PMIP_SCHCO
ID PMIP_SCHCO Reviewed; 775 AA.
AC P37932;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 115.
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; Synonyms=MEP, MIP;
OS Schizophyllum commune (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=5334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=1-71;
RX PubMed=7490080; DOI=10.1006/geno.1995.1174;
RA Isaya G., Sakati W.R., Rollins R.A., Shen G.P., Hanson L.C., Ullrich R.C.,
RA Novotny C.P.;
RT "Mammalian mitochondrial intermediate peptidase: structure/function
RT analysis of a new homologue from Schizophyllum commune and relationship to
RT thimet oligopeptidases.";
RL Genomics 28:450-461(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-775.
RC STRAIN=ATCC 44201 / CBS 340.81 / UVM 4-40 / 4-40, UVM 9-1, and UVM 9-4;
RX PubMed=1353886; DOI=10.1073/pnas.89.15.7169;
RA Stankis M.M., Specht C.A., Yang H., Giasson L., Ullrich R.C., Novotny C.P.;
RT "The A alpha mating locus of Schizophyllum commune encodes two dissimilar
RT multiallelic homeodomain proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7169-7173(1992).
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
CC {ECO:0000269|PubMed:7490080}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB01366.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L43072; AAA93531.1; -; Genomic_DNA.
DR EMBL; M97179; AAB01366.1; ALT_INIT; Genomic_DNA.
DR EMBL; M97180; AAB01368.1; -; Genomic_DNA.
DR EMBL; M97181; AAB01371.1; -; Genomic_DNA.
DR PIR; E37271; E37271.
DR PIR; F37271; F37271.
DR AlphaFoldDB; P37932; -.
DR SMR; P37932; -.
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; -; 2.
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 Transit peptide; Zinc.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..775
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000028581"
FT ACT_SITE 559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 558
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT VARIANT 572
FT /note="E -> G (in strain: UVM 9-4)"
FT VARIANT 651
FT /note="Q -> E (in strain: UVM 9-1 and CBS 340.81 / UVM 4-
FT 40)"
FT VARIANT 659
FT /note="K -> E (in strain: UVM 9-1 and CBS 340.81 / UVM 4-
FT 40)"
FT VARIANT 729
FT /note="R -> Q (in strain: UVM 9-1)"
FT CONFLICT 486
FT /note="T -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..622
FT /note="HD -> QH (in Ref. 2; AAB01366/AAB01368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 86915 MW; 875772B6D9560C55 CRC64;
MIARPARDVL SSATKKQFRF RGCLAARHEP YHTSTSRAGQ VAILPATTDD KTLVSVFDSP
RSNAKLSAFA TTGLFNHSTV THPRALNSIA QGTLIRAHVL TNRILRAKES REELFKVVKN
LDRLSDMLCS VIDLCELVRN SHPDRAWVEA ANDAYEGLCQ TMNELNTHVG LYDVLKIVLS
DPEIVKSLSP EAYRTAMIFW NDFEKSAINL PAKEREEFVA LSSEIISLGR MFLEETTAAR
PPAKIPPSDL AGLKDKGMGV RLQLQAQFTQ RDLHVYPGSL QAQMIMRSAP AEEARRRVYI
ASHSSTPEQI ELLERMLSTR ARLARLVGRE SFAAMALDDK MAKNPTNVAR FLDSLMDRSR
PYARRALRNL SMRKQEHLHT PPFPTIQAWD RDYYCPPEPP APPIPLPRLT FGTVLMGLSR
LFRHLYGIHL RPVKPIAGEV WHSDVHKLEV VDEERGVIGL IYADVFARRG KASGAAHYTV
RCSRRTDDDD VQGDNDELTR MYPDLIKQSE EFEAVGRGPI PGLPGTYQQP LVVLLCEFAR
PSLGAAVLEW HEVMTLFHEM GHAMHSMIGR TEYQNVSGTR CPTDFVELPS ILMEHFLNSR
QVLSLFHADS TSSSSQPIGN HDEDPCHSID TYAQIMLAAL DQIYHSPAAL QPGFDSTRKL
ARLHDEKGLI PYVPGTSFQT QFGHLFGYGA TYYSYLFDRA IASRVWKDVF SSSPLSRETG
ERYKQEVLRY GGGKDPWEMV SALLKAPELA SGDAEAMATV GRWKIEDEVG LPGRH
