Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8BM88 (CATO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. 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:
Cathepsin O
EC=3.4.22.42
Gene names
Name:Ctso
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover By similarity.

Catalytic activity

The recombinant human enzyme hydrolyzes synthetic endopeptidase substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-NHMec.

Subcellular location

Lysosome By similarity.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 9875Activation peptide
PRO_0000026323
Chain99 – 312214Cathepsin O
PRO_0000026324

Sites

Active site1231 By similarity
Active site2601 By similarity
Active site2801 By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Disulfide bond120 ↔ 161 By similarity
Disulfide bond154 ↔ 195 By similarity
Disulfide bond253 ↔ 301 By similarity

Experimental info

Sequence conflict631F → L in BAC33765. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BM88 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4C7C056D0771807C

FASTA31234,723
        10         20         30         40         50         60 
MKPQLVNLLL LCCCCLGRHG VAGTWSWSHQ REAAALRESL HRHRYLNSFP HENSTAFYGV 

        70         80         90        100        110        120 
NQFSYLFPEE FKALYLGSKY AWAPRYPAEG QRPIPNVSLP LRFDWRDKHV VNPVRNQEMC 

       130        140        150        160        170        180 
GGCWAFSVVS AIESARAIQG KSLDYLSVQQ VIDCSFNNSG CLGGSPLCAL RWLNETQLKL 

       190        200        210        220        230        240 
VADSQYPFKA VNGQCRHFPQ SQAGVSVKDF SAYNFRGQED EMARALLSFG PLVVIVDAMS 

       250        260        270        280        290        300 
WQDYLGGIIQ HHCSSGEANH AVLITGFDRT GNTPYWMVRN SWGSSWGVEG YAHVKMGGNV 

       310 
CGIADSVAAV FV

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Diencephalon, Embryo and Lung.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-312.
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK034490 mRNA. Translation: BAC28728.1.
AK049470 mRNA. Translation: BAC33765.1.
AK165930 mRNA. Translation: BAE38466.1.
AK166103 mRNA. Translation: BAE38573.1.
BC044664 mRNA. Translation: AAH44664.1.
IPIIPI00453524.
RefSeqNP_808330.1. NM_177662.2.
UniGeneMm.254642.

3D structure databases

ProteinModelPortalQ8BM88.
SMRQ8BM88. Positions 24-308.
ModBaseSearch...

Protein family/group databases

MEROPSC01.035.

PTM databases

PhosphoSiteQ8BM88.

Proteomic databases

PRIDEQ8BM88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029649; ENSMUSP00000029649; ENSMUSG00000028015.
GeneID229445.
KEGGmmu:229445.
UCSCuc008pon.1. mouse.

Organism-specific databases

CTD1519.
MGIMGI:2139628. Ctso.

Phylogenomic databases

eggNOGCOG4870.
GeneTreeENSGT00560000076599.
HOGENOMHOG000230774.
HOVERGENHBG105050.
InParanoidQ8BM88.
KOK01374.
OMASNVCGIA.
OrthoDBEOG4V6ZH1.

Gene expression databases

BgeeQ8BM88.
CleanExMM_CTSO.
GenevestigatorQ8BM88.
GermOnlineENSMUSG00000028015. Mus musculus.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379433.
SOURCESearch...

Entry information

Entry nameCATO_MOUSE
AccessionPrimary (citable) accession number: Q8BM88
Secondary accession number(s): Q3TM69, Q80V35, Q8BKX0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 79 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