ID HIP33_ARATH Reviewed; 587 AA.
AC F4JZL7; F4JZL8; Q84WQ1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Heavy metal-associated isoprenylated plant protein 33 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP33 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Flags: Precursor;
GN Name=HIPP33 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN OrderedLocusNames=At5g19090 {ECO:0000312|Araport:AT5G19090};
GN ORFNames=T16G12.130 {ECO:0000312|EMBL:AC068809};
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|Proteomes:UP000006548};
RN [1]
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 [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] OF 115-587.
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=2;
CC Name=1;
CC IsoId=F4JZL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JZL7-2; Sequence=VSP_058571;
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
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DR EMBL; AC068809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92650.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92651.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92652.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69822.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69823.1; -; Genomic_DNA.
DR EMBL; BT002910; AAO22726.1; -; mRNA.
DR RefSeq; NP_001154719.1; NM_001161247.1. [F4JZL7-2]
DR RefSeq; NP_001331474.1; NM_001343588.1. [F4JZL7-1]
DR RefSeq; NP_001331475.1; NM_001343587.1. [F4JZL7-1]
DR RefSeq; NP_197410.1; NM_121914.4. [F4JZL7-1]
DR RefSeq; NP_850851.1; NM_180520.2. [F4JZL7-2]
DR AlphaFoldDB; F4JZL7; -.
DR SMR; F4JZL7; -.
DR STRING; 3702.F4JZL7; -.
DR PaxDb; 3702-AT5G19090-1; -.
DR ProteomicsDB; 230193; -. [F4JZL7-1]
DR EnsemblPlants; AT5G19090.1; AT5G19090.1; AT5G19090. [F4JZL7-1]
DR EnsemblPlants; AT5G19090.2; AT5G19090.2; AT5G19090. [F4JZL7-2]
DR EnsemblPlants; AT5G19090.3; AT5G19090.3; AT5G19090. [F4JZL7-2]
DR EnsemblPlants; AT5G19090.4; AT5G19090.4; AT5G19090. [F4JZL7-1]
DR EnsemblPlants; AT5G19090.5; AT5G19090.5; AT5G19090. [F4JZL7-1]
DR GeneID; 832028; -.
DR Gramene; AT5G19090.1; AT5G19090.1; AT5G19090. [F4JZL7-1]
DR Gramene; AT5G19090.2; AT5G19090.2; AT5G19090. [F4JZL7-2]
DR Gramene; AT5G19090.3; AT5G19090.3; AT5G19090. [F4JZL7-2]
DR Gramene; AT5G19090.4; AT5G19090.4; AT5G19090. [F4JZL7-1]
DR Gramene; AT5G19090.5; AT5G19090.5; AT5G19090. [F4JZL7-1]
DR KEGG; ath:AT5G19090; -.
DR Araport; AT5G19090; -.
DR TAIR; AT5G19090; -.
DR eggNOG; KOG1603; Eukaryota.
DR InParanoid; F4JZL7; -.
DR OMA; GPPMKMG; -.
DR OrthoDB; 707220at2759; -.
DR PRO; PR:F4JZL7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JZL7; baseline and differential.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR PANTHER; PTHR45868:SF85; F15K9.8-RELATED; 1.
DR PANTHER; PTHR45868; HEAVY METAL-ASSOCIATED ISOPRENYLATED PLANT PROTEIN 33-RELATED; 1.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
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..584
FT /note="Heavy metal-associated isoprenylated plant protein
FT 33"
FT /id="PRO_0000437843"
FT PROPEP 585..587
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437844"
FT DOMAIN 9..72
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 98..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 23
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MOD_RES 584
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT LIPID 584
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT VAR_SEQ 291..412
FT /note="Missing (in isoform 2)"
FT /id="VSP_058571"
SQ SEQUENCE 587 AA; 59621 MW; 08C058F7B0953C93 CRC64;
MSKEEFMKIQ TCVLKVNIHC DGCKQKVKKI LQKIEGVFTT KIDAELGKVT VSGNVDPSVL
IKKLLKSGKH AEIWGAPKGG SNNNQNQPNL ANQFKAMQID HGGKGGGGGG GGPANNNKGQ
KIGGGGGGGG GGGGGGGGGP PKMVIPQLTP QQMQQLNPQQ LQQLQQLQQM KGFQDLKLPP
QLKGGPGPGP GSVPMNKNPQ MPNNPNQKAV KFNVPDDDDE EDFSDEFDDE FDEDDDEFDD
DLEDDEFDDH PPPPNKMKPM MGGGNMIMPN NMMPNMMMPN AQQMLNAHKN GGGPGPAGGK
IEGKGMPFPV QMGGGGGGPG GKKGGPGGGG GNMGNQNQGG GGKNGGKGGG GHPLDGKMGG
GGGGPNGNKG GGGVQMNGGP NGGKKGGGGG GGGGGGPMSG GLPPGFRPMG GGGGGGGGPQ
SMSMPMGGAM GGPMGSLPQM GGGPGPMSNN MQAVQGLPAM GPGGGGGGGP SAEAPPGYFQ
GQVSGNGGGG QDSMPGNPYL QQQQQQQQQQ YLAAVMNQQR SMGNERFQPM MYARPPPAVN
YMPPQPQPHQ QHPYPYPYPY PPQYPPHNGD QYSDYFNDEN TSSCNIM
//
