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Q6VMB4 (PMIP_LEUGO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 38. 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
Synonyms:MIP
OrganismLeucoagaricus gongylophorus (Leaf-cutting ant fungus)
Taxonomic identifier79220 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeLeucoagaricus

Protein attributes

Sequence length760 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
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 1919Mitochondrion Potential
Chain20 – 760741Mitochondrial intermediate peptidase
PRO_0000343202

Sites

Active site5441 By similarity
Metal binding5431Zinc; catalytic By similarity
Metal binding5471Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6VMB4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 66EDF1623874E4A1

FASTA76085,580
        10         20         30         40         50         60 
MLARSVRTLV VSPKTVFRFR GCLFEKHVST ASADDRAIVS LFDSPHAAFK YPSTISTGLF 

        70         80         90        100        110        120 
GHSQLSHPNA FISLAEATLV RAQLLTDRIL RARSSRDELL KVVKNLDRLS DMLCSVIDLA 

       130        140        150        160        170        180 
ELIRNAHPDR NWATAGHHVY EQLCEFMNVL NTHVGLYEVL KLVLADASIV KTLSPEAYQT 

       190        200        210        220        230        240 
ALIFWRDFEK SAINLPPEER QKFVSLSSDI LVLGREFLEN ANAPRPPASI KPEHMVGIKD 

       250        260        270        280        290        300 
KGLGVRLQLQ AQFTRRDLLV YPGSLQAQMI MRSAPDEEPR RRMYIAANSS TDQQIXTLER 

       310        320        330        340        350        360 
LLKTRAELAR LVGRSSFAHM TLDDKMAKTP ENVMNFLGAL IGQTRPFARR ALKTLSARKQ 

       370        380        390        400        410        420 
AHHGLSSLPT IQAWDRDFYC PPEPPAPPIP LPPLTLGTIF MGLSRLFKYL YGITLRPTEA 

       430        440        450        460        470        480 
QTGEVWHSDV HKLEVIDEDK GLIGWIYADL FARHGKSSGA AHYTVRCSRR TDLDDDLGDG 

       490        500        510        520        530        540 
GLTGHEELIQ QNLEFEKVKR HKIPNQDGVY QLPLVVLLCE FTRPSVLKGA TVLEWHDVMT 

       550        560        570        580        590        600 
LFHEMGHAML AMVGRTEYQN VSGTRCATDF VELPSILMEH FLSSPVVLSL FDLDGTHSLR 

       610        620        630        640        650        660 
QVGNTHEDPC HSIDTFSQII LASLDQIYHS PAVLDNSTFS TTDELENLTV SKGVIPHVPS 

       670        680        690        700        710        720 
TSFQTQFGHL FGYGATYYSY LFDRAIASRV WKKVFEKDPL KREVGEKYKL EVLRWGGGRD 

       730        740        750        760 
PWKMVSKLLD ASELEKGDAE AMREVGRWRI EDEVGLPGRH 

« Hide

References

[1]"Evolution of the gene encoding mitochondrial intermediate peptidase and its cosegregation with the A mating-type locus of mushroom fungi."
James T.Y., Kuees U., Rehner S.A., Vilgalys R.
Fungal Genet. Biol. 41:381-390(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SAR 000701-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY338827 Genomic DNA. Translation: AAR22310.1.

3D structure databases

ProteinModelPortalQ6VMB4.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
3.40.390.10. 2 hits.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
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_LEUGO
AccessionPrimary (citable) accession number: Q6VMB4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 5, 2004
Last modified: March 6, 2013
This is version 38 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