Reviewed, UniProtKB/Swiss-Prot Q9CXT8 (MPPB_MOUSE)

Names and origin

Protein names

Recommended name:
    Mitochondrial-processing peptidase subunit beta
    EC=3.4.24.64
Alternative name(s):
    Beta-MPP
    P-52

Gene names

Name:

Pmpcb

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	489 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 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.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Heterodimer of alpha and beta subunits By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the peptidase M16 family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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 – 45	45	Mitochondrion Potential
	Chain	46 – 489	444	Mitochondrial-processing peptidase subunit beta		PRO_0000026778
Sites
	Active site	104	1	Proton acceptor By similarity
	Metal binding	101	1	Zinc By similarity
	Metal binding	105	1	Zinc By similarity
	Metal binding	181	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CXT8-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 1B594EE0B6FE34A4	FASTA	489	54,614
	10 20 30 40 50 60 MAAAALSRTL LPEARRRLWG FTRRLPLRRA AAQPLYFGGD RLRSTQAAPQ VVLNVPETQV 70 80 90 100 110 120 TCLENGLRVA SENSGLSTCT VGLWIDAGSR YENEKNNGTA HFLEHMAFKG TKKRSQLDLE 130 140 150 160 170 180 LEIENMGAHL NAYTSREQTV YYAKAFSRDL PRAVEILADI IQNSTLGEAE IERERGVILR 190 200 210 220 230 240 EMQEVETNLQ EVVFDYLHAT AYQNTALGRT ILGPTENIKS INRKDLVDYI TTHYKGPRIV 250 260 270 280 290 300 LAAAGGVCHN ELLELAKFHF GDSLCSHKGA IPALPPCKFT GSEIRVRDDK MPLAHLAIAV 310 320 330 340 350 360 EAVGWAHPDT ICLMVANTLI GNWDRSFGGG MNLSSKLAQL TCHGNLCHSF QSFNTSYTDT 370 380 390 400 410 420 GLWGLYMVCE QATVADMLHV VQNEWKRLCT DVTESEVARA KNLLKTNMLL QLDGSTPICE 430 440 450 460 470 480 DIGRQMLCYN RRIPIPELEA RIDAVDAETV RRVCTKYIHD KSPAIAALGP IERLPDFNQI CSNMRWIRD

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: C57BL/6J. Tissue: Embryonic head.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK013995 mRNA. Translation: BAB29105.1.
IPI	IPI00274656.
RefSeq	NP_082707.1.
UniGene	Mm.301655
3D structure databases
HSSP	HSSP built from PDB template 1HR6 based on UniProtKB P10507.
ModBase	Search...
Protein family/group databases
MEROPS	M16.003.
2-D gel databases
REPRODUCTION-2DPAGE	Q9CXT8.
Genome annotation databases
Ensembl	ENSMUSG00000029017. Mus musculus. [Contig view]
GeneID	73078.
KEGG	mmu:73078.
Organism-specific databases
MGI	MGI:1920328. Pmpcb.
Phylogenomic databases
HOGENOM	Q9CXT8.
HOVERGEN	Q9CXT8.
OMA	Q9CXT8. IPLMVAN.
Enzyme and pathway databases
BRENDA	3.4.24.64. 244.
Gene expression databases
ArrayExpress	Q9CXT8.
Bgee	Q9CXT8.
CleanEx	MM_PMPCB.
GermOnline	ENSMUSG00000029017. Mus musculus.
Family and domain databases
InterPro	IPR011237. Pept_M16_core. IPR011765. Pept_M16_N. IPR001431. Pept_M16_Zn_BS. IPR007863. Peptidase_M16_C. [Graphical view]
Gene3D	G3DSA:3.30.830.10. Pept_M16_core. 2 hits.
Pfam	PF00675. Peptidase_M16. 1 hit. PF05193. Peptidase_M16_C. 1 hit. [Graphical view]
PROSITE	PS00143. INSULINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	337429.
SOURCE	Search...

Entry information

Entry name

MPPB_MOUSE

Accession

Primary (citable) accession number: Q9CXT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)