[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Bone marrow; DOI=10.1093/dnares/2.4.167; PubMed=8590280 [NCBI, ExPASy, EBI, Israel, Japan] Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.; "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."; DNA Res. 2:167-174(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. Miyajima N.; Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lymph, and Ovary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	MASS SPECTROMETRY. TISSUE=Mammary cancer; DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H; PubMed=11840567 [NCBI, ExPASy, EBI, Israel, Japan] Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.; "Cluster analysis of an extensive human breast cancer cell line protein expression map database."; Proteomics 2:212-223(2002).

Comments

FUNCTION: Cleaves presequences (transit peptides) from mitochondrial protein precursors (By similarity).
CATALYTIC ACTIVITY: Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.
SUBUNIT: Heterodimer of alpha and beta subunits (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
MASS SPECTROMETRY: Mass=54624.57; Method=MALDI; Range=33-525; Source=PubMed:11840567;.
SIMILARITY: Belongs to the peptidase M16 family [view classification].
CAUTION: Does not seem to have a protease activity as it lack the zinc-binding site.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D50913; BAA09472.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D21064; BAA04643.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022949; AAH22949.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033103; AAH33103.2; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_055975.1; -.

UniGene

Hs.495471

3D structure databases

HSSP

P11914; 1HR6. [HSSP ENTRY / PDB]

ModBase

Q10713.

Protein family/group databases

MEROPS

M16.971; -.

PTM databases

PhosphoSite

Q10713; -.

Organism-specific databases

HIX0008545; -.

HGNC:18667; PMPCA.

PA38629; -.

Gene expression databases

ArrayExpress

Q10713; -.

CleanEx

HS_INPP5E; -.
HS_PMPCA; -.

GermOnline

ENSG00000165688; Homo sapiens.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (traceable author statement from UniProtKB).
GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004222;	Molecular function: metalloendopeptidase activity (traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR011237; Pept_M16_core.
IPR011765; Pept_M16_N.
IPR001431; Pept_M16_Zn_BS.
IPR007863; Peptidase_M16_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.830.10; Pept_M16_core; 2.

Pfam

PF00675; Peptidase_M16; 1.
PF05193; Peptidase_M16_C; 1.
Pfam graphical view of domain structure.

PROSITE

PS00143; INSULINASE; 1.

ProtoNet

Q10713.

Proteomic databases

PeptideAtlas

Q10713; -.

Genome annotation databases

Ensembl

ENSG00000165688; Homo sapiens. [Contig view]

GeneID

23203; -.

KEGG

hsa:23203; -.

Phylogenomic databases

HOGENOM

Q10713; -.

HOVERGEN

Q10713; -.

Other

LinkHub

Q10713; -.

NextBio

44723; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Hydrolase; Metalloprotease; Mitochondrion; Protease; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 33`	`33`	`Mitochondrion.`
`CHAIN`	`34 525`	`492`	`Mitochondrial-processing peptidase subunit alpha.`	`PRO_0000026767`
`CONFLICT`	`495 495`		`G -> C (in Ref. 3; AAH22949).`
`CONFLICT`	`505 505`		`H -> D (in Ref. 1 and 2).`

Sequence information

Length: 525 AA [This is the length of the unprocessed precursor]

Molecular weight: 58253 Da [This is the MW of the unprocessed precursor]

CRC64: 2751E7FCDC864E3F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVVLAATR LLRGSGSWGC SRLRFGPPAY RRFSSGGAYP NIPLSSPLPG VPKPVFATVD 

        70         80         90        100        110        120 
GQEKFETKVT TLDNGLRVAS QNKFGQFCTV GILINSGSRY EAKYLSGIAH FLEKLAFSST 

       130        140        150        160        170        180 
ARFDSKDEIL LTLEKHGGIC DCQTSRDTTM YAVSADSKGL DTVVALLADV VLQPRLTDEE 

       190        200        210        220        230        240 
VEMTRMAVQF ELEDLNLRPD PEPLLTEMIH EAAYRENTVG LHRFCPTENV AKINREVLHS 

       250        260        270        280        290        300 
YLRNYYTPDR MVLAGVGVEH EHLVDCARKY LLGVQPAWGS AEAVDIDRSV AQYTGGIAKL 

       310        320        330        340        350        360 
ERDMSNVSLG PTPIPELTHI MVGLESCSFL EEDFIPFAVL NMMMGGGGSF SAGGPGKGMF 

       370        380        390        400        410        420 
SRLYLNVLNR HHWMYNATSY HHSYEDTGLL CIHASADPRQ VREMVEIITK EFILMGGTVD 

       430        440        450        460        470        480 
TVELERAKTQ LTSMLMMNLE SRPVIFEDVG RQVLATRSRK LPHELCTLIR NVKPEDVKRV 

       490        500        510        520 
ASKMLRGKPA VAALGDLTDL PTYEHIQTAL SSKDGRLPRT YRLFR

Q10713 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools