Reviewed, UniProtKB/Swiss-Prot A6H611 (MIPEP_MOUSE)

Names and origin

Protein names

Recommended name:
    Mitochondrial intermediate peptidase
      Short name=MIP
    EC=3.4.24.59

Gene names

Name:

Mipep

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	711 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Calcium Cobalt Iron Magnesium Manganese Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Acetylation
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion By similarity
	Chain	34 – 711	678	Mitochondrial intermediate peptidase		PRO_0000319045
Sites
	Active site	494	1	By similarity
	Metal binding	493	1	Zinc; catalytic By similarity
	Metal binding	497	1	Zinc; catalytic By similarity
	Metal binding	500	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	124	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	61	1	R → RVP in BAE27162. Ref.1
	Sequence conflict	286	1	S → N in BAE27162. Ref.1
	Sequence conflict	419	1	A → T in BAE27162. Ref.1
	Sequence conflict	508	1	Y → H in AAI10359. Ref.2
	Sequence conflict	595	1	T → A in BAE27162. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A6H611-1 [UniParc]. Last modified July 24, 2007. Version 1. Checksum: C22E9FFFB86A7ECB	FASTA	711	80,852
	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

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. , 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: 16141072] [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: 15489334] [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
EMBLGenBankDDBJ	AK146428 mRNA. Translation: BAE27162.1. BC049871 mRNA. Translation: AAH49871.1. BC110358 mRNA. Translation: AAI10359.1. BC145711 mRNA. Translation: AAI45712.1.
IPI	IPI00222838.
RefSeq	NP_081712.2.
UniGene	Mm.274650
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A6H611.
Protein family/group databases
MEROPS	M03.006.
Genome annotation databases
Ensembl	ENSMUST00000063562; ENSMUSP00000069840; ENSMUSG00000021993; Mus musculus. [Genome view]
GeneID	70478.
KEGG	mmu:70478.
Organism-specific databases
CTD	70478.
MGI	MGI:1917728. Mipep.
Enzyme and pathway databases
BRENDA	3.4.24.59. 244.
Gene expression databases
ArrayExpress	A6H611.
Bgee	A6H611.
CleanEx	MM_MIPEP.
Genevestigator	A6H611.
Family and domain databases
InterPro	IPR001567. Pept_M3A_M3B. IPR006025. Pept_M_Zn_BS. [Graphical view]
Pfam	PF01432. Peptidase_M3. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	331711.
SOURCE	Search...

Entry information

Entry name

MIPEP_MOUSE

Accession

Primary (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:	October 13, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)