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Q6FW88 (PMIP_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. 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:CAGL0D02112g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length761 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)
   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 – 761724Mitochondrial intermediate peptidase
PRO_0000338577

Sites

Active site5481 By similarity
Metal binding5471Zinc; catalytic By similarity
Metal binding5511Zinc; catalytic By similarity
Metal binding5541Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FW88 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 89CA8567A26EC72E

FASTA76187,333
        10         20         30         40         50         60 
MLIQKILLNK EISRLPRILS ILNYTGLRWL SGSSGRNTTE LQRIFDDSKY WQSLSENTTQ 

        70         80         90        100        110        120 
YTKETGLFKN PYLTSTDGLR QFSHDSLHKA HKLAEILRNS VSKEEKVHYI MNLDQLSDTL 

       130        140        150        160        170        180 
CRVIDLCEFL RSAHPDQSYV EAAQMCHEEM FEFMNVLNTD VVLCNKLKEV LEDPEILKVL 

       190        200        210        220        230        240 
SEEERKVGEI LLDDFEKSGI YMKAGIREQF IELSQQISVI GQEFINNTDY VAKEFIKVKR 

       250        260        270        280        290        300 
DEMDKSGISP LLTARLNRDL TGKYYKIPTY GQIPLQILKS CPDEDIRKEV WAALHNCPKA 

       310        320        330        340        350        360 
QIQRLNQLVR LRVILSNLLG KQSYSDYQLD NKMAGSPENV KGFIKTLMNV TKPLAARELE 

       370        380        390        400        410        420 
FIARDKLNAP DSRHMSDNEI LSIVKPWDKN YFSSKYDSDN EMAMIRDEQL RYYFSLGNVI 

       430        440        450        460        470        480 
NGLSELFKRI YGITLQPSRT ENGETWSPDV RRLDVISEEE GLVGVIYCDL FERVGKISNP 

       490        500        510        520        530        540 
AHFTVCCSRQ VYPDENDFTT IQTGQNSDGT VFQLPVISLV CNFSTVALPN GNRTCFLHMN 

       550        560        570        580        590        600 
EIETLFHEMG HAMHSMLGRT RLQNISGTRC ATDFVELPSI LMEHFARDIR VLRTIGSHYE 

       610        620        630        640        650        660 
TSEPAPEALL NDYLDKTQFL QHCETYSQAK MAMLDQKLHG SFSLSDIERI DSAKIYQKLE 

       670        680        690        700        710        720 
TRLQVLADDE SNWCGRFGHL FGYGATYYSY LFDRAIASKV WDSLFKDDPF NRTGGEKFKE 

       730        740        750        760 
RVLKWGGLKN PWSCIADVLE KPDLAKGGAE AMTYIGDSED L 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR380950 Genomic DNA. Translation: CAG58417.1.
RefSeqXP_445506.1. XM_445506.1.

3D structure databases

ProteinModelPortalQ6FW88.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2887167.
KEGGcgr:CAGL0D02112g.

Phylogenomic databases

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_CANGA
AccessionPrimary (citable) accession number: Q6FW88
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 19, 2004
Last modified: May 14, 2014
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