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Q9JIQ8

- TMPS2_MOUSE

UniProt

Q9JIQ8 - TMPS2_MOUSE

Protein

Transmembrane protease serine 2

Gene

Tmprss2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Serine protease that proteolytically cleaves and activates the viral spike glycoproteins which facilitate virus-cell membrane fusions. The spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Facilitates human SARS coronavirus (SARS-CoV) infection via two independent mechanisms, proteolytic cleavage of ACE2, which might promote viral uptake, and cleavage of coronavirus spike glycoprotein which activates the glycoprotein for cathepsin L-independent host cell entry. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9) and is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei253 – 2542CleavageSequence Analysis
    Active sitei294 – 2941Charge relay systemBy similarity
    Active sitei343 – 3431Charge relay systemBy similarity
    Active sitei439 – 4391Charge relay systemBy similarity

    GO - Molecular functioni

    1. scavenger receptor activity Source: InterPro
    2. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. positive regulation of viral entry into host cell Source: UniProtKB
    2. protein autoprocessing Source: UniProtKB
    3. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.247.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transmembrane protease serine 2 (EC:3.4.21.-)
    Alternative name(s):
    Epitheliasin
    Plasmic transmembrane protein X
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Tmprss2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1354381. Tmprss2.

    Subcellular locationi

    Transmembrane protease serine 2 catalytic chain : Secreted By similarity
    Note: Activated by cleavage and secreted.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Abrogation of viral spread and protection of mice from severe pathology and death seen after infection with influenza A virus strains H1N1 and H7N9.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 253253Transmembrane protease serine 2 non-catalytic chainPRO_0000027857Add
    BLAST
    Chaini254 – 490237Transmembrane protease serine 2 catalytic chainPRO_0000027858Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi112 ↔ 125By similarity
    Disulfide bondi119 ↔ 138By similarity
    Disulfide bondi132 ↔ 147By similarity
    Disulfide bondi171 ↔ 230By similarity
    Disulfide bondi184 ↔ 240By similarity
    Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi243 ↔ 363Interchain (between non-catalytic and catalytic chains)PROSITE-ProRule annotation
    Disulfide bondi279 ↔ 295By similarity
    Disulfide bondi408 ↔ 424By similarity
    Disulfide bondi435 ↔ 463By similarity
    Glycosylationi474 – 4741N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Proteolytically processed; by an autocatalytic mechanism.By similarity

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiQ9JIQ8.

    PTM databases

    PhosphoSiteiQ9JIQ8.

    Expressioni

    Tissue specificityi

    Larynx, trachea and bronchi, lung, prostate and kidney.2 Publications

    Gene expression databases

    BgeeiQ9JIQ8.
    CleanExiMM_TMPRSS2.
    GenevestigatoriQ9JIQ8.

    Interactioni

    Subunit structurei

    The catalytically active form interacts with ACE2.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JIQ8.
    SMRiQ9JIQ8. Positions 157-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 8383CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini105 – 490386ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei84 – 10421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 14939LDL-receptor class APROSITE-ProRule annotationAdd
    BLAST
    Domaini150 – 24293SRCRPROSITE-ProRule annotationAdd
    BLAST
    Domaini254 – 487234Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 LDL-receptor class A domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 1 SRCR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00730000110467.
    HOGENOMiHOG000251822.
    HOVERGENiHBG013304.
    InParanoidiQ7TN04.
    KOiK09633.
    OMAiKSWHPVC.
    OrthoDBiEOG75B84T.
    TreeFamiTF351678.

    Family and domain databases

    Gene3Di3.10.250.10. 1 hit.
    4.10.400.10. 1 hit.
    InterProiIPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00057. Ldl_recept_a. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00192. LDLa. 1 hit.
    SM00202. SR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 1 hit.
    SSF57424. SSF57424. 1 hit.
    PROSITEiPS01209. LDLRA_1. 1 hit.
    PS50068. LDLRA_2. 1 hit.
    PS50287. SRCR_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9JIQ8-1 [UniParc]FASTAAdd to Basket

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    MALNSGSPPG IGPCYENHGY QSEHICPPRP PVAPNGYNLY PAQYYPSPVP    50
    QYAPRITTQA STSVIHTHPK SSGALCTSKS KKSLCLALAL GTVLTGAAVA 100
    AVLLWRFWDS NCSTSEMECG SSGTCISSSL WCDGVAHCPN GEDENRCVRL 150
    YGQSFILQVY SSQRKAWYPV CQDDWSESYG RAACKDMGYK NNFYSSQGIP 200
    DQSGATSFMK LNVSSGNVDL YKKLYHSDSC SSRMVVSLRC IECGVRSVKR 250
    QSRIVGGLNA SPGDWPWQVS LHVQGVHVCG GSIITPEWIV TAAHCVEEPL 300
    SSPRYWTAFA GILRQSLMFY GSRHQVEKVI SHPNYDSKTK NNDIALMKLQ 350
    TPLAFNDLVK PVCLPNPGMM LDLDQECWIS GWGATYEKGK TSDVLNAAMV 400
    PLIEPSKCNS KYIYNNLITP AMICAGFLQG SVDSCQGDSG GPLVTLKNGI 450
    WWLIGDTSWG SGCAKALRPG VYGNVTVFTD WIYQQMRANS 490
    Length:490
    Mass (Da):53,526
    Last modified:July 27, 2011 - v3
    Checksum:i54650B028417665A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751L → P in AAF97867. (PubMed:11169526)Curated
    Sequence conflicti75 – 751L → P in AAF64186. 1 PublicationCurated
    Sequence conflicti75 – 751L → P in AAF21308. (PubMed:10683448)Curated
    Sequence conflicti75 – 751L → P in AAH38393. (PubMed:15489334)Curated
    Sequence conflicti122 – 1221S → L in AAF21308. (PubMed:10683448)Curated
    Sequence conflicti178 – 1781S → N in AAF21308. (PubMed:10683448)Curated
    Sequence conflicti302 – 3021S → G in AAF97867. (PubMed:11169526)Curated
    Sequence conflicti302 – 3021S → G in AAF64186. 1 PublicationCurated
    Sequence conflicti302 – 3021S → G in AAF21308. (PubMed:10683448)Curated
    Sequence conflicti302 – 3021S → G in AAH38393. (PubMed:15489334)Curated
    Sequence conflicti320 – 3201Y → H in AAF97867. (PubMed:11169526)Curated
    Sequence conflicti474 – 4741N → D in AAF97867. (PubMed:11169526)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF199362 mRNA. Translation: AAF97867.1.
    AF243500 mRNA. Translation: AAF64186.1.
    AF113596 mRNA. Translation: AAF21308.1.
    BC038393 mRNA. Translation: AAH38393.1.
    BC054348 mRNA. Translation: AAH54348.1.
    CCDSiCCDS37417.1.
    RefSeqiNP_056590.2. NM_015775.2.
    XP_006523127.1. XM_006523064.1.
    XP_006523128.1. XM_006523065.1.
    UniGeneiMm.276145.

    Genome annotation databases

    EnsembliENSMUST00000000395; ENSMUSP00000000395; ENSMUSG00000000385.
    GeneIDi50528.
    KEGGimmu:50528.
    UCSCiuc008adl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF199362 mRNA. Translation: AAF97867.1 .
    AF243500 mRNA. Translation: AAF64186.1 .
    AF113596 mRNA. Translation: AAF21308.1 .
    BC038393 mRNA. Translation: AAH38393.1 .
    BC054348 mRNA. Translation: AAH54348.1 .
    CCDSi CCDS37417.1.
    RefSeqi NP_056590.2. NM_015775.2.
    XP_006523127.1. XM_006523064.1.
    XP_006523128.1. XM_006523065.1.
    UniGenei Mm.276145.

    3D structure databases

    ProteinModelPortali Q9JIQ8.
    SMRi Q9JIQ8. Positions 157-490.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.247.

    PTM databases

    PhosphoSitei Q9JIQ8.

    Proteomic databases

    PRIDEi Q9JIQ8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000395 ; ENSMUSP00000000395 ; ENSMUSG00000000385 .
    GeneIDi 50528.
    KEGGi mmu:50528.
    UCSCi uc008adl.1. mouse.

    Organism-specific databases

    CTDi 7113.
    MGIi MGI:1354381. Tmprss2.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00730000110467.
    HOGENOMi HOG000251822.
    HOVERGENi HBG013304.
    InParanoidi Q7TN04.
    KOi K09633.
    OMAi KSWHPVC.
    OrthoDBi EOG75B84T.
    TreeFami TF351678.

    Miscellaneous databases

    NextBioi 307534.
    PROi Q9JIQ8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JIQ8.
    CleanExi MM_TMPRSS2.
    Genevestigatori Q9JIQ8.

    Family and domain databases

    Gene3Di 3.10.250.10. 1 hit.
    4.10.400.10. 1 hit.
    InterProi IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00057. Ldl_recept_a. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00192. LDLa. 1 hit.
    SM00202. SR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 1 hit.
    SSF57424. SSF57424. 1 hit.
    PROSITEi PS01209. LDLRA_1. 1 hit.
    PS50068. LDLRA_2. 1 hit.
    PS50287. SRCR_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of transmembrane serine protease TMPRSS2 in mouse and human tissues."
      Vaarala M.H., Porvari K.S., Kellokumpu S., Kyllonen A.P., Vihko P.T.
      J. Pathol. 193:134-140(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: BALB/c.
    2. "Putative transmembrane protease X."
      Han J., Kim S.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase: epitheliasin."
      Jacquinet E.J., Rao N.V., Rao G.V., Hoidal J.R.
      FEBS Lett. 468:93-100(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    4. "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].
      Strain: 129.
      Tissue: Mammary gland.
    5. Cited for: FUNCTION.
    6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "TMPRSS2 is a host factor that is essential for pneumotropism and pathogenicity of H7N9 influenza A virus in mice."
      Tarnow C., Engels G., Arendt A., Schwalm F., Sediri H., Preuss A., Nelson P.S., Garten W., Klenk H.D., Gabriel G., Boettcher-Friebertshaeuser E.
      J. Virol. 88:4744-4751(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    8. "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."
      Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S.
      J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiTMPS2_MOUSE
    AccessioniPrimary (citable) accession number: Q9JIQ8
    Secondary accession number(s): Q7TN04, Q9JKC4, Q9QY82
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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