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Protein

Transmembrane protease serine 11E

Gene

Tmprss11e

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

Functioni

Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position.1 Publication

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321Charge relay systemBy similarity
Active sitei277 – 2771Charge relay systemBy similarity
Active sitei373 – 3731Charge relay systemBy similarity

GO - Molecular functioni

  • serine-type endopeptidase activity Source: InterPro
  • serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  • cognition Source: MGI
  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.021.

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane protease serine 11E (EC:3.4.21.-)
Alternative name(s):
Serine protease DESC1
Cleaved into the following 2 chains:
Gene namesi
Name:Tmprss11e
Synonyms:Desc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:3513175. Tmprss11e.

Subcellular locationi

Chain Transmembrane protease serine 11E catalytic chain :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1818CytoplasmicSequence analysisAdd
BLAST
Transmembranei19 – 3921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini40 – 423384ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191Transmembrane protease serine 11E non-catalytic chainSequence analysisPRO_0000027893Add
BLAST
Chaini192 – 423232Transmembrane protease serine 11E catalytic chainSequence analysisPRO_0000027894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence analysis
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi176 ↔ 297Interchain (between non-catalytic and catalytic chains)PROSITE-ProRule annotation
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence analysis
Disulfide bondi217 ↔ 233PROSITE-ProRule annotation
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence analysis
Disulfide bondi342 ↔ 358PROSITE-ProRule annotation
Disulfide bondi369 ↔ 398PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ5S248.
PRIDEiQ5S248.

PTM databases

iPTMnetiQ5S248.
PhosphoSiteiQ5S248.

Expressioni

Tissue specificityi

Expressed in epidermal, oral and male reproductive tissues.1 Publication

Gene expression databases

BgeeiQ5S248.
CleanExiMM_TMPRSS11E.
GenevisibleiQ5S248. MM.

Interactioni

Subunit structurei

Forms a heterodimer with SERPINA5 and SERPINE1.

Binary interactionsi

WithEntry#Exp.IntActNotes
Serpina5P704582EBI-490889,EBI-490966
Serpine1P227772EBI-490889,EBI-490898

Protein-protein interaction databases

BioGridi232483. 2 interactions.
IntActiQ5S248. 2 interactions.
STRINGi10090.ENSMUSP00000124534.

Structurei

3D structure databases

ProteinModelPortaliQ5S248.
SMRiQ5S248. Positions 47-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 166119SEAPROSITE-ProRule annotationAdd
BLAST
Domaini192 – 422231Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251823.
HOVERGENiHBG013304.
InParanoidiQ5S248.
KOiK09642.
OMAiAHMLLIF.
OrthoDBiEOG75B84T.
TreeFamiTF351684.

Family and domain databases

Gene3Di3.30.70.960. 1 hit.
InterProiIPR017329. Pept_S1A_HAT/DESC1.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF037941. TMPRSS11ABCDE. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF82671. SSF82671. 1 hit.
PROSITEiPS50024. SEA. 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.

Q5S248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRSCVVRAR KRTCVEPWVI GIISFLSLIV LAVCIGLTVH YVRYNHRRTY
60 70 80 90 100
NYYSTLSFTS DKLYSEFGRE ASKNFTEMSQ RIETMVKHAF HKSPLRGQLV
110 120 130 140 150
KAHIIKFSKE DDGVLAHMLL IFRIRSTEDP ETVHKIIEYV LHEKLKYATG
160 170 180 190 200
PPNVDPESVK IKKINKTESD NYFNHCCGTR RNKSTVQTSV RIVGGTPVEE
210 220 230 240 250
EEWPWQSSLR WDGSHRCGAT LINNTWLVTA AHCFRTHKDP SRWSATFGAT
260 270 280 290 300
LQPRKLTTGI RRIIVHEKYK YPSHDYDIAL AELSKPVPCT NAVHKVCLPD
310 320 330 340 350
ANHEFQPGQR MFVTGFGALK NDGFTQNNLR QVQVDYIDTQ TCNQPQSYNG
360 370 380 390 400
AITPRMLCAG FLKGEKDACQ GDSGGPLVTA DVRDIWYLAG VVSWGDECGQ
410 420
PNKPGVYTRV TAFRHWIASN TGI
Length:423
Mass (Da):48,065
Last modified:June 28, 2011 - v2
Checksum:iD71BF4F0283BB896
GO

Sequence cautioni

The sequence AAV52922.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY787860 mRNA. Translation: AAV52922.1. Different initiation.
AK037235 mRNA. Translation: BAC29770.1.
BC115432 mRNA. Translation: AAI15433.1.
BC115433 mRNA. Translation: AAI15434.1.
CCDSiCCDS51533.1.
RefSeqiNP_766468.1. NM_172880.2.
UniGeneiMm.130801.

Genome annotation databases

EnsembliENSMUST00000161306; ENSMUSP00000124534; ENSMUSG00000054537.
GeneIDi243084.
KEGGimmu:243084.
UCSCiuc008xxv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY787860 mRNA. Translation: AAV52922.1. Different initiation.
AK037235 mRNA. Translation: BAC29770.1.
BC115432 mRNA. Translation: AAI15433.1.
BC115433 mRNA. Translation: AAI15434.1.
CCDSiCCDS51533.1.
RefSeqiNP_766468.1. NM_172880.2.
UniGeneiMm.130801.

3D structure databases

ProteinModelPortaliQ5S248.
SMRiQ5S248. Positions 47-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232483. 2 interactions.
IntActiQ5S248. 2 interactions.
STRINGi10090.ENSMUSP00000124534.

Protein family/group databases

MEROPSiS01.021.

PTM databases

iPTMnetiQ5S248.
PhosphoSiteiQ5S248.

Proteomic databases

PaxDbiQ5S248.
PRIDEiQ5S248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000161306; ENSMUSP00000124534; ENSMUSG00000054537.
GeneIDi243084.
KEGGimmu:243084.
UCSCiuc008xxv.1. mouse.

Organism-specific databases

CTDi28983.
MGIiMGI:3513175. Tmprss11e.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000251823.
HOVERGENiHBG013304.
InParanoidiQ5S248.
KOiK09642.
OMAiAHMLLIF.
OrthoDBiEOG75B84T.
TreeFamiTF351684.

Miscellaneous databases

PROiQ5S248.
SOURCEiSearch...

Gene expression databases

BgeeiQ5S248.
CleanExiMM_TMPRSS11E.
GenevisibleiQ5S248. MM.

Family and domain databases

Gene3Di3.30.70.960. 1 hit.
InterProiIPR017329. Pept_S1A_HAT/DESC1.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF037941. TMPRSS11ABCDE. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF82671. SSF82671. 1 hit.
PROSITEiPS50024. SEA. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes."
    Hobson J.P., Netzel-Arnett S., Szabo R., Rehault S.M., Church F.C., Strickland D.K., Lawrence D.A., Antalis T.M., Bugge T.H.
    J. Biol. Chem. 279:46981-46994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HETERODIMER WITH SERPINE1 AND SERPINA5, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: C57BL/6JImported.
  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: Skin.
  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].

Entry informationi

Entry nameiTM11E_MOUSE
AccessioniPrimary (citable) accession number: Q5S248
Secondary accession number(s): A4FUP5, Q8BM10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 28, 2011
Last modified: June 8, 2016
This is version 103 of the entry and version 2 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.