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PHB3_ARATH
ID   PHB3_ARATH              Reviewed;         277 AA.
AC   O04331;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Prohibitin-3, mitochondrial;
DE            Short=Atphb3;
DE   AltName: Full=Protein ENHANCED ETHYLENE RESPONSE 3;
GN   Name=PHB3; Synonyms=EER3; OrderedLocusNames=At5g40770; ORFNames=K1B16.2;
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 [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=9132067; DOI=10.1023/a:1005737026289;
RA   Snedden W.A., Fromm H.;
RT   "Characterization of the plant homologue of prohibitin, a gene associated
RT   with antiproliferative activity in mammalian cells.";
RL   Plant Mol. Biol. 33:753-756(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Sun L., Goodman H.M.;
RT   "Arabidopsis genes encoding prohibitin: importance for early development.";
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX   PubMed=12837548; DOI=10.1016/s0005-2728(03)00045-8;
RA   Heazlewood J.L., Howell K.A., Millar A.H.;
RT   "Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian
RT   and fungal components coupled with plant-specific subunits.";
RL   Biochim. Biophys. Acta 1604:159-169(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA   Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA   Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT   "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT   proteome.";
RL   Mol. Cell. Proteomics 3:675-691(2004).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-165, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=17525078; DOI=10.1093/jxb/erm086;
RA   Christians M.J., Larsen P.B.;
RT   "Mutational loss of the prohibitin AtPHB3 results in an extreme
RT   constitutive ethylene response phenotype coupled with partial loss of
RT   ethylene-inducible gene expression in Arabidopsis seedlings.";
RL   J. Exp. Bot. 58:2237-2248(2007).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=cv. Columbia;
RX   PubMed=17883375; DOI=10.1111/j.1365-313x.2007.03276.x;
RA   Van Aken O., Pecenkova T., van de Cotte B., De Rycke R., Eeckhout D.,
RA   Fromm H., De Jaeger G., Witters E., Beemster G.T.S., Inze D.,
RA   Van Breusegem F.;
RT   "Mitochondrial type-I prohibitins of Arabidopsis thaliana are required for
RT   supporting proficient meristem development.";
RL   Plant J. 52:850-864(2007).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=18189341; DOI=10.1021/pr700595p;
RA   Meyer E.H., Taylor N.L., Millar A.H.;
RT   "Resolving and identifying protein components of plant mitochondrial
RT   respiratory complexes using three dimensions of gel electrophoresis.";
RL   J. Proteome Res. 7:786-794(2008).
RN   [13]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-37.
RX   PubMed=20068191; DOI=10.1105/tpc.109.072066;
RA   Wang Y., Ries A., Wu K., Yang A., Crawford N.M.;
RT   "The Arabidopsis prohibitin gene PHB3 functions in nitric oxide-mediated
RT   responses and in hydrogen peroxide-induced nitric oxide accumulation.";
RL   Plant Cell 22:249-259(2010).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21841088; DOI=10.1104/pp.111.182352;
RA   Klodmann J., Senkler M., Rode C., Braun H.-P.;
RT   "Defining the protein complex proteome of plant mitochondria.";
RL   Plant Physiol. 157:587-598(2011).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the
CC       stabilization of newly synthesized mitochondrial proteins (By
CC       similarity). Necessary for mitochondrial and cell metabolism and
CC       biogenesis. Required to regulate the ethylene-mediated signaling;
CC       involved in growth maintenance in the presence of ethylene. Functions
CC       in nitric oxide (NO)-mediated responses and in hydrogen peroxide-
CC       induced NO accumulation. {ECO:0000250, ECO:0000269|PubMed:17525078,
CC       ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:20068191}.
CC   -!- SUBUNIT: Component of a prohibitin multimeric complex in mitochondrial
CC       membranes. {ECO:0000269|PubMed:12837548, ECO:0000269|PubMed:17883375,
CC       ECO:0000269|PubMed:18189341}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC       Mitochondrion inner membrane {ECO:0000269|PubMed:12837548,
CC       ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17883375,
CC       ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:21841088,
CC       ECO:0000269|PubMed:9132067}; Single-pass type II membrane protein
CC       {ECO:0000255}. Nucleus {ECO:0000269|PubMed:17525078}. Cytoplasm
CC       {ECO:0000269|PubMed:17525078}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in proliferative tissues,
CC       including vasculature, shoot and root apical tissues. Expressed in
CC       roots, stems, leaves and flowers (at protein level).
CC   -!- DISRUPTION PHENOTYPE: Extreme constitutive ethylene response in air
CC       associated with a partial loss of ethylene-inducible gene expression
CC       and an increased ethylene production. Mitochondrial swelling, decreased
CC       meristematic cell production, increased cell division time and reduced
CC       cell expansion rates, leading to severe growth retardation. Reduced
CC       sensitivity to salt stress and defective in H(2)O(2)-induced nitric
CC       oxide (NO) accumulation, light-induced NO in cotyledons, abscisic acid
CC       (ABA)-induced NO accumulation and stomatal closure, and in auxin-
CC       induced lateral root formation. {ECO:0000269|PubMed:17525078,
CC       ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:20068191}.
CC   -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR   EMBL; U69155; AAC49691.1; -; mRNA.
DR   EMBL; U66593; AAD00157.1; -; mRNA.
DR   EMBL; AB015470; BAB08838.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94592.1; -; Genomic_DNA.
DR   EMBL; AY054499; AAK96690.1; -; mRNA.
DR   EMBL; AY114631; AAM47950.1; -; mRNA.
DR   EMBL; AY087641; AAM65180.1; -; mRNA.
DR   RefSeq; NP_198893.1; NM_123442.5.
DR   AlphaFoldDB; O04331; -.
DR   SMR; O04331; -.
DR   BioGRID; 19328; 29.
DR   IntAct; O04331; 3.
DR   STRING; 3702.AT5G40770.1; -.
DR   iPTMnet; O04331; -.
DR   PaxDb; O04331; -.
DR   PRIDE; O04331; -.
DR   ProMEX; O04331; -.
DR   ProteomicsDB; 235078; -.
DR   EnsemblPlants; AT5G40770.1; AT5G40770.1; AT5G40770.
DR   GeneID; 834077; -.
DR   Gramene; AT5G40770.1; AT5G40770.1; AT5G40770.
DR   KEGG; ath:AT5G40770; -.
DR   Araport; AT5G40770; -.
DR   TAIR; locus:2154810; AT5G40770.
DR   eggNOG; KOG3083; Eukaryota.
DR   HOGENOM; CLU_047969_0_2_1; -.
DR   InParanoid; O04331; -.
DR   OMA; SAIEHKQ; -.
DR   OrthoDB; 1089994at2759; -.
DR   PhylomeDB; O04331; -.
DR   PRO; PR:O04331; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O04331; baseline and differential.
DR   Genevisible; O04331; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:TAIR.
DR   GO; GO:0051301; P:cell division; IMP:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:TAIR.
DR   GO; GO:0051782; P:negative regulation of cell division; IMP:TAIR.
DR   GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR   GO; GO:0009723; P:response to ethylene; IMP:UniProtKB.
DR   GO; GO:0071731; P:response to nitric oxide; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0009697; P:salicylic acid biosynthetic process; IMP:TAIR.
DR   CDD; cd03401; SPFH_prohibitin; 1.
DR   Gene3D; 3.30.479.30; -; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR000163; Prohibitin.
DR   PANTHER; PTHR23222; PTHR23222; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00679; PROHIBITIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; SSF117892; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Cytoplasm; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleus; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..277
FT                   /note="Prohibitin-3, mitochondrial"
FT                   /id="PRO_0000420598"
FT   TOPO_DOM        2..6
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..277
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MUTAGEN         37
FT                   /note="G->D: In phb3-3; reduced sensitivity to salt stress
FT                   and defective in H(2)O(2)-induced nitric oxide (NO)
FT                   accumulation, light-induced NO in cotyledons, abscisic acid
FT                   (ABA)-induced NO accumulation and stomatal closure, and in
FT                   auxin-induced lateral root formation."
FT                   /evidence="ECO:0000269|PubMed:20068191"
FT   MUTAGEN         165
FT                   /note="D->N: In eer3-1; increased sensitivity and profound
FT                   exaggeration of response to ethylene, as well as increased
FT                   ethylene production."
FT                   /evidence="ECO:0000269|PubMed:17525078"
SQ   SEQUENCE   277 AA;  30400 MW;  1D57190F11370693 CRC64;
     MGSQQAAVSF LSNLAKAAFG LGTAATVLNT SLFTVDGGER AVIFDRFRGV MDQTVGEGTH
     FLIPILQRPH IFDIRTKPHT FSSISGTKDL QMVNLTLRVL SRPEVSRLPY IFQTLGLEYD
     EKVLPSIGNE VLKAVVAQFN ADQLLTERPH VSALVRESLI TRAKDFNIVL DDVAITHLSY
     GVEFSRAVEQ KQVAQQEAER SKFVVMKADQ ERRAAVIRAE GESEAAQLIS DATAKAGMGL
     IELRRIEASR EIASTLARSP NVAYLPGGQS MLFALNR
 
 
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