Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8BW11

- PRS58_MOUSE

UniProt

Q8BW11 - PRS58_MOUSE

Protein

Putative inactive serine protease 58

Gene

Prss58

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei56 – 561Charge relay systemBy similarity
    Active sitei101 – 1011Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative inactive serine protease 58 (EC:3.4.21.4)
    Alternative name(s):
    Trypsin-X3
    Gene namesi
    Name:Prss58
    Synonyms:Tryx3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:3608323. Prss58.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 241224Putative inactive serine protease 58PRO_0000317764Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 57PROSITE-ProRule annotation
    Disulfide bondi133 ↔ 201PROSITE-ProRule annotation
    Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi165 ↔ 180PROSITE-ProRule annotation
    Disulfide bondi191 ↔ 215PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8BW11.

    PTM databases

    PhosphoSiteiQ8BW11.

    Expressioni

    Gene expression databases

    BgeeiQ8BW11.
    CleanExiMM_BC048599.
    GenevestigatoriQ8BW11.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000069833.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BW11.
    SMRiQ8BW11. Positions 6-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 239222Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG289695.
    GeneTreeiENSGT00750000117405.
    HOVERGENiHBG013304.
    InParanoidiQ8BW11.
    OMAiVSTWAYN.
    OrthoDBiEOG7TBC32.
    PhylomeDBiQ8BW11.
    TreeFamiTF331065.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8BW11-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLAFLCILS TLLRTFAYNP DHIAGTTPPY LVYLKSDYLP CTGVLIHPLW    50
    VITAAHCNLP NLQVILGITN PADPMERDVE VSDYEKIFHH PNFLVSSISH 100
    DLLLIKLKRR IKHSNYAKAV KLPQHIVSVN AMCSVSTWAY NLCDVTKDPD 150
    SLQTVNVTVI SKAECRNAYK AFDITENMIC VGIVPGRRLP CKEVTAAPAV 200
    CNGVLYGILS YADGCVLRAD VGIYASIFHY LPWIEDTMKN N 241
    Length:241
    Mass (Da):26,865
    Last modified:March 1, 2003 - v1
    Checksum:i8FC9D0D994A4AE7F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000663 Genomic DNA. Translation: AAB69042.1.
    AK075754 mRNA. Translation: BAC35932.1.
    BC048599 mRNA. Translation: AAH48599.1.
    CCDSiCCDS20040.1.
    RefSeqiNP_778185.1. NM_175020.3.
    UniGeneiMm.56997.

    Genome annotation databases

    EnsembliENSMUST00000063523; ENSMUSP00000069833; ENSMUSG00000051936.
    GeneIDi232717.
    KEGGimmu:232717.
    UCSCiuc009bnk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000663 Genomic DNA. Translation: AAB69042.1 .
    AK075754 mRNA. Translation: BAC35932.1 .
    BC048599 mRNA. Translation: AAH48599.1 .
    CCDSi CCDS20040.1.
    RefSeqi NP_778185.1. NM_175020.3.
    UniGenei Mm.56997.

    3D structure databases

    ProteinModelPortali Q8BW11.
    SMRi Q8BW11. Positions 6-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000069833.

    Protein family/group databases

    MEROPSi S01.984.

    PTM databases

    PhosphoSitei Q8BW11.

    Proteomic databases

    PRIDEi Q8BW11.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000063523 ; ENSMUSP00000069833 ; ENSMUSG00000051936 .
    GeneIDi 232717.
    KEGGi mmu:232717.
    UCSCi uc009bnk.1. mouse.

    Organism-specific databases

    CTDi 136541.
    MGIi MGI:3608323. Prss58.

    Phylogenomic databases

    eggNOGi NOG289695.
    GeneTreei ENSGT00750000117405.
    HOVERGENi HBG013304.
    InParanoidi Q8BW11.
    OMAi VSTWAYN.
    OrthoDBi EOG7TBC32.
    PhylomeDBi Q8BW11.
    TreeFami TF331065.

    Miscellaneous databases

    NextBioi 381207.
    PROi Q8BW11.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BW11.
    CleanExi MM_BC048599.
    Genevestigatori Q8BW11.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiPRS58_MOUSE
    AccessioniPrimary (citable) accession number: Q8BW11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3