Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8BW11 (PRS58_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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

Names and origin

Protein namesRecommended name:
Putative inactive serine protease 58

EC=3.4.21.4
Alternative name(s):
Trypsin-X3
Gene names
Name:Prss58
Synonyms:Tryx3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Caution

Thr-195 is present instead of the conserved Ser which is expected to be an active site residue. It is therefore unsure if this protein has kept its catalytic activity.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 241224Putative inactive serine protease 58
PRO_0000317764

Regions

Domain18 – 239222Peptidase S1

Sites

Active site561Charge relay system By similarity
Active site1011Charge relay system By similarity

Amino acid modifications

Glycosylation1561N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 57 By similarity
Disulfide bond133 ↔ 201 By similarity
Disulfide bond165 ↔ 180 By similarity
Disulfide bond191 ↔ 215 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BW11 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 8FC9D0D994A4AE7F

FASTA24126,865
        10         20         30         40         50         60 
MKLAFLCILS TLLRTFAYNP DHIAGTTPPY LVYLKSDYLP CTGVLIHPLW VITAAHCNLP 

        70         80         90        100        110        120 
NLQVILGITN PADPMERDVE VSDYEKIFHH PNFLVSSISH DLLLIKLKRR IKHSNYAKAV 

       130        140        150        160        170        180 
KLPQHIVSVN AMCSVSTWAY NLCDVTKDPD SLQTVNVTVI SKAECRNAYK AFDITENMIC 

       190        200        210        220        230        240 
VGIVPGRRLP CKEVTAAPAV CNGVLYGILS YADGCVLRAD VGIYASIFHY LPWIEDTMKN 


N 

« Hide

References

« Hide 'large scale' references
[1]"Differential transcriptional regulation of individual TCR V beta segments before gene rearrangement."
Chen F., Rowen L., Hood L., Rothenberg E.V.
J. Immunol. 166:1771-1780(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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: Testis.
[3]"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].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000663 Genomic DNA. Translation: AAB69042.1.
AK075754 mRNA. Translation: BAC35932.1.
BC048599 mRNA. Translation: AAH48599.1.
RefSeqNP_778185.1. NM_175020.3.
UniGeneMm.56997.

3D structure databases

ProteinModelPortalQ8BW11.
SMRQ8BW11. Positions 29-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000069833.

Protein family/group databases

MEROPSS01.984.

PTM databases

PhosphoSiteQ8BW11.

Proteomic databases

PRIDEQ8BW11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063523; ENSMUSP00000069833; ENSMUSG00000051936.
GeneID232717.
KEGGmmu:232717.
UCSCuc009bnk.1. mouse.

Organism-specific databases

CTD136541.
MGIMGI:3608323. Prss58.

Phylogenomic databases

eggNOGNOG289695.
GeneTreeENSGT00750000117405.
HOVERGENHBG013304.
InParanoidQ8BW11.
OMAVSTWAYN.
OrthoDBEOG7TBC32.
PhylomeDBQ8BW11.
TreeFamTF331065.

Gene expression databases

BgeeQ8BW11.
CleanExMM_BC048599.
GenevestigatorQ8BW11.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio381207.
PROQ8BW11.
SOURCESearch...

Entry information

Entry namePRS58_MOUSE
AccessionPrimary (citable) accession number: Q8BW11
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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