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Protein

Mitochondrial intermediate peptidase

Gene

OCT1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).By similarity

Catalytic activityi

Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi561 – 5611Zinc; catalyticPROSITE-ProRule annotation
Active sitei562 – 5621PROSITE-ProRule annotation
Metal bindingi565 – 5651Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi568 – 5681Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro

GO - Biological processi

  1. cellular iron ion homeostasis Source: EnsemblFungi
  2. protein processing involved in protein targeting to mitochondrion Source: EnsemblFungi
  3. protein stabilization Source: EnsemblFungi
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial intermediate peptidase (EC:3.4.24.59)
Short name:
MIP
Alternative name(s):
Octapeptidyl aminopeptidase
Gene namesi
Name:OCT1
Ordered Locus Names:YALI0A09988g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
ProteomesiUP000001300 Componenti: Chromosome A

Subcellular locationi

  1. Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionSequence AnalysisAdd
BLAST
Chaini29 – 776748Mitochondrial intermediate peptidasePRO_0000338597Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi4952.Q6CHD6.

Structurei

3D structure databases

ProteinModelPortaliQ6CHD6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000076521.
InParanoidiQ6CHD6.
KOiK01410.
OMAiIIIDGLH.
OrthoDBiEOG71GB4R.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6CHD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRFSTLSRR LQRVVPASSA STANTSPSPA LYTGLEPKIK ESQDSLIRAV
60 70 80 90 100
FDNGDVWQDF SQKSVAKPKQ SRSITGFINY LTNESDYETG LFMNDFLKTP
110 120 130 140 150
AGFQKYTAAS IEEAGQLIQQ LLGALTQRDK LRHAITTFDR LSDVLCQVID
160 170 180 190 200
LAEFIRAAHP EQHFVQAAQE AHEQMYEYMN VLNTSVELYT VLDMVFKDSE
210 220 230 240 250
IVNQLTHEEK VVGTLLLEDF KKSGVTLDDA GRENFVSLTT KISLLGRDFI
260 270 280 290 300
SSNHPKEDYI TLTQGEAQGL DPQLAQQLSQ GNSVYVPTGG VPGQLALRGM
310 320 330 340 350
KNENSRKLLW SKMRESSDKS IESLEDLLVS RLELANLMGK ESYADYLLSD
360 370 380 390 400
KMAGNPENVM RFLNGLLDKT LPGAKKELSV LEQIKKQATG NPKSILQAWD
410 420 430 440 450
KSYYASQLLY QKRNKTKTAH MLSEYFSVGT VVQGLSRIFD KIYGIRFVPT
460 470 480 490 500
ETKTGETWHH DVRRLDVVSE TEGLIGIMYA DLFQREGKSP NPAHFTVRCS
510 520 530 540 550
REIYPDELAH MSSSPIAKVP TLNLNGKVFQ IPTIALICDF TTPHDLYPSL
560 570 580 590 600
LSYQEVETLF HEMGHAIHSM LGRTSLHNVC GTRCATDFVE LPSVFMENFA
610 620 630 640 650
SNPESLALFA RHYSSDSPLP YQQLERHLNE QSYFKDVEQY TQIKMAMLDQ
660 670 680 690 700
VLHGNILKSI TNGHFNSQKL YDNLEKDRPL FPPSPSSWHG SFGHLFGYGA
710 720 730 740 750
SYYCYLLDRQ MADIVWKKLF SKNPLSRDAG SRMKNEVLQW GGSRDPWECI
760 770
AGVLEDPELA KGGSQAMEKI GNYDKH
Length:776
Mass (Da):87,572
Last modified:August 16, 2004 - v1
Checksum:i60F6B023BA9AEF67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382127 Genomic DNA. Translation: CAG83853.1.
RefSeqiXP_499926.1. XM_499926.1.

Genome annotation databases

EnsemblFungiiCAG83853; CAG83853; YALI0_A09988g.
GeneIDi2905768.
KEGGiyli:YALI0A09988g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382127 Genomic DNA. Translation: CAG83853.1.
RefSeqiXP_499926.1. XM_499926.1.

3D structure databases

ProteinModelPortaliQ6CHD6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4952.Q6CHD6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG83853; CAG83853; YALI0_A09988g.
GeneIDi2905768.
KEGGiyli:YALI0A09988g.

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000076521.
InParanoidiQ6CHD6.
KOiK01410.
OMAiIIIDGLH.
OrthoDBiEOG71GB4R.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMIP_YARLI
AccessioniPrimary (citable) accession number: Q6CHD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: August 16, 2004
Last modified: April 1, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.