MPPA2_ARATH
ID MPPA2_ARATH Reviewed; 499 AA.
AC O04308; B9DHQ2; Q94C54;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable mitochondrial-processing peptidase subunit alpha-2, chloroplastic/mitochondrial;
DE AltName: Full=Alpha-MPP 2;
DE AltName: Full=Complex III subunit II;
DE AltName: Full=Core protein II;
DE AltName: Full=Cytochrome b-c1 complex subunit 2-2, mitochondrial;
DE AltName: Full=Inactive zinc metalloprotease alpha-2 {ECO:0000305};
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase core protein 2-2;
DE Flags: Precursor;
GN Name=MPPalpha2;
GN OrderedLocusNames=At3g16480 {ECO:0000312|Araport:AT3G16480};
GN ORFNames=MDC8.11 {ECO:0000312|EMBL:BAB01147.1},
GN T02O04.2 {ECO:0000312|EMBL:AAB63629.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 350-499.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP SUBUNIT.
RX PubMed=12970493; DOI=10.1104/pp.103.024620;
RA Eubel H., Jansch L., Braun H.P.;
RT "New insights into the respiratory chain of plant mitochondria.
RT Supercomplexes and a unique composition of complex II.";
RL Plant Physiol. 133:274-286(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 SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [9]
RP SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=18305213; DOI=10.1104/pp.107.111260;
RA Zsigmond L., Rigo G., Szarka A., Szekely G., Oetvoes K., Darula Z.,
RA Medzihradszky K.F., Koncz C., Koncz Z., Szabados L.;
RT "Arabidopsis PPR40 connects abiotic stress responses to mitochondrial
RT electron transport.";
RL Plant Physiol. 146:1721-1737(2008).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=22131051; DOI=10.1093/mp/ssr092;
RA Baudisch B., Kloesgen R.B.;
RT "Dual targeting of a processing peptidase into both endosymbiotic
RT organelles mediated by a transport signal of unusual architecture.";
RL Mol. Plant 5:494-503(2012).
RN [11]
RP INTERACTION WITH TIM23-2.
RX PubMed=22730406; DOI=10.1105/tpc.112.098731;
RA Wang Y., Carrie C., Giraud E., Elhafez D., Narsai R., Duncan O., Whelan J.,
RA Murcha M.W.;
RT "Dual location of the mitochondrial preprotein transporters B14.7 and
RT Tim23-2 in complex I and the TIM17:23 complex in Arabidopsis links
RT mitochondrial activity and biogenesis.";
RL Plant Cell 24:2675-2695(2012).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000250|UniProtKB:P11914}.
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c. {ECO:0000250|UniProtKB:P07257}.
CC -!- SUBUNIT: Heterodimer of alpha and beta subunits, forming the
CC mitochondrial processing protease (MPP) in which subunit alpha is
CC involved in substrate recognition and binding and subunit beta is the
CC catalytic subunit (By similarity). Component of the ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII), a multisubunit enzyme composed of 10 subunits. The complex is
CC composed of 3 respiratory subunits cytochrome b (MT-CYB), cytochrome c1
CC (CYC1-1 or CYC1-2) and Rieske protein (UCR1-1 or UCR1-2), 2 core
CC protein subunits MPPalpha1 (or MPPalpha2) and MPPB, and 5 low-molecular
CC weight protein subunits QCR7-1 (or QCR7-2), UCRQ-1 (or UCRQ-2), QCR9,
CC UCRY and probably QCR6-1 (or QCR6-2) (PubMed:18189341,
CC PubMed:18305213). The complex exists as an obligatory dimer and forms
CC supercomplexes (SCs) in the inner mitochondrial membrane with NADH-
CC ubiquinone oxidoreductase (complex I, CI), resulting in different
CC assemblies (supercomplexes SCI(1)III(2) and SCI(2)III(4))
CC (PubMed:12970493). Interacts with TIM23-2 (PubMed:22730406).
CC {ECO:0000250|UniProtKB:P11914, ECO:0000269|PubMed:12970493,
CC ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:18305213,
CC ECO:0000269|PubMed:22730406}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:22131051}. Mitochondrion matrix
CC {ECO:0000269|PubMed:22131051}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:22131051}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:P07257}; Matrix side
CC {ECO:0000250|UniProtKB:P07257}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- CAUTION: Does not seem to have a protease activity as it lacks one of
CC the conserved zinc-binding sites. {ECO:0000305}.
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DR EMBL; AC001645; AAB63629.1; -; Genomic_DNA.
DR EMBL; AP000373; BAB01147.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75825.1; -; Genomic_DNA.
DR EMBL; AY035171; AAK59675.1; -; mRNA.
DR EMBL; AY142643; AAN13101.1; -; mRNA.
DR EMBL; AK317606; BAH20269.1; -; mRNA.
DR RefSeq; NP_566548.1; NM_112519.4.
DR AlphaFoldDB; O04308; -.
DR SMR; O04308; -.
DR BioGRID; 6230; 5.
DR STRING; 3702.AT3G16480.1; -.
DR iPTMnet; O04308; -.
DR SwissPalm; O04308; -.
DR PaxDb; O04308; -.
DR PRIDE; O04308; -.
DR ProteomicsDB; 250952; -.
DR EnsemblPlants; AT3G16480.1; AT3G16480.1; AT3G16480.
DR GeneID; 820896; -.
DR Gramene; AT3G16480.1; AT3G16480.1; AT3G16480.
DR KEGG; ath:AT3G16480; -.
DR Araport; AT3G16480; -.
DR TAIR; locus:2088309; AT3G16480.
DR eggNOG; KOG2067; Eukaryota.
DR HOGENOM; CLU_009902_5_1_1; -.
DR InParanoid; O04308; -.
DR OMA; QMIASED; -.
DR OrthoDB; 631107at2759; -.
DR PhylomeDB; O04308; -.
DR BioCyc; ARA:AT3G16480-MON; -.
DR BioCyc; MetaCyc:AT3G16480-MON; -.
DR PRO; PR:O04308; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O04308; baseline and differential.
DR Genevisible; O04308; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:TAIR.
DR GO; GO:0005758; C:mitochondrial intermembrane space; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; HDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:TAIR.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000269|PubMed:22131051"
FT CHAIN ?..499
FT /note="Probable mitochondrial-processing peptidase subunit
FT alpha-2, chloroplastic/mitochondrial"
FT /id="PRO_0000026775"
FT CONFLICT 304
FT /note="T -> K (in Ref. 4; AAK59675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 54053 MW; 6B8203674FAEC56E CRC64;
MYRTAASRAK ALKGILNHNF RASRYASSSA VATSSSSSSW LSGGYSSSLP SMNIPLAGVS
LPPPLSDHVE PSKLKTTTLP NGLTIATEMS PNPAASIGLY VDCGSIYETP QFRGATHLLE
RMAFKSTLNR SHFRLVREIE AIGGNTSASA SREQMGYTID ALKTYVPEMV EVLIDSVRNP
AFLDWEVNEE LRKVKVEIGE FATNPMGFLL EAVHSAGYSG ALANPLYAPE SAITGLTGEV
LENFVFENYT ASRMVLAASG VDHEELLKVV EPLLSDLPNV PRPAEPKSQY VGGDFRQHTG
GEATHFALAF EVPGWNNEKE AIIATVLQML MGGGGSFSAG GPGKGMHSWL YLRLLNQHQQ
FQSCTAFTSV FNNTGLFGIY GCTSPEFASQ GIELVASEMN AVADGKVNQK HLDRAKAATK
SAILMNLESR MIAAEDIGRQ ILTYGERKPV DQFLKTVDQL TLKDIADFTS KVITKPLTMA
TFGDVLNVPS YDSVSKRFR
