ID   PHB2_ARATH              Reviewed;         286 AA.
AC   Q9ZNT7; F4I2J2;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Prohibitin-2, mitochondrial;
DE            Short=Atphb2;
GN   Name=PHB2; OrderedLocusNames=At1g03860; ORFNames=F21M11.21;
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] (ISOFORM 1).
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Hatzfeld Y., Logan H.M., Cathala N., Davidian J.-C.;
RT   "Cloning of an Arabidopsis thaliana prohibitin-like cDNA by functional
RT   complementation of a sulfate transport yeast mutant.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [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] (ISOFORM 1).
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   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   [7]
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   [8]
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   [9]
RP   TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP   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   [10]
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   [11]
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).
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:12837548, ECO:0000269|PubMed:17883375,
CC       ECO:0000269|PubMed:18189341}.
CC   -!- INTERACTION:
CC       Q9ZNT7; Q9LF53: RGL3; NbExp=3; IntAct=EBI-531812, EBI-15681313;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:12837548, ECO:0000269|PubMed:14671022,
CC       ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:18189341,
CC       ECO:0000269|PubMed:21841088}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:12837548, ECO:0000269|PubMed:14671022,
CC       ECO:0000269|PubMed:17883375, ECO:0000269|PubMed:18189341,
CC       ECO:0000269|PubMed:21841088}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ZNT7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ZNT7-2; Sequence=VSP_044541;
CC   -!- TISSUE SPECIFICITY: Mostly expressed in proliferative tissues,
CC       including vasculature, shoot and root apical tissues.
CC       {ECO:0000269|PubMed:17883375}.
CC   -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR   EMBL; U66592; AAD00156.1; -; mRNA.
DR   EMBL; U89791; AAD09244.1; -; mRNA.
DR   EMBL; AC003027; AAD10682.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27624.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27625.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27626.1; -; Genomic_DNA.
DR   EMBL; AF370317; AAK44132.1; -; mRNA.
DR   EMBL; AY063102; AAL34276.1; -; mRNA.
DR   PIR; C86169; C86169.
DR   RefSeq; NP_171882.1; NM_100266.3. [Q9ZNT7-1]
DR   RefSeq; NP_973755.1; NM_202026.2. [Q9ZNT7-2]
DR   RefSeq; NP_973756.1; NM_202027.2. [Q9ZNT7-1]
DR   AlphaFoldDB; Q9ZNT7; -.
DR   SMR; Q9ZNT7; -.
DR   BioGRID; 24464; 9.
DR   IntAct; Q9ZNT7; 4.
DR   STRING; 3702.Q9ZNT7; -.
DR   PaxDb; 3702-AT1G03860-3; -.
DR   ProteomicsDB; 234719; -. [Q9ZNT7-1]
DR   EnsemblPlants; AT1G03860.1; AT1G03860.1; AT1G03860. [Q9ZNT7-1]
DR   EnsemblPlants; AT1G03860.2; AT1G03860.2; AT1G03860. [Q9ZNT7-2]
DR   EnsemblPlants; AT1G03860.3; AT1G03860.3; AT1G03860. [Q9ZNT7-1]
DR   GeneID; 839228; -.
DR   Gramene; AT1G03860.1; AT1G03860.1; AT1G03860. [Q9ZNT7-1]
DR   Gramene; AT1G03860.2; AT1G03860.2; AT1G03860. [Q9ZNT7-2]
DR   Gramene; AT1G03860.3; AT1G03860.3; AT1G03860. [Q9ZNT7-1]
DR   KEGG; ath:AT1G03860; -.
DR   Araport; AT1G03860; -.
DR   TAIR; AT1G03860; PHB2.
DR   eggNOG; KOG3090; Eukaryota.
DR   HOGENOM; CLU_047969_0_2_1; -.
DR   InParanoid; Q9ZNT7; -.
DR   OMA; DTHMPPP; -.
DR   OrthoDB; 1330394at2759; -.
DR   PhylomeDB; Q9ZNT7; -.
DR   PRO; PR:Q9ZNT7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9ZNT7; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA: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   CDD; cd03401; SPFH_prohibitin; 1.
DR   Gene3D; 3.30.479.30; Band 7 domain; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR000163; Prohibitin.
DR   PANTHER; PTHR23222; PROHIBITIN; 1.
DR   PANTHER; PTHR23222:SF20; PROHIBITIN-2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00679; PROHIBITIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
DR   Genevisible; Q9ZNT7; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..286
FT                   /note="Prohibitin-2, mitochondrial"
FT                   /id="PRO_0000420597"
FT   TOPO_DOM        1..13
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..286
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   COILED          186..219
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..65
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044541"
SQ   SEQUENCE   286 AA;  31811 MW;  89A48ECBA4F56DB8 CRC64;
     MSFNKVPNIP GAPALSALLK VSVIGGLGVY ALTNSLYNVD GGHRAVMFNR LTGIKEKVYP
     EGTHFMVPWF ERPIIYDVRA RPYLVESTTG SHDLQMVKIG LRVLTRPMGD RLPQIYRTLG
     ENYSERVLPS IIHETLKAVV AQYNASQLIT QREAVSREIR KILTERASNF DIALDDVSIT
     TLTFGKEFTA AIEAKQVAAQ EAERAKFIVE KAEQDRRSAV IRAQGEAKSA QLIGQAIANN
     QAFITLRKIE AAREIAQTIA QSANKVYLSS NDLLLNLQEM NLEPKK
//