MIP_ARATH
ID MIP_ARATH Reviewed; 706 AA.
AC F4KDA5; Q9FHN0;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Mitochondrial intermediate peptidase, mitochondrial {ECO:0000305};
DE EC=3.4.24.- {ECO:0000305};
DE AltName: Full=AtOCT1 {ECO:0000303|PubMed:25732537};
DE Flags: Precursor;
GN Name=OCT1 {ECO:0000303|PubMed:25732537}; Synonyms=MIP {ECO:0000305};
GN OrderedLocusNames=At5g51540 {ECO:0000312|Araport:AT5G51540};
GN ORFNames=K17N15.9 {ECO:0000312|EMBL:BAB08670.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 IDENTIFICATION, AND REVIEW.
RX PubMed=22085399; DOI=10.1111/j.1399-3054.2011.01542.x;
RA Kwasniak M., Pogorzelec L., Migdal I., Smakowska E., Janska H.;
RT "Proteolytic system of plant mitochondria.";
RL Physiol. Plantarum 145:187-195(2012).
RN [4]
RP REVIEW.
RX PubMed=22495024; DOI=10.1016/j.bbamcr.2012.03.012;
RA Teixeira P.F., Glaser E.;
RT "Processing peptidases in mitochondria and chloroplasts.";
RL Biochim. Biophys. Acta 1833:360-370(2013).
RN [5]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Aminopeptidase which cleaves preproteins, imported into the
CC mitochondrion, to their mature size. Could cleave both preproteins and
CC preprotein intermediates already cleaved by the mitochondrial
CC processing peptidase (MPP). {ECO:0000269|PubMed:25732537}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25732537}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08670.1; Type=Erroneous gene model prediction; Note=The predicted gene At5g51540 has been split into 2 genes: At5g51540 and At5g51545.; Evidence={ECO:0000305};
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DR EMBL; AB018109; BAB08670.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96095.1; -; Genomic_DNA.
DR RefSeq; NP_199967.2; NM_124533.2.
DR AlphaFoldDB; F4KDA5; -.
DR SMR; F4KDA5; -.
DR STRING; 3702.AT5G51540.1; -.
DR MEROPS; M03.A12; -.
DR PaxDb; F4KDA5; -.
DR PRIDE; F4KDA5; -.
DR ProteomicsDB; 250712; -.
DR EnsemblPlants; AT5G51540.1; AT5G51540.1; AT5G51540.
DR GeneID; 835228; -.
DR Gramene; AT5G51540.1; AT5G51540.1; AT5G51540.
DR KEGG; ath:AT5G51540; -.
DR Araport; AT5G51540; -.
DR TAIR; locus:2153067; AT5G51540.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_2_1; -.
DR InParanoid; F4KDA5; -.
DR OMA; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
DR PRO; PR:F4KDA5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KDA5; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PTHR11804; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..706
FT /note="Mitochondrial intermediate peptidase, mitochondrial"
FT /id="PRO_0000425141"
FT REGION 212..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 79925 MW; CC04E79B4EAC4685 CRC64;
MWKLTRRLQP HINSTRWLVR NFRNGGAGDA TGLYGFDHLK TAKGFQRFVA DAIERSGELV
SYISGMPSSP EIIKAMDEIS DTVCCVVDSA ELCRQTHPDR EFVEEANKAA IEMNDYLHHL
NTNHTLYAAV KKAEQDSNLL TKEASRTAHH LRMDFERGGI HLDPEKLDKV NNLTTNIFQL
CREFSENIAD DPGHVDIFPG SRIPRHLHHL LNPTYRSTSG GSRGSTRSAH KSKQKGFRIN
TDPRTVSSIL QWTSDEEVRK MVYIQGNSVP HANHGVLEKL IAARHELSQM MGCNSYADIM
VEPNLAKSPK VVTSFLQELS KTVKPKADEE FIAIRDFKRE KCGNPSAELE PWDETYYTSM
MKSSINDVDT AVVASYFPLP QCIEGLKVLV ESLFGATFHT IPLAPGESWH PNVVKLSLHH
PDEGDLGYLY LDLYSRKGKY PGCASFAIRG GRKISETEYQ LPVIALVCNF SRACDSSIVK
LNHSEVEVLF HEFGHALHSL LSRTDYQHFS GTRVALDLAE MPSNLFEYYA WDYRLLKRFA
RHYSTGETIP EKLVNSLQGA RNMFAATEMQ RQVFYALIDQ MLFGEQPETA RDVSHLVAEL
KRQHTSWNHV EGTHWYIRFS HLLNYGAGYY SYLYAKCFAS TIWQSICEED PLSLNTGTLL
REKFFKHGGA KDPAELLTDL AGKEIISVHG EGIVPATTYL LNELRL
