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A6H611

- MIPEP_MOUSE

UniProt

A6H611 - MIPEP_MOUSE

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Protein

Mitochondrial intermediate peptidase

Gene

Mipep

Organism
Mus musculus (Mouse)
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 bindingi493 – 4931Zinc; catalyticPROSITE-ProRule annotation
Active sitei494 – 4941PROSITE-ProRule annotation
Metal bindingi497 – 4971Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi500 – 5001Zinc; 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1917728. Mipep.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionBy similarityAdd
BLAST
Chaini34 – 711678Mitochondrial intermediate peptidasePRO_0000319045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiA6H611.
PaxDbiA6H611.
PRIDEiA6H611.

PTM databases

PhosphoSiteiA6H611.

Expressioni

Gene expression databases

BgeeiA6H611.
CleanExiMM_MIPEP.
GenevestigatoriA6H611.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliA6H611.
SMRiA6H611. Positions 118-692.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000075047.
HOGENOMiHOG000230535.
HOVERGENiHBG008215.
InParanoidiA6H611.
KOiK01410.
OMAiNADLMEC.
OrthoDBiEOG7TTQ72.
PhylomeDBiA6H611.
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.

A6H611-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLAAGARYA RRLCGRGAAA ALQGRTGRSC ARDVSTSWSP VGAAFNVKPQ
60 70 80 90 100
SHLWNLLGER RGLFGVPELS TPEGFQVAQE EALKKTEWLV ERACSTPPGP
110 120 130 140 150
QTVLIFDELS DCLCRVADLA DFVKIGHPDP AFREAAQEAC RSIGTMVEKL
160 170 180 190 200
NTNVELYQSL QRLLGDKKLM ESLDAETRRV AELFMFDFEI SGIHLDEEKR
210 220 230 240 250
RRAVDLNVKI LDLSNAFLMR TNFPNKIRKS LLPEHIQHHF ARDGSHLIID
260 270 280 290 300
GLHAEASDDL VREAAYKIFL YPNADQLKCL EELLSSRDLL AKLVGYSTFS
310 320 330 340 350
HRALQGTIAQ TPETVMQFLE KLSEKLSERT RKDFKMMQGM KTKLNPQNSK
360 370 380 390 400
LMPWDPPYYS GVIRAERYNI EPSLYCPFLS LGACMEGLNV LFNKLLGITL
410 420 430 440 450
YAEQTFKGEV WCNDIRKLAV VHESEGLLGY IYCDFFQRAN KPQQDCHFTI
460 470 480 490 500
RGGRLKEDGS YQLPVVVLML NLPHASRDFP TLLTPGMMEN LFHEMGHAMH
510 520 530 540 550
SMLGRTRYQH VTGTRCPTDF AEVPSILMEY FSNDYRVVSQ FAKHYQTGQP
560 570 580 590 600
LPKAMVSRLC ESKKVCTAAE MQLQVFYAAL DQIYHGQHPL KKSTTDILME
610 620 630 640 650
TQEQFYGLPY VPDTAWQLRF SHLVGYGAKY YSYLMSRAVA SMIWKECFLQ
660 670 680 690 700
DPFNRAAGER YRREMLAHGG GKEPMLMIQG MLQKCPSIDD FVDALVSDMN
710
LDFETFFLDS K
Length:711
Mass (Da):80,852
Last modified:July 24, 2007 - v1
Checksum:iC22E9FFFB86A7ECB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611R → RVP in BAE27162. (PubMed:16141072)Curated
Sequence conflicti286 – 2861S → N in BAE27162. (PubMed:16141072)Curated
Sequence conflicti419 – 4191A → T in BAE27162. (PubMed:16141072)Curated
Sequence conflicti508 – 5081Y → H in AAI10359. (PubMed:15489334)Curated
Sequence conflicti595 – 5951T → A in BAE27162. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146428 mRNA. Translation: BAE27162.1.
BC049871 mRNA. Translation: AAH49871.1.
BC110358 mRNA. Translation: AAI10359.1.
BC145711 mRNA. Translation: AAI45712.1.
CCDSiCCDS49517.1.
RefSeqiNP_081712.2. NM_027436.3.
UniGeneiMm.274650.
Mm.486410.

Genome annotation databases

EnsembliENSMUST00000063562; ENSMUSP00000069840; ENSMUSG00000021993.
GeneIDi70478.
KEGGimmu:70478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146428 mRNA. Translation: BAE27162.1 .
BC049871 mRNA. Translation: AAH49871.1 .
BC110358 mRNA. Translation: AAI10359.1 .
BC145711 mRNA. Translation: AAI45712.1 .
CCDSi CCDS49517.1.
RefSeqi NP_081712.2. NM_027436.3.
UniGenei Mm.274650.
Mm.486410.

3D structure databases

ProteinModelPortali A6H611.
SMRi A6H611. Positions 118-692.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei A6H611.

Proteomic databases

MaxQBi A6H611.
PaxDbi A6H611.
PRIDEi A6H611.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000063562 ; ENSMUSP00000069840 ; ENSMUSG00000021993 .
GeneIDi 70478.
KEGGi mmu:70478.

Organism-specific databases

CTDi 4285.
MGIi MGI:1917728. Mipep.

Phylogenomic databases

eggNOGi COG0339.
GeneTreei ENSGT00550000075047.
HOGENOMi HOG000230535.
HOVERGENi HBG008215.
InParanoidi A6H611.
KOi K01410.
OMAi NADLMEC.
OrthoDBi EOG7TTQ72.
PhylomeDBi A6H611.
TreeFami TF105715.

Miscellaneous databases

NextBioi 331711.
PROi A6H611.
SOURCEi Search...

Gene expression databases

Bgeei A6H611.
CleanExi MM_MIPEP.
Genevestigatori A6H611.

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 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.
    , 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.

Entry informationi

Entry nameiMIPEP_MOUSE
AccessioniPrimary (citable) accession number: A6H611
Secondary accession number(s): Q2YD79, Q3UJJ3, Q80VA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 24, 2007
Last modified: November 26, 2014
This is version 65 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3