580.1; AT5G24580.1; AT5G24580. [Q9FLU5-1]
DR EnsemblPlants; AT5G24580.4; AT5G24580.4; AT5G24580. [Q9FLU5-1]
DR GeneID; 832529; -.
DR Gramene; AT5G24580.1; AT5G24580.1; AT5G24580. [Q9FLU5-1]
DR Gramene; AT5G24580.4; AT5G24580.4; AT5G24580. [Q9FLU5-1]
DR KEGG; ath:AT5G24580; -.
DR Araport; AT5G24580; -.
DR TAIR; locus:2153969; AT5G24580.
DR eggNOG; KOG1603; Eukaryota.
DR InParanoid; Q9FLU5; -.
DR OMA; CTGCARR; -.
DR OrthoDB; 1334286at2759; -.
DR PhylomeDB; Q9FLU5; -.
DR PRO; PR:Q9FLU5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLU5; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 2.
DR InterPro; IPR044258; HIPP09-like.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR PANTHER; PTHR47066; PTHR47066; 1.
DR Pfam; PF00403; HMA; 2.
DR SUPFAM; SSF55008; SSF55008; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Lipoprotein; Metal-binding; Methylation;
KW Prenylation; Reference proteome; Repeat.
FT CHAIN 1..316
FT /note="Heavy metal-associated isoprenylated plant protein
FT 9"
FT /id="PRO_0000437807"
FT PROPEP 317..319
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437808"
FT DOMAIN 55..118
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 144..208
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..48
FT /evidence="ECO:0000255"
FT COMPBIAS 20..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 69
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 155
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 158
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 316
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT LIPID 316
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
SQ SEQUENCE 319 AA; 35350 MW; 5A97CA58833BCDE0 CRC64;
MGEEVKPEAK EAASAPQAVP AEEEEKKKDV AEEKKVAAEE EKPKEEEEPQ PPPPPPPFIL
YVDLHCVGCA KKIERSILKI RGVEEVVMDM NENQVTIKGV LDPQAVCNKI KKKTKRMAKV
LSPLPAAEGE PLPPIITSQV SGGLTTVELS VNMHCQACAD QLKKKILKMR GVQTTVTEHT
TGKVIVTGTM DAEKLVDYVY RRTKKQARIV PQPDPEPEAP AAAQEEKKEE SGEGNEKPPE
TGEEKEEEKK KEGEENGEEG GGEEAAATEE ERRDNEMTAM AQEEGMKRMM YYYQPSYVIE
RIPPPQLFSD ENPNACCIS
