Reviewed, UniProtKB/Swiss-Prot Q99797 (MIPEP_HUMAN)

Names and origin

Protein names

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

Gene names

Name:	MIPEP
Synonyms:	MIP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	713 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves proteins, imported into the mitochondrion, to their mature size.
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.
Sequence similarities	Belongs to the peptidase M3 family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Calcium Cobalt Iron Magnesium Manganese Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Gene Ontology (GO)
Biological process	mitochondrial protein processing during import Ref.1 Traceable author statement. Source: ProtInc 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 Ref.1 Traceable author statement. Source: ProtInc 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 – 35	35	Mitochondrion
	Chain	36 – 713	678	Mitochondrial intermediate peptidase		PRO_0000028579
Sites
	Active site	496	1	By similarity
	Metal binding	495	1	Zinc; catalytic By similarity
	Metal binding	499	1	Zinc; catalytic By similarity
	Metal binding	502	1	Zinc; catalytic By similarity
Natural variations
	Natural variant	137	1	A → V: dbSNP rs2312296.		VAR_038934
	Natural variant	340	1	R → Q: dbSNP rs11551114.		VAR_038935
	Natural variant	453	1	R → H: dbSNP rs12858248.		VAR_038936
	Natural variant	488	1	S → G: dbSNP rs7333040. Ref.1 Ref.2 Ref.4		VAR_038937
Experimental info
	Sequence conflict	63 – 64	2	RG → AR in AAC51231. Ref.1
	Sequence conflict	200	1	E → Q in AAC51231. Ref.1
	Sequence conflict	348	1	P → A in AAC51231. Ref.1
	Sequence conflict	467	1	V → L in AAC51231. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99797-1 [UniParc]. Last modified February 26, 2008. Version 2. Checksum: 9DBB26B74355B9C1	FASTA	713	80,641
	10 20 30 40 50 60 MLCVGRLGGL GARAAALPPR RAGRGSLEAG IRARRVSTSW SPVGAAFNVK PQGSRLDLFG 70 80 90 100 110 120 ERRGLFGVPE LSAPEGFHIA QEKALRKTEL LVDRACSTPP GPQTVLIFDE LSDSLCRVAD 130 140 150 160 170 180 LADFVKIAHP EPAFREAAEE ACRSIGTMVE KLNTNVDLYQ SLQKLLADKK LVDSLDPETR 190 200 210 220 230 240 RVAELFMFDF EISGIHLDKE KRKRAVDLNV KILDLSSTFL MGTNFPNKIE KHLLPEHIRR 250 260 270 280 290 300 NFTSAGDHII IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST 310 320 330 340 350 360 FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN SEVMPWDPPY 370 380 390 400 410 420 YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI SLYAEQPAKG EVWSEDVRKL 430 440 450 460 470 480 AVVHESEGLL GYIYCDFFQR ADKPHQDCHF TIRGGRLKED GDYQLPVVVL MLNLPRSSRS 490 500 510 520 530 540 SPTLLTPSMM ENLFHEMGHA MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV 550 560 570 580 590 600 NQFARHYQTG QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL 610 620 630 640 650 660 KETQEKFYGL PYVPNTAWQL RFSHLVGYGA RYYSYLMSRA VASMVWKECF LQDPFNRAAG 670 680 690 700 710 ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD LDLDFETFLM DSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9073519] [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: 14702039] [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: 15057823] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-488. Tissue: Uterus.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00241860.
RefSeq	NP_005923.2.
UniGene	Hs.507498
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M03.006.
PTM databases
PhosphoSite	Q99797.
Proteomic databases
PRIDE	Q99797.
Genome annotation databases
Ensembl	ENSG00000027001. Homo sapiens. [Contig view]
GeneID	4285.
KEGG	hsa:4285.
Organism-specific databases
GeneCards	GC13M023202.
HGNC	HGNC:7104. MIPEP.
MIM	602241. gene.
PharmGKB	PA30822.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q99797.
HOVERGEN	Q99797.
OMA	Q99797. AMGERYR.
Enzyme and pathway databases
BRENDA	3.4.24.59. 247.
Gene expression databases
ArrayExpress	Q99797.
Bgee	Q99797.
CleanEx	HS_MIP. HS_MIPEP.
GermOnline	ENSG00000027001. Homo sapiens.
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	16857.
SOURCE	Search...

Entry information

Entry name

MIPEP_HUMAN

Accession

Primary (citable) accession number: Q99797
Secondary accession number(s): Q5JV15, Q5T9Q9, Q96G65

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 26, 2008
Last modified:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)