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
//
