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Q6CVF7 (PMIP_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. 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:KLLA0B12397g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length779 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 – 2727Mitochondrion Potential
Chain28 – 779752Mitochondrial intermediate peptidase
PRO_0000338584

Sites

Active site5661 By similarity
Metal binding5651Zinc; catalytic By similarity
Metal binding5691Zinc; catalytic By similarity
Metal binding5721Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CVF7 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: E25823250E5683BF

FASTA77989,380
        10         20         30         40         50         60 
MLRTVSVGRQ YVQRYFGHCL IVNSVRHSSS ATVNRLKQPL RRVFDDDSHW RALNHSNYKL 

        70         80         90        100        110        120 
NESKGRKFGL RSTSDLETGL FQNSYLKSAN GLVEFTQHSF EKAKELVQKI HSIETQDEMK 

       130        140        150        160        170        180 
YYIKDLDQLS DVLCRVIDLC EFIRATHPDK KFVQTAQQCH EKMFEIMNIL NTDVRLCDLL 

       190        200        210        220        230        240 
TQCLRESDVL GLDSEEIRTG KILLEDFEKS GIYMKPEIRE KFIQLSQEIS VIGQDFINNT 

       250        260        270        280        290        300 
EYVRSNYIKI SCELMDAHVN KMVCSQMKKD ITGEYYKVPT YGYIPHTLLR TCSDEVIRMK 

       310        320        330        340        350        360 
IWTEMHSCSD AQIERLTKLI SLRVELAKLL GSQNFAQYQL HGKMAKTPEN VSGFLESLVH 

       370        380        390        400        410        420 
STRIKAASEL KPLAVLKSEL TGTQTPHTSE EVLELMKPWD RDYYGSIQAL AQRRSSSLDN 

       430        440        450        460        470        480 
GESISSSFSL GVVMQGLSDL FEKIYGIKLV PATPKTGETW SPDVRRIDVV DEHDGLIGVM 

       490        500        510        520        530        540 
YCDLFEREGK TPNPAHFTVC CSRNMYLNEA DTSTIQVGVN SNGQKFQLPV ISLVCDFRWV 

       550        560        570        580        590        600 
EVNMGDGKHQ QMCLLQLNEI ETLFHEMGHA MHSMLGRTQL QNVSGTRCAT DFVELPSILM 

       610        620        630        640        650        660 
EHFARDTRVL SSISSHYKTG KSLDVEVLKN HQLENQFLQN CETFSQIKMS FLDQELHNLD 

       670        680        690        700        710        720 
HTTDGSIDVI AIYHRLERRL AVLPDDQSNW CGKFGHLFGY GASYYSYLFD RAIASKIWDH 

       730        740        750        760        770 
LFEQDPFNRT NGTKFKEGLL QWGGSRDPWY LLSQVLDEPR LAKGDEWGMR YIGDVKTGM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382122 Genomic DNA. Translation: CAH02475.1.
RefSeqXP_452082.1. XM_452082.1.

3D structure databases

ProteinModelPortalQ6CVF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.Q6CVF7.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2897324.
KEGGkla:KLLA0B12397g.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OMALQVFYSA.
OrthoDBEOG71GB4R.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
3.40.390.10. 1 hit.
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_KLULA
AccessionPrimary (citable) accession number: Q6CVF7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: August 16, 2004
Last modified: November 13, 2013
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