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Q5RF14

- MIPEP_PONAB

UniProt

Q5RF14 - MIPEP_PONAB

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Protein

Mitochondrial intermediate peptidase

Gene

MIPEP

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Cleaves proteins, imported into the mitochondrion, to their mature size.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

Enzyme regulationi

Activity is divalent cation-dependent. It is stimulated by manganese, magnesium or calcium ions and reversibly inhibited by zinc, cobalt and iron (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi495 – 4951Zinc; catalyticPROSITE-ProRule annotation
Active sitei496 – 4961PROSITE-ProRule annotation
Metal bindingi499 – 4991Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi502 – 5021Zinc; 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

Calcium, Cobalt, Iron, Magnesium, Manganese, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial intermediate peptidase (EC:3.4.24.59)
Short name:
MIP
Gene namesi
Name:MIPEP
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionBy similarityAdd
BLAST
Chaini36 – 713678Mitochondrial intermediate peptidasePRO_0000319049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5RF14.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000230535.
HOVERGENiHBG008215.
InParanoidiQ5RF14.
KOiK01410.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
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.

Q5RF14-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLCVGRLGGL GARAAALPPR RAGRGILEAG IRARRVSTSW SPVGAAFNVK
60 70 80 90 100
PQGSRLDLFG ERRGLFGVPE LSAPEGFHAA QEKALRKAEL LVGRACSTPP
110 120 130 140 150
GPQTVLIFDE LSDSLCRVAD LADFVKIAHP EPAFREAAEE ACRSIGTMVE
160 170 180 190 200
KLNTNVDLYQ SLRKLLADKK LVDSLDPETR RVAELFMFDF EISGIHLDKE
210 220 230 240 250
KRKRAVDLNV KILDLSSTFL MGANFPNKIE KHLLPEHIRR NFTSAGDHII
260 270 280 290 300
IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST
310 320 330 340 350
FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN
360 370 380 390 400
SEVMPWDPPY YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI
410 420 430 440 450
SLYAEQPAKG EVWSEDVRKL AVVHESEGLL GYIYCDFFQR ADKPHQDCHF
460 470 480 490 500
TIRGGRLKED GDYQLPVVVL MLNLPRSSRS SPTLLTPGMM ENLFHEMGHA
510 520 530 540 550
MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV NQFARHYQTG
560 570 580 590 600
QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL
610 620 630 640 650
KETQEKFYGL PYVPDTAWQL RFSHLVGYGA KYYSYLMSRA VASMVWKECF
660 670 680 690 700
LQDPFNRAAG ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD
710
LDLDFETFLM DSE
Length:713
Mass (Da):80,478
Last modified:December 21, 2004 - v1
Checksum:i32FB7C32F5BD1FF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857347 mRNA. Translation: CAH89643.1.
RefSeqiNP_001124737.1. NM_001131265.1.

Genome annotation databases

GeneIDi100171586.
KEGGipon:100171586.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857347 mRNA. Translation: CAH89643.1 .
RefSeqi NP_001124737.1. NM_001131265.1.

3D structure databases

ProteinModelPortali Q5RF14.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100171586.
KEGGi pon:100171586.

Organism-specific databases

CTDi 4285.

Phylogenomic databases

HOGENOMi HOG000230535.
HOVERGENi HBG008215.
InParanoidi Q5RF14.
KOi K01410.

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view ]
Pfami PF01432. Peptidase_M3. 1 hit.
[Graphical view ]
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiMIPEP_PONAB
AccessioniPrimary (citable) accession number: Q5RF14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 21, 2004
Last modified: November 26, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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