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HIP44_ARATH
ID   HIP44_ARATH             Reviewed;         183 AA.
AC   F4JMB8; Q1G3J1;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Heavy metal-associated isoprenylated plant protein 44 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE            Short=AtHIP44 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
DE   Flags: Precursor;
GN   Name=HIPP44 {ECO:0000303|PubMed:21072340, ECO:0000303|PubMed:23368984};
GN   OrderedLocusNames=At4g10465 {ECO:0000312|Araport:AT4G10465};
GN   ORFNames=F7L13 {ECO:0000312|EMBL:AL049524};
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=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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
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   -!- SIMILARITY: Belongs to the HIPP family. {ECO:0000305}.
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DR   EMBL; AL049524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002687; AEE82886.1; -; Genomic_DNA.
DR   EMBL; DQ487593; ABF59244.1; -; mRNA.
DR   RefSeq; NP_001078368.1; NM_001084899.2.
DR   AlphaFoldDB; F4JMB8; -.
DR   SMR; F4JMB8; -.
DR   STRING; 3702.AT4G10465.1; -.
DR   PaxDb; F4JMB8; -.
DR   PRIDE; F4JMB8; -.
DR   ProteomicsDB; 230135; -.
DR   EnsemblPlants; AT4G10465.1; AT4G10465.1; AT4G10465.
DR   GeneID; 5008132; -.
DR   Gramene; AT4G10465.1; AT4G10465.1; AT4G10465.
DR   KEGG; ath:AT4G10465; -.
DR   Araport; AT4G10465; -.
DR   TAIR; locus:4010713877; AT4G10465.
DR   eggNOG; KOG1603; Eukaryota.
DR   HOGENOM; CLU_100095_0_0_1; -.
DR   InParanoid; F4JMB8; -.
DR   OMA; GCERVVT; -.
DR   OrthoDB; 1365780at2759; -.
DR   PRO; PR:F4JMB8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JMB8; baseline.
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   2: Evidence at transcript level;
KW   Lipoprotein; Metal-binding; Methylation; Prenylation; Reference proteome.
FT   CHAIN           1..180
FT                   /note="Heavy metal-associated isoprenylated plant protein
FT                   44"
FT                   /id="PRO_0000437861"
FT   PROPEP          181..183
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000437862"
FT   DOMAIN          50..113
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         61
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         64
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   MOD_RES         180
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT   LIPID           180
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SZN7"
FT   CONFLICT        65
FT                   /note="V -> L (in Ref. 3; ABF59244)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   183 AA;  21009 MW;  80963BD9E48FB46F CRC64;
     MSSLIVKSLG SIVSIIARIF FFRRSRPVSN PRTTAHISYF RMSRKRPLSL QTVELKVRMC
     CTGCVRIVRN AISKLRGVDS VEVDKELGRV RVVGYVDRNK VLKAVRRAGK RAEFSPYPEP
     PLYFTSTQNY FVDPSKEFKE SYNYYRHGYN GTEQHGNIPV GSRGDDRVSN MFNDDNVNAC
     RLM
 
 
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