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A6H611 (MIPEP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:Mipep
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Enzyme regulation

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

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion By similarity
Chain34 – 711678Mitochondrial intermediate peptidase
PRO_0000319045

Sites

Active site4941 By similarity
Metal binding4931Zinc; catalytic By similarity
Metal binding4971Zinc; catalytic By similarity
Metal binding5001Zinc; catalytic By similarity

Amino acid modifications

Modified residue1241N6-acetyllysine By similarity

Experimental info

Sequence conflict611R → RVP in BAE27162. Ref.1
Sequence conflict2861S → N in BAE27162. Ref.1
Sequence conflict4191A → T in BAE27162. Ref.1
Sequence conflict5081Y → H in AAI10359. Ref.2
Sequence conflict5951T → A in BAE27162. Ref.1

Sequences

Sequence LengthMass (Da)Tools
A6H611 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: C22E9FFFB86A7ECB

FASTA71180,852
        10         20         30         40         50         60 
MLLAAGARYA RRLCGRGAAA ALQGRTGRSC ARDVSTSWSP VGAAFNVKPQ SHLWNLLGER 

        70         80         90        100        110        120 
RGLFGVPELS TPEGFQVAQE EALKKTEWLV ERACSTPPGP QTVLIFDELS DCLCRVADLA 

       130        140        150        160        170        180 
DFVKIGHPDP AFREAAQEAC RSIGTMVEKL NTNVELYQSL QRLLGDKKLM ESLDAETRRV 

       190        200        210        220        230        240 
AELFMFDFEI SGIHLDEEKR RRAVDLNVKI LDLSNAFLMR TNFPNKIRKS LLPEHIQHHF 

       250        260        270        280        290        300 
ARDGSHLIID GLHAEASDDL VREAAYKIFL YPNADQLKCL EELLSSRDLL AKLVGYSTFS 

       310        320        330        340        350        360 
HRALQGTIAQ TPETVMQFLE KLSEKLSERT RKDFKMMQGM KTKLNPQNSK LMPWDPPYYS 

       370        380        390        400        410        420 
GVIRAERYNI EPSLYCPFLS LGACMEGLNV LFNKLLGITL YAEQTFKGEV WCNDIRKLAV 

       430        440        450        460        470        480 
VHESEGLLGY IYCDFFQRAN KPQQDCHFTI RGGRLKEDGS YQLPVVVLML NLPHASRDFP 

       490        500        510        520        530        540 
TLLTPGMMEN LFHEMGHAMH SMLGRTRYQH VTGTRCPTDF AEVPSILMEY FSNDYRVVSQ 

       550        560        570        580        590        600 
FAKHYQTGQP LPKAMVSRLC ESKKVCTAAE MQLQVFYAAL DQIYHGQHPL KKSTTDILME 

       610        620        630        640        650        660 
TQEQFYGLPY VPDTAWQLRF SHLVGYGAKY YSYLMSRAVA SMIWKECFLQ DPFNRAAGER 

       670        680        690        700        710 
YRREMLAHGG GKEPMLMIQG MLQKCPSIDD FVDALVSDMN LDFETFFLDS K 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: DBA/2.
[2]"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].
Strain: Czech II and FVB/N.
Tissue: Brain and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK146428 mRNA. Translation: BAE27162.1.
BC049871 mRNA. Translation: AAH49871.1.
BC110358 mRNA. Translation: AAI10359.1.
BC145711 mRNA. Translation: AAI45712.1.
CCDSCCDS49517.1.
RefSeqNP_081712.2. NM_027436.3.
UniGeneMm.274650.
Mm.486410.

3D structure databases

ProteinModelPortalA6H611.
SMRA6H611. Positions 97-692.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.A05.

PTM databases

PhosphoSiteA6H611.

Proteomic databases

MaxQBA6H611.
PaxDbA6H611.
PRIDEA6H611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063562; ENSMUSP00000069840; ENSMUSG00000021993.
GeneID70478.
KEGGmmu:70478.

Organism-specific databases

CTD4285.
MGIMGI:1917728. Mipep.

Phylogenomic databases

eggNOGCOG0339.
GeneTreeENSGT00550000075047.
HOGENOMHOG000230535.
HOVERGENHBG008215.
InParanoidA6H611.
KOK01410.
OMANADLMEC.
OrthoDBEOG7TTQ72.
PhylomeDBA6H611.
TreeFamTF105715.

Gene expression databases

BgeeA6H611.
CleanExMM_MIPEP.
GenevestigatorA6H611.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio331711.
PROA6H611.
SOURCESearch...

Entry information

Entry nameMIPEP_MOUSE
AccessionPrimary (citable) accession number: A6H611
Secondary accession number(s): Q2YD79, Q3UJJ3, Q80VA3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 24, 2007
Last modified: July 9, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot