PHB4_ARATH
ID PHB4_ARATH Reviewed; 279 AA.
AC Q9LK25; Q84WL7; Q8LBC7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Prohibitin-4, mitochondrial;
DE Short=Atphb4;
GN Name=PHB4; OrderedLocusNames=At3g27280; ORFNames=K17E12.10;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP INDUCTION BY IMBIBITION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=16455359; DOI=10.1016/j.jplph.2005.04.032;
RA de Diego J.G., David Rodriguez F., Rodriguez Lorenzo J.L., Grappin P.,
RA Cervantes E.;
RT "cDNA-AFLP analysis of seed germination in Arabidopsis thaliana identifies
RT transposons and new genomic sequences.";
RL J. Plant Physiol. 163:452-462(2006).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY IMBIBITION.
RC STRAIN=cv. Columbia;
RX PubMed=16876910; DOI=10.1016/j.jplph.2006.05.002;
RA De Diego J.G., David Rodriguez F., Rodriguez Lorenzo J.L., Cervantes E.;
RT "The prohibitin genes in Arabidopsis thaliana: expression in seeds,
RT hormonal regulation and possible role in cell cycle control during seed
RT germination.";
RL J. Plant Physiol. 164:371-373(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [10]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBUNIT, SUBCELLULAR LOCATION, AND
RP 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 [11]
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 [12]
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 [13]
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.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of a prohibitin multimeric complex in mitochondrial
CC membranes. {ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:18189341}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17883375,
CC ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:21841088}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:18189341,
CC ECO:0000269|PubMed:21841088}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in proliferative tissues,
CC including vasculature, shoot and root apical tissues. Accumulates in
CC dry seeds. {ECO:0000269|PubMed:16876910, ECO:0000269|PubMed:17883375}.
CC -!- DEVELOPMENTAL STAGE: Observed in all organs primordia and meristems. In
CC cotyledons, hypocotyls and differentiating leaves, present in stomatal
CC meristemoid cells, guard mother cells and trichomes. Within the
CC anthers, transiently expressed in the proximity of the sporogenous
CC tissue. Accumulates in embryos at globular stages, except in suspensor
CC cell. In root elongation zones, mostly present in epidermal cells,
CC particularly in trichoblasts. {ECO:0000269|PubMed:17883375}.
CC -!- INDUCTION: Transcripts levels decrease upon imbibition but remains
CC stable at the protein level. {ECO:0000269|PubMed:16455359,
CC ECO:0000269|PubMed:16876910}.
CC -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP000381; BAB02123.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77287.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77288.1; -; Genomic_DNA.
DR EMBL; BT003072; AAO23637.1; -; mRNA.
DR EMBL; AK227607; BAE99598.1; -; mRNA.
DR EMBL; AY087293; AAM64845.1; -; mRNA.
DR RefSeq; NP_189364.1; NM_113642.4.
DR RefSeq; NP_974369.1; NM_202640.2.
DR AlphaFoldDB; Q9LK25; -.
DR SMR; Q9LK25; -.
DR BioGRID; 7677; 28.
DR IntAct; Q9LK25; 1.
DR STRING; 3702.AT3G27280.2; -.
DR iPTMnet; Q9LK25; -.
DR PaxDb; Q9LK25; -.
DR PRIDE; Q9LK25; -.
DR ProteomicsDB; 236346; -.
DR EnsemblPlants; AT3G27280.1; AT3G27280.1; AT3G27280.
DR EnsemblPlants; AT3G27280.2; AT3G27280.2; AT3G27280.
DR GeneID; 822347; -.
DR Gramene; AT3G27280.1; AT3G27280.1; AT3G27280.
DR Gramene; AT3G27280.2; AT3G27280.2; AT3G27280.
DR KEGG; ath:AT3G27280; -.
DR Araport; AT3G27280; -.
DR TAIR; locus:2086538; AT3G27280.
DR eggNOG; KOG3083; Eukaryota.
DR HOGENOM; CLU_047969_0_2_1; -.
DR InParanoid; Q9LK25; -.
DR OMA; WNITYLL; -.
DR OrthoDB; 1089994at2759; -.
DR PhylomeDB; Q9LK25; -.
DR PRO; PR:Q9LK25; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK25; baseline and differential.
DR Genevisible; Q9LK25; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
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; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..279
FT /note="Prohibitin-4, mitochondrial"
FT /id="PRO_0000420599"
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..279
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 6
FT /note="V -> A (in Ref. 5; AAM64845)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="K -> E (in Ref. 3; AAO23637 and 4; BAE99598)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="D -> E (in Ref. 5; AAM64845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30638 MW; 31AA08A4BADDCE8C CRC64;
MGSQQVAISF LTNLAKAAFG LGVAATALNS SLYTVDGGER AVLFDRFRGV LDQTVGEGTH
FLIPYLQTPH IYDIRTKPHT FSSKSGTKDL QMVNLTLRVL FRPEVSRLPY IFQTLGLEYD
EKVLPSIGNE VLKAVVANFN ADQLLTERPQ VSALVRDALI KRAREFNIEL DDIAITHLSY
GAEFSRAVEA KQVAQQEAER SKFVVMKADQ ERRAAVIRAE GESEAAQLIS DATAKAGMGL
IELRRIEASR EVAATLARSP NVAYLPGGQS MLFNLNPGR
