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Q6CHD6 (PMIP_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial intermediate peptidase

Short name=MIP
EC=3.4.24.59
Alternative name(s):
Octapeptidyl aminopeptidase
Gene names
Name:OCT1
Ordered Locus Names:YALI0A09988g
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia

Protein attributes

Sequence length776 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 1 zinc ion By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 776748Mitochondrial intermediate peptidase
PRO_0000338597

Sites

Active site5621 By similarity
Metal binding5611Zinc; catalytic By similarity
Metal binding5651Zinc; catalytic By similarity
Metal binding5681Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CHD6 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 60F6B023BA9AEF67

FASTA77687,572
        10         20         30         40         50         60 
MRRFSTLSRR LQRVVPASSA STANTSPSPA LYTGLEPKIK ESQDSLIRAV FDNGDVWQDF 

        70         80         90        100        110        120 
SQKSVAKPKQ SRSITGFINY LTNESDYETG LFMNDFLKTP AGFQKYTAAS IEEAGQLIQQ 

       130        140        150        160        170        180 
LLGALTQRDK LRHAITTFDR LSDVLCQVID LAEFIRAAHP EQHFVQAAQE AHEQMYEYMN 

       190        200        210        220        230        240 
VLNTSVELYT VLDMVFKDSE IVNQLTHEEK VVGTLLLEDF KKSGVTLDDA GRENFVSLTT 

       250        260        270        280        290        300 
KISLLGRDFI SSNHPKEDYI TLTQGEAQGL DPQLAQQLSQ GNSVYVPTGG VPGQLALRGM 

       310        320        330        340        350        360 
KNENSRKLLW SKMRESSDKS IESLEDLLVS RLELANLMGK ESYADYLLSD KMAGNPENVM 

       370        380        390        400        410        420 
RFLNGLLDKT LPGAKKELSV LEQIKKQATG NPKSILQAWD KSYYASQLLY QKRNKTKTAH 

       430        440        450        460        470        480 
MLSEYFSVGT VVQGLSRIFD KIYGIRFVPT ETKTGETWHH DVRRLDVVSE TEGLIGIMYA 

       490        500        510        520        530        540 
DLFQREGKSP NPAHFTVRCS REIYPDELAH MSSSPIAKVP TLNLNGKVFQ IPTIALICDF 

       550        560        570        580        590        600 
TTPHDLYPSL LSYQEVETLF HEMGHAIHSM LGRTSLHNVC GTRCATDFVE LPSVFMENFA 

       610        620        630        640        650        660 
SNPESLALFA RHYSSDSPLP YQQLERHLNE QSYFKDVEQY TQIKMAMLDQ VLHGNILKSI 

       670        680        690        700        710        720 
TNGHFNSQKL YDNLEKDRPL FPPSPSSWHG SFGHLFGYGA SYYCYLLDRQ MADIVWKKLF 

       730        740        750        760        770 
SKNPLSRDAG SRMKNEVLQW GGSRDPWECI AGVLEDPELA KGGSQAMEKI GNYDKH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382127 Genomic DNA. Translation: CAG83853.1.
RefSeqXP_499926.1. XM_499926.1.

3D structure databases

ProteinModelPortalQ6CHD6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4952.Q6CHD6.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCAG83853; CAG83853; YALI0_A09988g.
GeneID2905768.
KEGGyli:YALI0A09988g.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OMALQVFYSA.
OrthoDBEOG71GB4R.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP_YARLI
AccessionPrimary (citable) accession number: Q6CHD6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: August 16, 2004
Last modified: May 14, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries