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HIP23_ARATH
ID   HIP23_ARATH             Reviewed;         158 AA.
AC   O65657;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Heavy metal-associated isoprenylated plant protein 23 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE            Short=AtHIP23 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE   Flags: Precursor;
GN   Name=HIPP23 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN   OrderedLocusNames=At4g39700 {ECO:0000312|Araport:AT4G39700};
GN   ORFNames=T19P19.90 {ECO:0000312|EMBL:CAA18756.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   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   [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   -!- SUBUNIT: Interacts with ZHD11/HB29. {ECO:0000269|PubMed:18974936}.
CC   -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
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DR   EMBL; AL022605; CAA18756.1; -; Genomic_DNA.
DR   EMBL; AL161595; CAB80633.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE87106.1; -; Genomic_DNA.
DR   PIR; T05007; T05007.
DR   RefSeq; NP_195680.1; NM_120131.2.
DR   AlphaFoldDB; O65657; -.
DR   SMR; O65657; -.
DR   IntAct; O65657; 1.
DR   STRING; 3702.AT4G39700.1; -.
DR   PaxDb; O65657; -.
DR   PRIDE; O65657; -.
DR   EnsemblPlants; AT4G39700.1; AT4G39700.1; AT4G39700.
DR   GeneID; 830125; -.
DR   Gramene; AT4G39700.1; AT4G39700.1; AT4G39700.
DR   KEGG; ath:AT4G39700; -.
DR   Araport; AT4G39700; -.
DR   TAIR; locus:2135277; AT4G39700.
DR   eggNOG; KOG1603; Eukaryota.
DR   HOGENOM; CLU_100095_1_0_1; -.
DR   InParanoid; O65657; -.
DR   OMA; KRVRQTG; -.
DR   OrthoDB; 1388007at2759; -.
DR   PhylomeDB; O65657; -.
DR   PRO; PR:O65657; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O65657; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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   Lipoprotein; Metal-binding; Methylation; Prenylation; Reference proteome.
FT   CHAIN           1..155
FT                   /note="Heavy metal-associated isoprenylated plant protein
FT                   23"
FT                   /id="PRO_0000437829"
FT   PROPEP          156..158
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000437830"
FT   DOMAIN          31..94
FT                   /note="HMA"
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   BINDING         45
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   MOD_RES         155
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT   LIPID           155
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZN7"
SQ   SEQUENCE   158 AA;  17355 MW;  4B3FC92237EBE961 CRC64;
     MGVGGTLEYI SELIGNGGSH SYGKRKKKKQ FQTVELKVRM DCDGCVLKIK NSLSSLKGVK
     TVEINKKQQK VTVSGYADAS KVLKKAKATG KKAEIWPYVP YNLVAQPYIA QAYDKKAPPG
     YVRKVDPNVT TGTMAVYYDD PSYTSLFSDD NPNACSIM
 
 
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