ID   PMIP2_CRYNJ             Reviewed;         823 AA.
AC   P0CQ20; Q55XK7; Q5KMC8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Mitochondrial intermediate peptidase 2;
DE            Short=MIP 2;
DE            EC=3.4.24.59;
DE   AltName: Full=Octapeptidyl aminopeptidase 2;
DE   Flags: Precursor;
GN   Name=OCT2; OrderedLocusNames=CNB02140;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW41837.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017342; AAW41837.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_569144.1; XM_569144.1.
DR   AlphaFoldDB; P0CQ20; -.
DR   SMR; P0CQ20; -.
DR   STRING; 5207.AAW41837; -.
DR   PaxDb; P0CQ20; -.
DR   EnsemblFungi; AAW41837; AAW41837; CNB02140.
DR   GeneID; 3255573; -.
DR   KEGG; cne:CNB02140; -.
DR   VEuPathDB; FungiDB:CNB02140; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   InParanoid; P0CQ20; -.
DR   OrthoDB; 642479at2759; -.
DR   Proteomes; UP000002149; Chromosome 2.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0006627; P:protein processing involved in protein targeting to mitochondrion; 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..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..823
FT                   /note="Mitochondrial intermediate peptidase 2"
FT                   /id="PRO_0000338582"
FT   REGION          532..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        596
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         595
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         599
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         602
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   823 AA;  92172 MW;  4C30FAD763938997 CRC64;
     MRRLQQSLRR RSARRCPFIL IPHRLLTTSY ASYKPAPQAT LEIEDTNSPT FLLKTSPIQL
     PARATSDDSA IKAHFDLPHS IFGDMVGVRR EHVKGLFHYD SLTQPESLMR LTDRTLIQAS
     AIVQRIVVAP QDPTGRELRL VVKNLDRLSD ILCGVIDMCE LIRNVHPHQD WVNQSDRTHQ
     ILCSFMNELN ATRGLYESLA KAIAHPFNDP LTTSELRVAR IFLTDFERSG IHLPPSVRER
     FVKHSDALLF LGRSFLSSAS SGPSTVPHIE IPDPHRLLTG LGRQFVDSLP RTGRNGQAVI
     EPGSWEAQMI LRYAREGRAR ELVYVGGMRA DKKRISVLEA MLKERAELAS VLGKNNWAEV
     VLVDKMTKTP ENVMRFLTSL AQHHQPVARA EVDMLRRMKA TALTGNYFDP RNSRTRHLPL
     FHAWDRDYYS DKYLTSLIPT GSPPSISPYL STGTVMSGLS RIFSRLYGIS FKPAVVSPGE
     VWHPSVRRLD VVHEEEGLIG VIYCDFFSRI GKSSGAAHYT VRCSRRVDDD DIDGDGLPED
     WDKPYGPGLE ADKESLSGKP GKYQLPIIAL SMDVGTVNEG RPALLNWQEL ETLFHEMGHA
     IHSMIGRTEY HNVSGTRCAT DFVELPSILM EHFVSSPEVL STLAFHHATG EPLPIPVIEA
     HLALNQSLSA LETHGQIAMA LLDQKYHTLR HGQDSFDSTA IWFQLQQEIG VIQPVPGTAW
     QMQFGHLYGY GATYYSYLFD RAIAGKIWST LFHRSGTSQA YDRKAEGILS REGGELLKEK
     VLKWGGGRDP WEMVGDVIGG VEGDELSKGD ERALALVGSW SVV