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Protein

Transmembrane protease serine 2

Gene

Tmprss2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei294Charge relay systemBy similarity1
Active sitei343Charge relay systemBy similarity1
Active sitei439Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1354381. Tmprss2.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type II membrane protein By similarity
Chain Transmembrane protease serine 2 catalytic chain :
  • Secreted By similarity

  • Note: Activated by cleavage and secreted.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 83CytoplasmicSequence analysisAdd BLAST83
Transmembranei84 – 104Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini105 – 490ExtracellularSequence analysisAdd BLAST386

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000278571 – 253Transmembrane protease serine 2 non-catalytic chainAdd BLAST253
ChainiPRO_0000027858254 – 490Transmembrane protease serine 2 catalytic chainAdd BLAST237

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi111N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi112 ↔ 125By similarity
Disulfide bondi119 ↔ 138By similarity
Disulfide bondi132 ↔ 147By similarity
Disulfide bondi171 ↔ 230By similarity
Disulfide bondi184 ↔ 240By similarity
Glycosylationi212N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi243 ↔ 363Interchain (between non-catalytic and catalytic chains)PROSITE-ProRule annotation
Disulfide bondi279 ↔ 295By similarity
Disulfide bondi408 ↔ 424By similarity
Disulfide bondi435 ↔ 463By similarity
Glycosylationi474N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Proteolytically processed; by an autocatalytic mechanism.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei253 – 254CleavageSequence analysis2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ9JIQ8.
PaxDbiQ9JIQ8.
PRIDEiQ9JIQ8.

PTM databases

iPTMnetiQ9JIQ8.
PhosphoSitePlusiQ9JIQ8.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000000385.
CleanExiMM_TMPRSS2.
GenevisibleiQ9JIQ8. MM.

Interactioni

Subunit structurei

The catalytically active form interacts with ACE2.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000395.

Structurei

3D structure databases

ProteinModelPortaliQ9JIQ8.
SMRiQ9JIQ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini111 – 149LDL-receptor class APROSITE-ProRule annotationAdd BLAST39
Domaini150 – 242SRCRPROSITE-ProRule annotationAdd BLAST93
Domaini254 – 487Peptidase S1PROSITE-ProRule annotationAdd BLAST234

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

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251822.
HOVERGENiHBG013304.
InParanoidiQ9JIQ8.
KOiK09633.
OMAiKSWHPVC.
OrthoDBiEOG091G0DF7.
TreeFamiTF351678.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di3.10.250.10. 1 hit.
4.10.400.10. 1 hit.
InterProiIPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF15494. SRCR_2. 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)DescriptionActionsGraphical viewLength
Sequence conflicti75L → P in AAF97867 (PubMed:11169526).Curated1
Sequence conflicti75L → P in AAF64186 (Ref. 2) Curated1
Sequence conflicti75L → P in AAF21308 (PubMed:10683448).Curated1
Sequence conflicti75L → P in AAH38393 (PubMed:15489334).Curated1
Sequence conflicti122S → L in AAF21308 (PubMed:10683448).Curated1
Sequence conflicti178S → N in AAF21308 (PubMed:10683448).Curated1
Sequence conflicti302S → G in AAF97867 (PubMed:11169526).Curated1
Sequence conflicti302S → G in AAF64186 (Ref. 2) Curated1
Sequence conflicti302S → G in AAF21308 (PubMed:10683448).Curated1
Sequence conflicti302S → G in AAH38393 (PubMed:15489334).Curated1
Sequence conflicti320Y → H in AAF97867 (PubMed:11169526).Curated1
Sequence conflicti474N → D in AAF97867 (PubMed:11169526).Curated1

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_006523064.3.
XP_006523128.1. XM_006523065.2.
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.
CCDSiCCDS37417.1.
RefSeqiNP_056590.2. NM_015775.2.
XP_006523127.1. XM_006523064.3.
XP_006523128.1. XM_006523065.2.
UniGeneiMm.276145.

3D structure databases

ProteinModelPortaliQ9JIQ8.
SMRiQ9JIQ8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000395.

Protein family/group databases

MEROPSiS01.247.

PTM databases

iPTMnetiQ9JIQ8.
PhosphoSitePlusiQ9JIQ8.

Proteomic databases

MaxQBiQ9JIQ8.
PaxDbiQ9JIQ8.
PRIDEiQ9JIQ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7113.
MGIiMGI:1354381. Tmprss2.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251822.
HOVERGENiHBG013304.
InParanoidiQ9JIQ8.
KOiK09633.
OMAiKSWHPVC.
OrthoDBiEOG091G0DF7.
TreeFamiTF351678.

Miscellaneous databases

ChiTaRSiTmprss2. mouse.
PROiQ9JIQ8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000385.
CleanExiMM_TMPRSS2.
GenevisibleiQ9JIQ8. MM.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di3.10.250.10. 1 hit.
4.10.400.10. 1 hit.
InterProiIPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF15494. SRCR_2. 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]
ProtoNetiSearch...

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 2, 2016
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.