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A8N2T3 (PMIP_COPC7) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 33. 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
ORF Names:CC1G_01835
OrganismCoprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata) [Reference proteome]
Taxonomic identifier240176 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

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)
   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 – 3838Mitochondrion Potential
Chain39 – 776738Mitochondrial intermediate peptidase
PRO_0000338580

Regions

Compositional bias489 – 4924Poly-Asp

Sites

Active site5611 By similarity
Metal binding5601Zinc; catalytic By similarity
Metal binding5641Zinc; catalytic By similarity
Metal binding5671Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A8N2T3 [UniParc].

Last modified March 8, 2011. Version 2.
Checksum: 359633EECC153F99

FASTA77687,377
        10         20         30         40         50         60 
MLNSARTVLA RHSARQLYRF RGCLVHQQRH RHQVQRTLAT HVQRHLPASL DDKALVALFD 

        70         80         90        100        110        120 
QPNGSKLRSP FNTTGLFGHP NLTHPRALVS LAESTLVRAQ LLTQRILEAG KSEHELAKVV 

       130        140        150        160        170        180 
KNLDRLSDML CGVIDLAELV RNAHPDRLWV EAANHAYETL CEFMNVLNTH TGLYEVLKQV 

       190        200        210        220        230        240 
LSNPTLVNSL SPEAYQTALI FWRDFEKSAI DLPPAQRNKF VSLSSDILVL GRQFLENAST 

       250        260        270        280        290        300 
PRPPTSIKAS DLAGLKDKGM GVRLQLQAQF TNRDLQIYPG SLQAHMIMRS APNEEPRRRL 

       310        320        330        340        350        360 
YLAANSSTQE QIEVLEALLK KRAELAQLVG RESFAHMTLD DKMAKTPDNV TNFLDALIDH 

       370        380        390        400        410        420 
TRPFARSALR TLAQRKQAHH GLSSLPIIQA WDRDFYCPPD PPAPPIPLPP LTLGTVFMGL 

       430        440        450        460        470        480 
SRLFRHLYGV SLRPVPSASG EVWHTDVQKL EVVDEDQGII GWIYADLFAR RGKASGAAHY 

       490        500        510        520        530        540 
TVRCSRRTDD DDEQGDGMFE GAELQILESQ EFEAVKRHRL PNQEGVFQLP LVVLLCEFTR 

       550        560        570        580        590        600 
PTVSKGGTIL EWHEVQTLFH EMGHAMHSML GRTEYQNVSG TRCATDFVEL PSILMEHFLN 

       610        620        630        640        650        660 
SPAVLSLFDA DGTSTLRQIG NHHHDPCHAI DTYSQIMLAV VDQIYHSPTV LDPSFDSTRE 

       670        680        690        700        710        720 
YGNLQNTRGL IPYVPGTSYQ TQFGHLFGYG ATYYSYLFDR AIASRVWSKV FSKDPLDREL 

       730        740        750        760        770 
GEKYKREVLR WGGARDPWEM VATLLDAPEL AAGDAEAMRE VGRWRIEDEV GVGGRH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACS02000001 Genomic DNA. Translation: EAU92790.2.
RefSeqXP_001829155.2. XM_001829103.2.

3D structure databases

ProteinModelPortalA8N2T3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6005581.
KEGGcci:CC1G_01835.

Phylogenomic databases

KOK01410.
OrthoDBEOG71GB4R.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 2 hits.
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_COPC7
AccessionPrimary (citable) accession number: A8N2T3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 8, 2011
Last modified: November 13, 2013
This is version 33 of the entry and version 2 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