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Q9CXT8 (MPPB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial-processing peptidase subunit beta
EC=3.4.24.64
Alternative name(s):
Beta-MPP
P-52
Gene names
Name:Pmpcb
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial inner membrane

Inferred from direct assay. Source: MGI

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Mitochondrion By similarity
Chain46 – 489444Mitochondrial-processing peptidase subunit beta
PRO_0000026778

Sites

Active site1041Proton acceptor By similarity
Metal binding1011Zinc By similarity
Metal binding1051Zinc By similarity
Metal binding1811Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CXT8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1B594EE0B6FE34A4

FASTA48954,614
        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

« Hide

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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK013995 mRNA. Translation: BAB29105.1.
IPIIPI00274656.
RefSeqNP_082707.1. NM_028431.2.
UniGeneMm.301655.

3D structure databases

ProteinModelPortalQ9CXT8.
SMRQ9CXT8. Positions 47-488.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9CXT8.

Protein family/group databases

MEROPSM16.003.

PTM databases

PhosphoSiteQ9CXT8.

2D gel databases

REPRODUCTION-2DPAGEQ9CXT8.

Proteomic databases

PRIDEQ9CXT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030882; ENSMUSP00000030882; ENSMUSG00000029017.
GeneID73078.
KEGGmmu:73078.
UCSCuc008wox.1. mouse.

Organism-specific databases

CTD9512.
MGIMGI:1920328. Pmpcb.

Phylogenomic databases

GeneTreeENSGT00550000074701.
HOGENOMHBG476859.
HOVERGENHBG006393.
InParanoidQ9CXT8.
OMAIPLMVAN.
OrthoDBEOG4XPQFR.
PhylomeDBQ9CXT8.

Gene expression databases

ArrayExpressQ9CXT8.
BgeeQ9CXT8.
CleanExMM_PMPCB.
GenevestigatorQ9CXT8.
GermOnlineENSMUSG00000029017. Mus musculus.

Family and domain databases

InterProIPR011249. Metalloenz_metal-bd.
IPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
Gene3DG3DSA:3.30.830.10. Pept_M16_core. 2 hits.
KOK01412.
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMSSF63411. Metalloenz_metal-bd. 2 hits.
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio337429.
SOURCESearch...

Entry information

Entry nameMPPB_MOUSE
AccessionPrimary (citable) accession number: Q9CXT8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents