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Q9JIQ8 (TMPS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. 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:
Transmembrane protease serine 2

EC=3.4.21.-
Alternative name(s):
Epitheliasin
Plasmic transmembrane protein X
Gene names
Name:Tmprss2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7 Ref.8

Subunit structure

The catalytically active form interacts with ACE2 By similarity.

Subcellular location

Cell membrane; Single-pass type II membrane protein By similarity.

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

Tissue specificity

Larynx, trachea and bronchi, lung, prostate and kidney. Ref.1 Ref.7

Post-translational modification

Proteolytically processed; by an autocatalytic mechanism By similarity.

Disruption phenotype

Abrogation of viral spread and protection of mice from severe pathology and death seen after infection with influenza A virus strains H1N1 and H7N9. Ref.6 Ref.7

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 LDL-receptor class A domain.

Contains 1 peptidase S1 domain.

Contains 1 SRCR domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 253253Transmembrane protease serine 2 non-catalytic chain
PRO_0000027857
Chain254 – 490237Transmembrane protease serine 2 catalytic chain
PRO_0000027858

Regions

Topological domain1 – 8383Cytoplasmic Potential
Transmembrane84 – 10421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain105 – 490386Extracellular Potential
Domain111 – 14939LDL-receptor class A
Domain150 – 24293SRCR
Domain254 – 487234Peptidase S1

Sites

Active site2941Charge relay system By similarity
Active site3431Charge relay system By similarity
Active site4391Charge relay system By similarity
Site253 – 2542Cleavage Potential

Amino acid modifications

Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation4741N-linked (GlcNAc...) Potential
Disulfide bond112 ↔ 125 By similarity
Disulfide bond119 ↔ 138 By similarity
Disulfide bond132 ↔ 147 By similarity
Disulfide bond171 ↔ 230 By similarity
Disulfide bond184 ↔ 240 By similarity
Disulfide bond243 ↔ 363Interchain (between non-catalytic and catalytic chains) By similarity
Disulfide bond279 ↔ 295 By similarity
Disulfide bond408 ↔ 424 By similarity
Disulfide bond435 ↔ 463 By similarity

Experimental info

Sequence conflict751L → P in AAF97867. Ref.1
Sequence conflict751L → P in AAF64186. Ref.2
Sequence conflict751L → P in AAF21308. Ref.3
Sequence conflict751L → P in AAH38393. Ref.4
Sequence conflict1221S → L in AAF21308. Ref.3
Sequence conflict1781S → N in AAF21308. Ref.3
Sequence conflict3021S → G in AAF97867. Ref.1
Sequence conflict3021S → G in AAF64186. Ref.2
Sequence conflict3021S → G in AAF21308. Ref.3
Sequence conflict3021S → G in AAH38393. Ref.4
Sequence conflict3201Y → H in AAF97867. Ref.1
Sequence conflict4741N → D in AAF97867. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JIQ8 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 54650B028417665A

FASTA49053,526
        10         20         30         40         50         60 
MALNSGSPPG IGPCYENHGY QSEHICPPRP PVAPNGYNLY PAQYYPSPVP QYAPRITTQA 

        70         80         90        100        110        120 
STSVIHTHPK SSGALCTSKS KKSLCLALAL GTVLTGAAVA AVLLWRFWDS NCSTSEMECG 

       130        140        150        160        170        180 
SSGTCISSSL WCDGVAHCPN GEDENRCVRL YGQSFILQVY SSQRKAWYPV CQDDWSESYG 

       190        200        210        220        230        240 
RAACKDMGYK NNFYSSQGIP DQSGATSFMK LNVSSGNVDL YKKLYHSDSC SSRMVVSLRC 

       250        260        270        280        290        300 
IECGVRSVKR QSRIVGGLNA SPGDWPWQVS LHVQGVHVCG GSIITPEWIV TAAHCVEEPL 

       310        320        330        340        350        360 
SSPRYWTAFA GILRQSLMFY GSRHQVEKVI SHPNYDSKTK NNDIALMKLQ TPLAFNDLVK 

       370        380        390        400        410        420 
PVCLPNPGMM LDLDQECWIS GWGATYEKGK TSDVLNAAMV PLIEPSKCNS KYIYNNLITP 

       430        440        450        460        470        480 
AMICAGFLQG SVDSCQGDSG GPLVTLKNGI WWLIGDTSWG SGCAKALRPG VYGNVTVFTD 

       490 
WIYQQMRANS 

« Hide

References

« Hide 'large scale' references
[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]"Tmprss2 is essential for influenza H1N1 virus pathogenesis in mice."
Hatesuer B., Bertram S., Mehnert N., Bahgat M.M., Nelson P.S., Poehlman S., Schughart K.
PLoS Pathog. 9:E1003774-E1003774(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The host protease TMPRSS2 plays a major role for in vivo replication of emerging H7N9 and seasonal influenza viruses."
Sakai K., Ami Y., Tahara M., Kubota T., Anraku M., Abe M., Nakajima N., Sekizuka T., Shirato K., Suzaki Y., Ainai A., Nakatsu Y., Kanou K., Nakamura K., Suzuki T., Komase K., Nobusawa E., Maenaka K. expand/collapse author list , Kuroda M., Hasegawa H., Kawaoka Y., Tashiro M., Takeda M.
J. Virol. 88:5608-5616(2014) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS37417.1.
RefSeqNP_056590.2. NM_015775.2.
XP_006523127.1. XM_006523064.1.
XP_006523128.1. XM_006523065.1.
UniGeneMm.276145.

3D structure databases

ProteinModelPortalQ9JIQ8.
SMRQ9JIQ8. Positions 157-490.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.247.

PTM databases

PhosphoSiteQ9JIQ8.

Proteomic databases

PRIDEQ9JIQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000395; ENSMUSP00000000395; ENSMUSG00000000385.
GeneID50528.
KEGGmmu:50528.
UCSCuc008adl.1. mouse.

Organism-specific databases

CTD7113.
MGIMGI:1354381. Tmprss2.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00730000110467.
HOGENOMHOG000251822.
HOVERGENHBG013304.
InParanoidQ7TN04.
KOK09633.
OMAKSWHPVC.
OrthoDBEOG75B84T.
TreeFamTF351678.

Gene expression databases

BgeeQ9JIQ8.
CleanExMM_TMPRSS2.
GenevestigatorQ9JIQ8.

Family and domain databases

Gene3D3.10.250.10. 1 hit.
4.10.400.10. 1 hit.
InterProIPR023415. 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]
PfamPF00057. Ldl_recept_a. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00192. LDLa. 1 hit.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 1 hit.
PROSITEPS01209. 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]
ProtoNetSearch...

Other

NextBio307534.
PROQ9JIQ8.
SOURCESearch...

Entry information

Entry nameTMPS2_MOUSE
AccessionPrimary (citable) accession number: Q9JIQ8
Secondary accession number(s): Q7TN04, Q9JKC4, Q9QY82
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 131 of the entry and version 3 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