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Q9JIQ8

- TMPS2_MOUSE

UniProt

Q9JIQ8 - TMPS2_MOUSE

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Protein

Transmembrane protease serine 2

Gene

Tmprss2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8383CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei84 – 10421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini105 – 490386ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

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...

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.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251822.
HOVERGENiHBG013304.
InParanoidiQ9JIQ8.
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

« Hide

        10         20         30         40         50
MALNSGSPPG IGPCYENHGY QSEHICPPRP PVAPNGYNLY PAQYYPSPVP
60 70 80 90 100
QYAPRITTQA STSVIHTHPK SSGALCTSKS KKSLCLALAL GTVLTGAAVA
110 120 130 140 150
AVLLWRFWDS NCSTSEMECG SSGTCISSSL WCDGVAHCPN GEDENRCVRL
160 170 180 190 200
YGQSFILQVY SSQRKAWYPV CQDDWSESYG RAACKDMGYK NNFYSSQGIP
210 220 230 240 250
DQSGATSFMK LNVSSGNVDL YKKLYHSDSC SSRMVVSLRC IECGVRSVKR
260 270 280 290 300
QSRIVGGLNA SPGDWPWQVS LHVQGVHVCG GSIITPEWIV TAAHCVEEPL
310 320 330 340 350
SSPRYWTAFA GILRQSLMFY GSRHQVEKVI SHPNYDSKTK NNDIALMKLQ
360 370 380 390 400
TPLAFNDLVK PVCLPNPGMM LDLDQECWIS GWGATYEKGK TSDVLNAAMV
410 420 430 440 450
PLIEPSKCNS KYIYNNLITP AMICAGFLQG SVDSCQGDSG GPLVTLKNGI
460 470 480 490
WWLIGDTSWG SGCAKALRPG VYGNVTVFTD WIYQQMRANS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000118962.
HOGENOMi HOG000251822.
HOVERGENi HBG013304.
InParanoidi Q9JIQ8.
KOi K09633.
OMAi KSWHPVC.
OrthoDBi EOG75B84T.
TreeFami TF351678.

Miscellaneous databases

ChiTaRSi Tmprss2. mouse.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 134 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