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Reviewed, UniProtKB/Swiss-Prot A8N2T3 (PMIP_COPC7)

Last modified June 16, 2009. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
ORF Names: CC1G_01835
OrganismCoprinopsis cinerea (strain Okayama-7 / 130 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata)
Taxonomic identifier240176 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaHomobasidiomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

Protein attributes

Sequence length777 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: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion Potential
Chain40 – 777738Mitochondrial intermediate peptidase
PRO_0000338580

Regions

Compositional bias490 – 4934Poly-Asp

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
A8N2T3-1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 1BE83120B6ECF1B2

FASTA77787,437
        10         20         30         40         50         60 
MLSSSARTVL ARHSARQLYR FRGCLVHQQR HRHQVQRTLA THVQRHLPAS LDDKALVALF 

        70         80         90        100        110        120 
DQPNGSKLRS PFNTTGLFGH PNLTHPRALV SLAESTLVRA QLLTQRILEA GKSEHELAKV 

       130        140        150        160        170        180 
VKNLDRLSDM LCGVIDLAEL VRNAHPDRLW VEAANHAYET LCEFMNVLNT HTGLYEVLKQ 

       190        200        210        220        230        240 
VLSNPTLVNS LSPEAYQTAL IFWRDFEKSA IDLPPAQRNK FVSLSSDILV LGRQFLENAS 

       250        260        270        280        290        300 
TPRPPTSIKA SDLAGLKDKG MGVRLQLQAQ FTNRDLQIYP GSLQAHMIMR SAPNEEPRRR 

       310        320        330        340        350        360 
LYLAANSSTQ EQIEVLEALL KKRAELAQLV GRESFAHMTL DDKMAKTPDN VTNFLDALID 

       370        380        390        400        410        420 
HTRPFARSAL RTLAQRKQAH HGLSSLPIIQ AWDRDFYCPP DPPAPPIPLP PLTLGTVFMG 

       430        440        450        460        470        480 
LSRLFRHLYG VSLRPVPSAS GEVWHTDVQK LEVVDEDQGI IGWIYADLFA RRGKASGAAH 

       490        500        510        520        530        540 
YTVRCSRRTD DDDEQGDGMF EGAELQILES QEFEAVKRHR LPNQEGVFQL PLVVLLCEFT 

       550        560        570        580        590        600 
RPTVSKGGTI LEWHEVQTLF HEMGHAMHSM LGRTEYQNVS GTRCATDFVE LPSILMEHFL 

       610        620        630        640        650        660 
NSPAVLSLFD ADGTSTLRQI GNHHHDPCHA IDTYSQIMLA VVDQIYHSPT VLDPSFDSTR 

       670        680        690        700        710        720 
EYGNLQNTRG LIPYVPGTSY QTQFGHLFGY GATYYSYLFD RAIASRVWSK VFSKDPLDRE 

       730        740        750        760        770 
LGEKYKREVL RWGGARDPWE MVATLLDAPE LAAGDAEAMR EVGRWRIEDE VGVGGRH 

« Hide

References

Cross-references

Sequence databases

AACS01000026 Genomic DNA. Translation: EAU92790.1.
RefSeqXP_001829155.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM03.006.

Genome annotation databases

GeneID6005581.

Family and domain databases

InterProIPR001567. Pept_M3A_M3B.
IPR006025. Pept_M_Zn_BS.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP_COPC7
AccessionPrimary (citable) accession number: A8N2T3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 15, 2008
Last modified: June 16, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents