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Q2HFL8 (PMIP_CHAGB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 41. 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:CHGG_00986
OrganismChaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus) [Complete proteome]
Taxonomic identifier306901 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeChaetomium

Protein attributes

Sequence length778 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
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 – 3737Mitochondrion Potential
Chain38 – 778741Mitochondrial intermediate peptidase
PRO_0000338578

Sites

Active site5581 By similarity
Metal binding5571Zinc; catalytic By similarity
Metal binding5611Zinc; catalytic By similarity
Metal binding5641Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2HFL8 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 77933C763AF2F3D9

FASTA77887,685
        10         20         30         40         50         60 
MIRTVTRPRQ WQRWVYSSCL LQRAVPPAAA RQQPRFTTSH KANHFGYHQP IAPVTHAPIT 

        70         80         90        100        110        120 
REDDFVLRSV FDYPQFWQDF TSVPGGIPVG LFRNSFLKEP RGMLTFAYVS LKKARAVVAK 

       130        140        150        160        170        180 
VLAASSVTEY RLIVRDLDRL SDILCRVLDM ADFVRVTHPD PEIQQNASKA WESVYEYMNE 

       190        200        210        220        230        240 
LNTMTGLHDQ LATAMANPDV TVVWSEEEKT VAEVLKLDFT KSAVSLPQKY RDRFVQLSSE 

       250        260        270        280        290        300 
ISAVGSAFVQ EMAPEQETVV LPSSDLRGMD PVRARDLTRR GKVYLPTLSG EAVMALRTVH 

       310        320        330        340        350        360 
DADARKHIFY ASRTASRRSV QMLEYLMRLR SELASLSGFE SYGHLALRDR MMAKSPEAVD 

       370        380        390        400        410        420 
QFLRALVESN RPKAMQEMAE LLAEKQKAYP QTNSLDPWDK DYYSDIIRRP LRVAGRQGDL 

       430        440        450        460        470        480 
LSSYFSLGVP LVGETWHPDV RRLDVVSDTD GHVAVLYCDL FTRPNKSPNP AHFTLRCSRE 

       490        500        510        520        530        540 
IFASEMEEVW EQTQQSNQKS MFGSPELAAT DGMTFSRHGD SIKQLPTIAL VCDFPQPSKH 

       550        560        570        580        590        600 
GDQPALLSFL QLETLFHEMG HAIHSVLART SFQTVAGTRC ATDLAELPST LMEFFAADAA 

       610        620        630        640        650        660 
VLGQFARHHE TNEPLPYRMV AQKARQTRRF EALDTENQIV TAMFDQALHS PRAGEPGFDP 

       670        680        690        700        710        720 
TAIFHALQRT HSCAPPDPPG TSWPGFFGHL SGYGSVYYSY LFDRVLAQRV WDVVFKAGER 

       730        740        750        760        770 
RAALSRENGE KLKQSLLKWG GARDPWKCLA EALDDDRLAE GGEEAMALVG SWGSTKPR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH408029 Genomic DNA. Translation: EAQ92751.1.
RefSeqXP_001220207.1. XM_001220206.1.

3D structure databases

ProteinModelPortalQ2HFL8.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4386396.

Phylogenomic databases

OrthoDBEOG71GB4R.

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_CHAGB
AccessionPrimary (citable) accession number: Q2HFL8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 21, 2006
Last modified: November 13, 2013
This is version 41 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