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Protein

Mitochondrial intermediate peptidase

Gene

OCT1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi565 – 5651Zinc; catalyticPROSITE-ProRule annotation
Active sitei566 – 5661PROSITE-ProRule annotation
Metal bindingi569 – 5691Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi572 – 5721Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial intermediate peptidase (EC:3.4.24.59)
Short name:
MIP
Alternative name(s):
Octapeptidyl aminopeptidase
Gene namesi
Name:OCT1
Ordered Locus Names:KLLA0B12397g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598 Componenti: Chromosome B

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
BLAST
Chaini28 – 779752Mitochondrial intermediate peptidasePRO_0000338584Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi28985.Q6CVF7.

Structurei

3D structure databases

ProteinModelPortaliQ6CVF7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000076521.
InParanoidiQ6CVF7.
KOiK01410.
OMAiIIIDGLH.
OrthoDBiEOG71GB4R.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6CVF7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRTVSVGRQ YVQRYFGHCL IVNSVRHSSS ATVNRLKQPL RRVFDDDSHW
60 70 80 90 100
RALNHSNYKL NESKGRKFGL RSTSDLETGL FQNSYLKSAN GLVEFTQHSF
110 120 130 140 150
EKAKELVQKI HSIETQDEMK YYIKDLDQLS DVLCRVIDLC EFIRATHPDK
160 170 180 190 200
KFVQTAQQCH EKMFEIMNIL NTDVRLCDLL TQCLRESDVL GLDSEEIRTG
210 220 230 240 250
KILLEDFEKS GIYMKPEIRE KFIQLSQEIS VIGQDFINNT EYVRSNYIKI
260 270 280 290 300
SCELMDAHVN KMVCSQMKKD ITGEYYKVPT YGYIPHTLLR TCSDEVIRMK
310 320 330 340 350
IWTEMHSCSD AQIERLTKLI SLRVELAKLL GSQNFAQYQL HGKMAKTPEN
360 370 380 390 400
VSGFLESLVH STRIKAASEL KPLAVLKSEL TGTQTPHTSE EVLELMKPWD
410 420 430 440 450
RDYYGSIQAL AQRRSSSLDN GESISSSFSL GVVMQGLSDL FEKIYGIKLV
460 470 480 490 500
PATPKTGETW SPDVRRIDVV DEHDGLIGVM YCDLFEREGK TPNPAHFTVC
510 520 530 540 550
CSRNMYLNEA DTSTIQVGVN SNGQKFQLPV ISLVCDFRWV EVNMGDGKHQ
560 570 580 590 600
QMCLLQLNEI ETLFHEMGHA MHSMLGRTQL QNVSGTRCAT DFVELPSILM
610 620 630 640 650
EHFARDTRVL SSISSHYKTG KSLDVEVLKN HQLENQFLQN CETFSQIKMS
660 670 680 690 700
FLDQELHNLD HTTDGSIDVI AIYHRLERRL AVLPDDQSNW CGKFGHLFGY
710 720 730 740 750
GASYYSYLFD RAIASKIWDH LFEQDPFNRT NGTKFKEGLL QWGGSRDPWY
760 770
LLSQVLDEPR LAKGDEWGMR YIGDVKTGM
Length:779
Mass (Da):89,380
Last modified:August 15, 2004 - v1
Checksum:iE25823250E5683BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382122 Genomic DNA. Translation: CAH02475.1.
RefSeqiXP_452082.1. XM_452082.1.

Genome annotation databases

GeneIDi2897324.
KEGGikla:KLLA0B12397g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382122 Genomic DNA. Translation: CAH02475.1.
RefSeqiXP_452082.1. XM_452082.1.

3D structure databases

ProteinModelPortaliQ6CVF7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi28985.Q6CVF7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2897324.
KEGGikla:KLLA0B12397g.

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000076521.
InParanoidiQ6CVF7.
KOiK01410.
OMAiIIIDGLH.
OrthoDBiEOG71GB4R.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMIP_KLULA
AccessioniPrimary (citable) accession number: Q6CVF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 9, 2008
Last sequence update: August 15, 2004
Last modified: January 6, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.