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A3LUT4 (PMIP_PICST) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 47. 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:PICST_89481
OrganismScheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) [Complete proteome]
Taxonomic identifier322104 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeScheffersomyces

Protein attributes

Sequence length812 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 – 2929Mitochondrion Potential
Chain30 – 812783Mitochondrial intermediate peptidase
PRO_0000338593

Sites

Active site5961 By similarity
Metal binding5951Zinc; catalytic By similarity
Metal binding5991Zinc; catalytic By similarity
Metal binding6021Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A3LUT4 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 54B0D82CDCD7BB7B

FASTA81292,517
        10         20         30         40         50         60 
MRLSRQLLRS TPFLTRAKPV SGKVSHFRSR TDLKGGSSNS SKSPDSVGDG ASAHLRHIFD 

        70         80         90        100        110        120 
DQKYFNSFTK SAAETSGKVS SLPAIFSFRR SGLFCNDNLS TPHGLIDFSK NSLREAKSLV 

       130        140        150        160        170        180 
ESMLHDVKSD PAGRLSYINK LDQLSDILCR VIDVAEFIRV AHPSQKWVNA AQQTHEIMFE 

       190        200        210        220        230        240 
YMNQLNTNVE LYQNLRDILS DSSVTAQLTE EEIQVGEYLK QDFERSGIHM NPSARNNFVA 

       250        260        270        280        290        300 
ITQEISLLGS RFNNEIHNLK SYWCEIPRYE FEQLEDSNLK KEILGYQSKA PPSKHSSQTI 

       310        320        330        340        350        360 
SIPLVGHIPF TILTTCSIES IRREIWISLH NSSDEQIATL NNFLKYRATL AKMLGYKSFS 

       370        380        390        400        410        420 
HYQLEHKMAK NPENVVTFLT NLQKSLREKG VTEEIKKLYQ YRDDSTISQV QKASTEDIID 

       430        440        450        460        470        480 
GVKPWDRDYL LEKLQKASNK NLEELENINE YLSVGTIVAG LSELFKSIYN VEFVPVATLK 

       490        500        510        520        530        540 
GETWDQNQVR KVAVVDDSTK KKLGFLYLDF WSPKVLPSHF TIVCSRKLNL DIKSETKDKM 

       550        560        570        580        590        600 
RQLVQLDEDE TSQLPVISLI CNFQKSNDGH IGRFAGVENE KPTLLSLNQV DTVFHEMGHA 

       610        620        630        640        650        660 
MHSMIGRTDL HNLSGTRCAT DFVELPSVLM ESFSKDPRVL CKIAKHYETG EPLSPKLLAQ 

       670        680        690        700        710        720 
HQTQKVMLDE CETYMQSKMA MLDQVLHSED VVRTISEDFA NFDSTPIYHS LESKLKVFAD 

       730        740        750        760        770        780 
TWSTWHGKFP HLFSYGAVYY SYLLDRAIAE KIWNGLFAHD PWSREAGEKY KNSILKWGGT 

       790        800        810 
RDPWECLADA LENDELSKGD SRAMEIIGKD SL 

« Hide

References

[1]"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.
Nat. Biotechnol. 25:319-326(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000499 Genomic DNA. Translation: ABN66647.2.
RefSeqXP_001384676.2. XM_001384639.1.

3D structure databases

ProteinModelPortalA3LUT4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4924.PICST_89481.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4839065.
KEGGpic:PICST_89481.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OMAVTEMNIE.
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_PICST
AccessionPrimary (citable) accession number: A3LUT4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 24, 2007
Last modified: November 13, 2013
This is version 47 of the entry and version 2 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