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Protein

Mitochondrial intermediate peptidase

Gene

MIPEP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

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

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: ProtInc

GO - Biological processi

  • protein processing involved in protein targeting to mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

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

Protein family/group databases

MEROPSiM03.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial intermediate peptidase (EC:3.4.24.59)
Short name:
MIP
Gene namesi
Name:MIPEP
Synonyms:MIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:7104. MIPEP.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30822.

Polymorphism and mutation databases

BioMutaiMIPEP.
DMDMi182639267.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionAdd
BLAST
Chaini36 – 713678Mitochondrial intermediate peptidasePRO_0000028579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99797.
PaxDbiQ99797.
PRIDEiQ99797.

PTM databases

PhosphoSiteiQ99797.

Expressioni

Gene expression databases

BgeeiQ99797.
CleanExiHS_MIP.
HS_MIPEP.
GenevisibleiQ99797. HS.

Organism-specific databases

HPAiHPA030676.
HPA031669.
HPA031670.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi110431. 13 interactions.
IntActiQ99797. 4 interactions.
MINTiMINT-2815808.
STRINGi9606.ENSP00000371607.

Structurei

3D structure databases

ProteinModelPortaliQ99797.
SMRiQ99797. Positions 120-694.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000075047.
HOGENOMiHOG000230535.
HOVERGENiHBG008215.
InParanoidiQ99797.
KOiK01410.
OMAiIIIDGLH.
OrthoDBiEOG7TTQ72.
PhylomeDBiQ99797.
TreeFamiTF105715.

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.

Q99797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCVGRLGGL GARAAALPPR RAGRGSLEAG IRARRVSTSW SPVGAAFNVK
60 70 80 90 100
PQGSRLDLFG ERRGLFGVPE LSAPEGFHIA QEKALRKTEL LVDRACSTPP
110 120 130 140 150
GPQTVLIFDE LSDSLCRVAD LADFVKIAHP EPAFREAAEE ACRSIGTMVE
160 170 180 190 200
KLNTNVDLYQ SLQKLLADKK LVDSLDPETR RVAELFMFDF EISGIHLDKE
210 220 230 240 250
KRKRAVDLNV KILDLSSTFL MGTNFPNKIE 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 SPTLLTPSMM 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 PYVPNTAWQL RFSHLVGYGA RYYSYLMSRA VASMVWKECF
660 670 680 690 700
LQDPFNRAAG ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD
710
LDLDFETFLM DSE
Length:713
Mass (Da):80,641
Last modified:February 26, 2008 - v2
Checksum:i9DBB26B74355B9C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 642RG → AR in AAC51231 (PubMed:9073519).Curated
Sequence conflicti200 – 2001E → Q in AAC51231 (PubMed:9073519).Curated
Sequence conflicti348 – 3481P → A in AAC51231 (PubMed:9073519).Curated
Sequence conflicti467 – 4671V → L in AAC51231 (PubMed:9073519).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371A → V.
Corresponds to variant rs2312296 [ dbSNP | Ensembl ].
VAR_038934
Natural varianti340 – 3401R → Q.
Corresponds to variant rs11551114 [ dbSNP | Ensembl ].
VAR_038935
Natural varianti453 – 4531R → H.
Corresponds to variant rs12858248 [ dbSNP | Ensembl ].
VAR_038936
Natural varianti488 – 4881S → G.3 Publications
Corresponds to variant rs7333040 [ dbSNP | Ensembl ].
VAR_038937

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80034 mRNA. Translation: AAC51231.1.
AK291923 mRNA. Translation: BAF84612.1.
AL157368, AL139080, AL445985 Genomic DNA. Translation: CAI15091.1.
AL139080, AL157368, AL445985 Genomic DNA. Translation: CAI39630.1.
AL445985, AL139080, AL157368 Genomic DNA. Translation: CAM20040.1.
BC009934 mRNA. Translation: AAH09934.1.
CCDSiCCDS9303.1.
RefSeqiNP_005923.2. NM_005932.3.
UniGeneiHs.507498.

Genome annotation databases

EnsembliENST00000382172; ENSP00000371607; ENSG00000027001.
GeneIDi4285.
KEGGihsa:4285.
UCSCiuc001uox.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80034 mRNA. Translation: AAC51231.1.
AK291923 mRNA. Translation: BAF84612.1.
AL157368, AL139080, AL445985 Genomic DNA. Translation: CAI15091.1.
AL139080, AL157368, AL445985 Genomic DNA. Translation: CAI39630.1.
AL445985, AL139080, AL157368 Genomic DNA. Translation: CAM20040.1.
BC009934 mRNA. Translation: AAH09934.1.
CCDSiCCDS9303.1.
RefSeqiNP_005923.2. NM_005932.3.
UniGeneiHs.507498.

3D structure databases

ProteinModelPortaliQ99797.
SMRiQ99797. Positions 120-694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110431. 13 interactions.
IntActiQ99797. 4 interactions.
MINTiMINT-2815808.
STRINGi9606.ENSP00000371607.

Protein family/group databases

MEROPSiM03.006.

PTM databases

PhosphoSiteiQ99797.

Polymorphism and mutation databases

BioMutaiMIPEP.
DMDMi182639267.

Proteomic databases

MaxQBiQ99797.
PaxDbiQ99797.
PRIDEiQ99797.

Protocols and materials databases

DNASUi4285.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382172; ENSP00000371607; ENSG00000027001.
GeneIDi4285.
KEGGihsa:4285.
UCSCiuc001uox.4. human.

Organism-specific databases

CTDi4285.
GeneCardsiGC13M024304.
HGNCiHGNC:7104. MIPEP.
HPAiHPA030676.
HPA031669.
HPA031670.
MIMi602241. gene.
neXtProtiNX_Q99797.
PharmGKBiPA30822.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000075047.
HOGENOMiHOG000230535.
HOVERGENiHBG008215.
InParanoidiQ99797.
KOiK01410.
OMAiIIIDGLH.
OrthoDBiEOG7TTQ72.
PhylomeDBiQ99797.
TreeFamiTF105715.

Miscellaneous databases

ChiTaRSiMIPEP. human.
GenomeRNAii4285.
NextBioi16857.
PROiQ99797.
SOURCEiSearch...

Gene expression databases

BgeeiQ99797.
CleanExiHS_MIP.
HS_MIPEP.
GenevisibleiQ99797. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and chromosomal assignment of the human mitochondrial intermediate peptidase gene (MIPEP)."
    Chew A., Buck E.A., Peretz S., Sirugo G., Rinaldo P., Isaya G.
    Genomics 40:493-496(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-488.
    Tissue: Liver.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-488.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-488.
    Tissue: Uterus.
  5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMIPEP_HUMAN
AccessioniPrimary (citable) accession number: Q99797
Secondary accession number(s): Q5JV15, Q5T9Q9, Q96G65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 26, 2008
Last modified: June 24, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. 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.