PMIP_VANPO
ID PMIP_VANPO Reviewed; 787 AA.
AC A7TSL2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Kpol_297p8;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480515; EDO14747.1; -; Genomic_DNA.
DR RefSeq; XP_001642605.1; XM_001642555.1.
DR AlphaFoldDB; A7TSL2; -.
DR SMR; A7TSL2; -.
DR STRING; 436907.A7TSL2; -.
DR MEROPS; M03.006; -.
DR PRIDE; A7TSL2; -.
DR EnsemblFungi; EDO14747; EDO14747; Kpol_297p8.
DR GeneID; 5542774; -.
DR KEGG; vpo:Kpol_297p8; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; A7TSL2; -.
DR OMA; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
DR PhylomeDB; A7TSL2; -.
DR Proteomes; UP000000267; 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; 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..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..787
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338596"
FT ACT_SITE 574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 787 AA; 90031 MW; 478D339F977CF096 CRC64;
MQNKVLRGIL FKNVPLGYSY NRSIRHPTFG NSIIRWASTQ VKTSSDVLQR SFDDHLYWTE
INKQNYSSKE GWGSITKRLK GNKLTTNRSG LFNNEYLTSP EGLKLFSQVS LEKSQKIVDK
LRSDRTPEGL RLYVQNLDLL SDTLCRVIDL CEFIRSSHPD YKFVEAAQDC YEEMFEFMNM
LNTDVNLCFT LKHVLENKEI ASKLSEEELR VGRILLEDFE KSGIYMKPEV REQFITLSQS
ISVIGQEFIS NTDFVKDNNV VVSCNQLDSL GIDPELLSQI EKDIAGKNYK IPTYGYIPFA
LLKSCPSEEI REKIWVAVHN CSNEQIKRLT DLVKLRAVLS QLLGKKSYAE YQLEGKMAKN
PKEVIEFIKT LMDFTKPMAA KELDGIAEKK LTIKSNGSNL SVCDILKTVR PWDRDYYSAI
EREQTSAKNL YGSEEVLKYF TLGNVMQGLS NLFQKIYGIK LELDVPKIGE TWSPEVRKIN
VISEDEGLIG IIYCDLFERS GKTSNAAHFT ICCSRDISPY ETEDSTTQIA IDSKGTRFQL
PIISLVCNFS KTMISETDSV CFLHLPEVET LFHEMGHAMH SMLGRTKLQN ISGTRCATDF
VELPSILMEY FARDPRVLET IGKHYLTKET VKREMLEPHL QDLKYLQHCE TYSQAKMAML
DQTLHGETIS SHLDHLDVVK LYQDLERQLG VLVDDKSNWC GKFGHLFGYS AVYYSYLFDR
AIASKIWGAL FERNPFSRAS GDKYRNSVLQ WGGSRDPWHC IASALDKPEL AKGDDEAIKY
IGSTNQL