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Reviewed, UniProtKB/Swiss-Prot Q8BW11 (TRYX3_MOUSE)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative trypsin-X3
    EC=3.4.21.4
Gene names
Name: Tryx3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   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 trypsin-X3
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
Q8BW11-1 [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: 11160223] [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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.

Cross-references

Sequence databases

AE000663 Genomic DNA. Translation: AAB69042.1.
AK075754 mRNA. Translation: BAC35932.1.
BC048599 mRNA. Translation: AAH48599.1.
IPIIPI00225978.
RefSeqNP_778185.1.
UniGeneMm.56997

3D structure databases

HSSPHSSP built from PDB template 2HNT based on UniProtKB P00734.
ModBaseSearch...

Protein family/group databases

MEROPSS01.984.

Genome annotation databases

EnsemblENSMUSG00000051936. Mus musculus. [Contig view]
GeneID232717.
KEGGmmu:232717.

Organism-specific databases

MGIMGI:3608323. BC048599.

Phylogenomic databases

HOGENOMQ8BW11.
HOVERGENQ8BW11.
OMAQ8BW11. VSTWAYN.

Enzyme and pathway databases

BRENDA3.4.21.4. 244.

Gene expression databases

ArrayExpressQ8BW11.
BgeeQ8BW11.
CleanExMM_BC048599.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio381207.
SOURCESearch...

Entry information

Entry nameTRYX3_MOUSE
AccessionPrimary (citable) accession number: Q8BW11
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents