PMIP_LODEL
ID PMIP_LODEL Reviewed; 811 AA.
AC A5E4V6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Mitochondrial intermediate peptidase;
DE Short=MIP;
DE EC=3.4.24.59;
DE AltName: Full=Octapeptidyl aminopeptidase;
DE Flags: Precursor;
GN Name=OCT1; ORFNames=LELG_04645;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to their
CC mature size. While most mitochondrial precursor proteins are processed
CC to the mature form in one step by mitochondrial processing peptidase
CC (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC processing by MPP is a required step for a subgroup of nuclear-encoded
CC precursor proteins destined for the matrix or the inner membrane (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal octapeptide as second stage of
CC processing of some proteins imported into the mitochondrion.;
CC EC=3.4.24.59;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR EMBL; CH981530; EDK46464.1; -; Genomic_DNA.
DR RefSeq; XP_001523832.1; XM_001523782.1.
DR AlphaFoldDB; A5E4V6; -.
DR SMR; A5E4V6; -.
DR STRING; 379508.A5E4V6; -.
DR EnsemblFungi; EDK46464; EDK46464; LELG_04645.
DR GeneID; 5231285; -.
DR KEGG; lel:LELG_04645; -.
DR VEuPathDB; FungiDB:LELG_04645; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; A5E4V6; -.
DR OMA; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 2.
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..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..811
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338586"
FT REGION 423..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 593
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 597
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 811 AA; 91934 MW; E9995C8F9BF12958 CRC64;
MRSGSRLSNY LVRLSGRVSF TQKRSLTNVK LPSNVNYERL KAAFDSDEHT LNGKNNNNEG
KLFSKTALFQ GQKDGSASTG LFKNSYLTSP QGLVQFSKKS KLQAQTLVDE MTRDVLTHQG
KLDYIKKLDQ LSDILCRTID VAEFIRVVHD DQKWVDAAQQ THEIIFEYMN QLNTNVELYA
NLVKILEDKD LISQLSDEEI KVGEYLRQDF ERSGIHMDPQ SRDQFVSLTQ EISIMGSHFN
NESSSLKSDW ISITSNEFSA IEDRFIQSEV MRASALYPGK KESGTYYIPL ASAIPYRIMI
QCGSGNLRKK MWIGLHEASD EQVQVLNHFV AYRALLAKML GYDSYAHYQL EHKMAKKPEN
VLSFLTNLQE NLKNSQVLKE LRALSALQQG YSLLSDEELI RQIKPWDRDF LLKSFEAKKL
SSTENGEKAS TDTSTSTTTS TTTTDSTTTT ATFSNSTDSV AIKRLCEYFS IGTVIAGLSK
LFSALYNISF VVEPTVKGEV WNEKRVRKLN VLNNSNGETM GYLYLDFCSP KVFPSHFTVV
CLRQLNKAES VSEHGDMVQL SKDYQLPVVA LVCNFTSGNP TLLSLDQVDT IFHEMGHAMH
SMIGRTQLHN LSGTRCATDF VEIPSVLMES FSKDPRVLSE IGCHYRTGEP VPINLLEQAQ
SQRSALEACE TFVQSKMAML DQELHSKEIV ELLRQGLEAI NSTEIYHQVE RDLEIFADEW
STWHGKFPHL FSYGAVYYSY LLDRAIANVL WQKLFAKDPW SRDAGIKYKE EILKWGGTKD
PWACLADALQ MEELRKGDAH AMQIIGENSK L