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A7TSL2 (PMIP_VANPO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 34. 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:Kpol_297p8
OrganismVanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus) [Complete proteome]
Taxonomic identifier436907 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeVanderwaltozyma

Protein attributes

Sequence length787 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 – 3636Mitochondrion Potential
Chain37 – 787751Mitochondrial intermediate peptidase
PRO_0000338596

Sites

Active site5741 By similarity
Metal binding5731Zinc; catalytic By similarity
Metal binding5771Zinc; catalytic By similarity
Metal binding5801Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A7TSL2 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 478D339F977CF096

FASTA78790,031
        10         20         30         40         50         60 
MQNKVLRGIL FKNVPLGYSY NRSIRHPTFG NSIIRWASTQ VKTSSDVLQR SFDDHLYWTE 

        70         80         90        100        110        120 
INKQNYSSKE GWGSITKRLK GNKLTTNRSG LFNNEYLTSP EGLKLFSQVS LEKSQKIVDK 

       130        140        150        160        170        180 
LRSDRTPEGL RLYVQNLDLL SDTLCRVIDL CEFIRSSHPD YKFVEAAQDC YEEMFEFMNM 

       190        200        210        220        230        240 
LNTDVNLCFT LKHVLENKEI ASKLSEEELR VGRILLEDFE KSGIYMKPEV REQFITLSQS 

       250        260        270        280        290        300 
ISVIGQEFIS NTDFVKDNNV VVSCNQLDSL GIDPELLSQI EKDIAGKNYK IPTYGYIPFA 

       310        320        330        340        350        360 
LLKSCPSEEI REKIWVAVHN CSNEQIKRLT DLVKLRAVLS QLLGKKSYAE YQLEGKMAKN 

       370        380        390        400        410        420 
PKEVIEFIKT LMDFTKPMAA KELDGIAEKK LTIKSNGSNL SVCDILKTVR PWDRDYYSAI 

       430        440        450        460        470        480 
EREQTSAKNL YGSEEVLKYF TLGNVMQGLS NLFQKIYGIK LELDVPKIGE TWSPEVRKIN 

       490        500        510        520        530        540 
VISEDEGLIG IIYCDLFERS GKTSNAAHFT ICCSRDISPY ETEDSTTQIA IDSKGTRFQL 

       550        560        570        580        590        600 
PIISLVCNFS KTMISETDSV CFLHLPEVET LFHEMGHAMH SMLGRTKLQN ISGTRCATDF 

       610        620        630        640        650        660 
VELPSILMEY FARDPRVLET IGKHYLTKET VKREMLEPHL QDLKYLQHCE TYSQAKMAML 

       670        680        690        700        710        720 
DQTLHGETIS SHLDHLDVVK LYQDLERQLG VLVDDKSNWC GKFGHLFGYS AVYYSYLFDR 

       730        740        750        760        770        780 
AIASKIWGAL FERNPFSRAS GDKYRNSVLQ WGGSRDPWHC IASALDKPEL AKGDDEAIKY 


IGSTNQL 

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References

[1]"Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication."
Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.
Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 22028 / DSM 70294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS480515 Genomic DNA. Translation: EDO14747.1.
RefSeqXP_001642605.1. XM_001642555.1.

3D structure databases

ProteinModelPortalA7TSL2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436907.A7TSL2.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5542774.
KEGGvpo:Kpol_297p8.

Phylogenomic databases

eggNOGCOG0339.
KOK01410.
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_VANPO
AccessionPrimary (citable) accession number: A7TSL2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: October 2, 2007
Last modified: November 13, 2013
This is version 34 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