ID   PMIP1_CRYNB             Reviewed;         761 AA.
AC   P0CQ19; Q55VY2; Q5KKA9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Mitochondrial intermediate peptidase 1;
DE            Short=MIP 1;
DE            EC=3.4.24.59;
DE   AltName: Full=Octapeptidyl aminopeptidase 1;
DE   Flags: Precursor;
GN   Name=OCT1; OrderedLocusNames=CNBC3550;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
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}.
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DR   EMBL; AAEY01000013; EAL22217.1; -; Genomic_DNA.
DR   RefSeq; XP_776864.1; XM_771771.1.
DR   AlphaFoldDB; P0CQ19; -.
DR   SMR; P0CQ19; -.
DR   GeneID; 4935020; -.
DR   KEGG; cnb:CNBC3550; -.
DR   VEuPathDB; FungiDB:CNBC3550; -.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   OrthoDB; 735202at2759; -.
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   CDD; cd06457; M3A_MIP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR033851; M3A_MIP.
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:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..761
FT                   /note="Mitochondrial intermediate peptidase 1"
FT                   /id="PRO_0000410219"
FT   ACT_SITE        531
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         530
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         534
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         537
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   761 AA;  83271 MW;  8AAD7126975FB945 CRC64;
     MLRLPRITRR ALSSGALAPH FDRPLPPPPP APPAPLCALP PLTAPDALAP LTRRTVRHAD
     ALVARIAAAP AHPDPAELRR VVKNLDRLSD VLCGVIDMCE LVRNVHPDPH WVAAAEKTYE
     TLCSFMNQLN TSTGLYDALV ATVSHTFPGN PLSPAELRVA QTFLSDFERS GIQLPPGVRA
     KFVRHSDNIL SLGRTFLSFA AAGPSADTPI EIPEPEVLLA GLSSKFVASL PRKKRKGPAL
     LAPGSWEAQM IGRYADNEEA RRLVYIGSMR EDKDRVYVLE TMLKERAELA HVLGKETWAD
     VALSDKMAKT PQNVLQFLTS LATHHRPSAA ADVAALQRLK ALSTVSRTSS QLPTVHAWDR
     DHYAEQYAAS LLPNGSLPSI TPYFSVGTAM SGLSHMLSRL YGISFKPVSV AHGEVWHPSV
     RRLDVMDEHG KRIGVIYCDL FSRPGKPSAG AAHYTVRCSR RVDDDPSEGD GLPPGWDQHL
     GKGMEVQGEA LHGKEGKYQL PIVVLTTDFG TVEESGPALL GWNDLETLFH EMGHAIHSMI
     GQTEFHNVSG TRCATDFVEL PSILMEHFIS SPAVLSTFAT HYTTNEPLPI PLIQAHLQLD
     QSLKALETHS QILMALLDQK YHSIKHGEQL DSTRVWNELQ SQVGVIPPVR GTAWQTQFGH
     LYGYGATYYS YLFDRAIAGK IWSSLFARGR TGPAAANHDP AAAEDILSRE GGEAFKEKVL
     KWGGGRDPWE MVGDVIGGAE GEQVAKGDEK AMELVGRWMI K
//