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Q59RK9 (PMIP_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:CaO19.1195, CaO19.8786
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length783 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 – 3333Mitochondrion Potential
Chain34 – 783750Mitochondrial intermediate peptidase
PRO_0000338576

Regions

Compositional bias27 – 315Poly-Thr

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
Q59RK9 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 88739AB0D0DA1928

FASTA78389,368
        10         20         30         40         50         60 
MKAGIPLSRC TQRLPLLVAR QVSRNITTTT TKFSLAPEYN HIRKVFDSQK YFNHFTKQGS 

        70         80         90        100        110        120 
HATLFSSPQT GLFHNEYLTT PQGLVDFSQQ SLSQAKQLVS EMLSQVNTVD GKLKFIKKLD 

       130        140        150        160        170        180 
QLSDILCRVI DVAEFIRVVH PSVKWINAAQ QTHEMMFEFM NQLNTNVELY SSLRDILNNP 

       190        200        210        220        230        240 
LITEQLTPEE IKVGEYLRQD FERSGIHMDP QTRENFVTIT QEISLLGSQF GNQINGLKSY 

       250        260        270        280        290        300 
WCPVTVTEWE SIEDPQLKKE IKNYQSKYDG IRQPETIQIP LVANIPYTIL TNCSSDTLRK 

       310        320        330        340        350        360 
KVWVALHNSP DEQIETLNRF ISYRALLSKM LNYKSFADYQ LEHKMAKTPE NVITFLSNLQ 

       370        380        390        400        410        420 
KSLIKKGVVE ELSQLSEIKH NGSGSASVND IVNDIKPWDR DYLLARLQQR MQSEVSAGNV 

       430        440        450        460        470        480 
KEYFSVGTVI AGLNELFTRL YDISFVPMAA LKGETWDSHQ VRKIKVVDNA ANKTLGFLYL 

       490        500        510        520        530        540 
DFWSTKVLPS HFTIVCSRRL NTSIGSETIE GMEKLVQLDE DYQLPVVSLV CNFASSGNFS 

       550        560        570        580        590        600 
FGRFAGVENE KPTLLTLDQV DTIFHEMGHA MHSMIGRTEL HNLSGTRCST DFVELPSVLM 

       610        620        630        640        650        660 
ESFSKDPRVI CQIGRHFDTD EKLPESLLGQ AHEHRIMLDA CETFMQSKMA MLDQKLHNEE 

       670        680        690        700        710        720 
MVNLLAKGLY EVDSTKVYHS VEKELKVFAD EWSTWHGKFP HLFSYGAVYY SYLLDRAIAD 

       730        740        750        760        770        780 
KIWQGLFAKD PWNGEAGKKY KESVLKWGGT RDPWECLADA LGNDELKQGD SRAMEIIGQN 


SNL 

« Hide

References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000161 Genomic DNA. Translation: EAK93122.1.
AACQ01000157 Genomic DNA. Translation: EAK93273.1.
RefSeqXP_712312.1. XM_707219.1.
XP_712456.1. XM_707363.1.

3D structure databases

ProteinModelPortalQ59RK9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0002161.

Protein family/group databases

MEROPSM03.006.

Proteomic databases

PRIDEQ59RK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3645934.
3646074.
KEGGcal:CaO19.1195.
cal:CaO19.8786.

Phylogenomic databases

eggNOGCOG0339.
KOK01410.
OrthoDBEOG71GB4R.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
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_CANAL
AccessionPrimary (citable) accession number: Q59RK9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: April 26, 2005
Last modified: November 13, 2013
This is version 58 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

Candida albicans

Candida albicans: entries and gene names