ICP55_ARATH
ID ICP55_ARATH Reviewed; 493 AA.
AC F4HZG9; F4HZH0; Q8GYQ0; Q9ZPZ5; W6HYK5;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Intermediate cleaving peptidase 55, mitochondrial {ECO:0000305};
DE EC=3.4.11.- {ECO:0000305};
DE AltName: Full=AtICP55 {ECO:0000303|PubMed:25732537};
DE AltName: Full=Protein INTERMEDIATE CLEAVAGE PEPTIDASE 55 {ECO:0000303|PubMed:25862457};
DE Flags: Precursor;
GN Name=ICP55 {ECO:0000303|PubMed:25732537, ECO:0000312|EMBL:AHJ59463.1};
GN OrderedLocusNames=At1g09300 {ECO:0000312|Araport:AT1G09300};
GN ORFNames=T31J12.2 {ECO:0000312|EMBL:AAD18095.1};
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 [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25862457; DOI=10.1104/pp.15.00300;
RA Huang S., Nelson C.J., Li L., Taylor N.L., Stroeher E., Peteriet J.,
RA Millar A.H.;
RT "INTERMEDIATE CLEAVAGE PEPTIDASE55 modifies enzyme amino termini and alters
RT protein stability in Arabidopsis mitochondria.";
RL Plant Physiol. 168:415-427(2015).
RN [2]
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 [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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
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 preprotein intermediates that
CC carry destabilizing N-ter amino acid residues after the mitochondrial
CC processing peptidase (MPP) cleavage site and is thus critical for
CC stabilization of the mitochondrial proteome.
CC {ECO:0000269|PubMed:25732537, ECO:0000269|PubMed:25862457}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:25732537}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:25732537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4HZG9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HZG9-2; Sequence=VSP_059054;
CC -!- DISRUPTION PHENOTYPE: Altered mitochondrial protein stability.
CC {ECO:0000269|PubMed:25862457}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD18095.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AHJ59463.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC42121.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; KF921304; AHJ59463.1; ALT_FRAME; mRNA.
DR EMBL; AC006416; AAD18095.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28426.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28427.1; -; Genomic_DNA.
DR EMBL; AK117456; BAC42121.1; ALT_FRAME; mRNA.
DR PIR; A86226; A86226.
DR RefSeq; NP_001117254.1; NM_001123782.1. [F4HZG9-2]
DR RefSeq; NP_172401.2; NM_100800.4. [F4HZG9-1]
DR AlphaFoldDB; F4HZG9; -.
DR SMR; F4HZG9; -.
DR STRING; 3702.AT1G09300.1; -.
DR MEROPS; M24.A14; -.
DR PaxDb; F4HZG9; -.
DR PRIDE; F4HZG9; -.
DR ProteomicsDB; 228766; -. [F4HZG9-1]
DR EnsemblPlants; AT1G09300.1; AT1G09300.1; AT1G09300. [F4HZG9-1]
DR EnsemblPlants; AT1G09300.2; AT1G09300.2; AT1G09300. [F4HZG9-2]
DR GeneID; 837451; -.
DR Gramene; AT1G09300.1; AT1G09300.1; AT1G09300. [F4HZG9-1]
DR Gramene; AT1G09300.2; AT1G09300.2; AT1G09300. [F4HZG9-2]
DR KEGG; ath:AT1G09300; -.
DR Araport; AT1G09300; -.
DR TAIR; locus:2203038; AT1G09300.
DR eggNOG; KOG2414; Eukaryota.
DR InParanoid; F4HZG9; -.
DR OMA; GWADTEL; -.
DR OrthoDB; 352329at2759; -.
DR BRENDA; 3.4.11.26; 399.
DR BRENDA; 3.4.24.59; 399.
DR PRO; PR:F4HZG9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HZG9; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; IMP:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IMP:TAIR.
DR GO; GO:0050821; P:protein stabilization; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IGI:TAIR.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aminopeptidase; Hydrolase; Manganese; Metal-binding;
KW Metalloprotease; Mitochondrion; Nucleus; Protease; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..493
FT /note="Intermediate cleaving peptidase 55, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441250"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 383
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 410
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..41
FT /note="MQFLARNLVRRVSRTQVVSRNAYSTQTVRDIGQPTPASHPH -> MLRWFAL
FT PHQ (in isoform 2)"
FT /id="VSP_059054"
FT CONFLICT 398
FT /note="D -> G (in Ref. 4; BAC42121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54982 MW; 06BDBA4FCF901825 CRC64;
MQFLARNLVR RVSRTQVVSR NAYSTQTVRD IGQPTPASHP HLMAEGEVTP GIRIEEYIGR
RKKLVELLPE NSLAIISSAP VKMMTDVVPY TFRQDADYLY LTGCQQPGGV AVLSDERGLC
MFMPESTPKD IAWEGEVAGV DAASEVFKAD QAYPISKLPE ILSDMIRHSS KVFHNVQSAS
QRYTNLDDFQ NSASLGKVKT LSSLTHELRL IKSPAELKLM RESASIACQG LLKTMLHSKG
FPDEGILSAQ VEYECRVRGA QRMAFNPVVG GGSNASVIHY SRNDQRIKDG DLVLMDMGCE
LHGYVSDLTR TWPPCGKFSS VQEELYDLIL QTNKECIKQC KPGTTIRQLN TYSTELLCDG
LMKMGILKSR RLYHQLNPTS IGHYLGMDVH DSSAVGYDRP LQPGFVITIE PGVYIPSSFD
CPERFQGIGI RIEDDVLITE TGYEVLTGSM PKEIKHIETL LNNHCHDNSA RTSPVSLCKV
KGLHTNRNPR RLF
