HIP22_ARATH
ID HIP22_ARATH Reviewed; 152 AA.
AC Q93VP2; Q9ZRE3;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Heavy metal-associated isoprenylated plant protein 22 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE Short=AtHIP22 {ECO:0000303|PubMed:23368984};
DE Short=AtHIPP22 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE AltName: Full=Farnesylated protein 7 {ECO:0000303|PubMed:8837031};
DE Short=AtFP7 {ECO:0000303|PubMed:8837031};
DE Flags: Precursor;
GN Name=HIPP22 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN Synonyms=FP7 {ECO:0000303|PubMed:8837031};
GN OrderedLocusNames=At1g22990 {ECO:0000312|Araport:AT1G22990};
GN ORFNames=F19G10.25 {ECO:0000312|EMBL:AF000657};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 41-152.
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 INTERACTION WITH ZHD11/HB29.
RC STRAIN=cv. Columbia;
RX PubMed=18974936; DOI=10.1007/s11103-008-9419-0;
RA Barth O., Vogt S., Uhlemann R., Zschiesche W., Humbeck K.;
RT "Stress induced and nuclear localized HIPP26 from Arabidopsis thaliana
RT interacts via its heavy metal associated domain with the drought stress
RT related zinc finger transcription factor ATHB29.";
RL Plant Mol. Biol. 69:213-226(2009).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, NOMENCLATURE, GENE FAMILY, AND DISRUPTION
RP PHENOTYPE.
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 cadmium. May be involved
CC in cadmium transport and play a role in cadmium detoxification.
CC {ECO:0000269|PubMed:21072340}.
CC -!- SUBUNIT: Interacts with ZHD11/HB29. {ECO:0000269|PubMed:18974936}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9SZN7}.
CC -!- TISSUE SPECIFICITY: Expressed in lateral roots and mature anthers.
CC {ECO:0000269|PubMed:21072340}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Hipp20, hipp21 and hipp22
CC triple mutants are cadmium sensitive. {ECO:0000269|PubMed:21072340}.
CC -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
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DR EMBL; AF000657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE30319.1; -; Genomic_DNA.
DR EMBL; AF370526; AAK48953.1; -; mRNA.
DR EMBL; AF446887; AAL38620.1; -; mRNA.
DR EMBL; AY052659; AAK96563.1; -; mRNA.
DR EMBL; AY072474; AAL66889.1; -; mRNA.
DR EMBL; U64910; AAD09511.1; -; mRNA.
DR RefSeq; NP_173712.1; NM_102147.3.
DR AlphaFoldDB; Q93VP2; -.
DR SMR; Q93VP2; -.
DR IntAct; Q93VP2; 1.
DR STRING; 3702.AT1G22990.1; -.
DR PaxDb; Q93VP2; -.
DR PRIDE; Q93VP2; -.
DR ProteomicsDB; 230330; -.
DR EnsemblPlants; AT1G22990.1; AT1G22990.1; AT1G22990.
DR GeneID; 838907; -.
DR Gramene; AT1G22990.1; AT1G22990.1; AT1G22990.
DR KEGG; ath:AT1G22990; -.
DR Araport; AT1G22990; -.
DR TAIR; locus:2017759; AT1G22990.
DR eggNOG; KOG1603; Eukaryota.
DR HOGENOM; CLU_100095_1_0_1; -.
DR InParanoid; Q93VP2; -.
DR OMA; PYAANTY; -.
DR OrthoDB; 1352064at2759; -.
DR PhylomeDB; Q93VP2; -.
DR PRO; PR:Q93VP2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93VP2; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055073; P:cadmium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0071585; P:detoxification of cadmium ion; IMP:UniProtKB.
DR CDD; cd00371; HMA; 1.
DR InterPro; IPR045181; HIPP/ATX1-like.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR PANTHER; PTHR22814; PTHR22814; 1.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW Cadmium; Lipoprotein; Membrane; Metal-binding; Methylation; Prenylation;
KW Reference proteome.
FT CHAIN 1..149
FT /note="Heavy metal-associated isoprenylated plant protein
FT 22"
FT /id="PRO_0000435859"
FT PROPEP 150..152
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435860"
FT DOMAIN 28..91
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 123..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 42
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MOD_RES 149
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT LIPID 149
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT CONFLICT 85
FT /note="S -> N (in Ref. 4; AAD09511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17107 MW; 98015E9EA3AFF0BF CRC64;
MGALNYLSEY FSNHFYVSIR KRKKRKVMQT VNIKVKIDCD GCERKIKNAV SSIKGAKSVE
VNRKMHKVTV SGYVDPKKVL KTVQSTGKKK AELWPYVPYT MVAYPYAAGA YDKRAPPGFV
RKSEQAQAQP GSTDDKLMSL FSDENPNACT VM
