Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O60235

- TM11D_HUMAN

UniProt

O60235 - TM11D_HUMAN

Protein

Transmembrane protease serine 11D

Gene

TMPRSS11D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Proteolytically cleaves and activates the human coronavirus 229E (HCoV-229E) spike glycoprotein which facilitate virus-cell membrane fusions; 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.2 Publications

    Catalytic activityi

    Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides, cleaving Boc-Phe-Ser-Arg-4-methylcoumaryl-7-amide most efficiently and having an optimum pH of 8.6 with this substrate.

    Enzyme regulationi

    Strongly inhibited by diisopropyl fluorophosphate, leupeptin, antipain, aprotinin, and soybean trypsin inhibitor, but hardly inhibited by secretory leukocyte protease inhibitor at 10 microM.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei227 – 2271Charge relay systemBy similarity
    Active sitei272 – 2721Charge relay systemBy similarity
    Active sitei368 – 3681Charge relay systemBy similarity

    GO - Molecular functioni

    1. peptidase activity Source: ProtInc
    2. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. proteolysis Source: UniProtKB
    2. respiratory gaseous exchange Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.047.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transmembrane protease serine 11D (EC:3.4.21.-)
    Alternative name(s):
    Airway trypsin-like protease
    Cleaved into the following 2 chains:
    Gene namesi
    Name:TMPRSS11D
    Synonyms:HAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:24059. TMPRSS11D.

    Subcellular locationi

    Cell membrane; Single-pass type II membrane protein
    Note: Activated by cleavage and secreted.
    Transmembrane protease serine 11D catalytic chain : Secreted
    Note: Activated by cleavage and secreted.

    GO - Cellular componenti

    1. extracellular region Source: ProtInc
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142670728.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 186186Transmembrane protease serine 11D non-catalytic chainPRO_0000027885Add
    BLAST
    Chaini187 – 418232Transmembrane protease serine 11D catalytic chainPRO_0000027886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi173 ↔ 292Interchain (between non-catalytic and catalytic chains)PROSITE-ProRule annotation
    Disulfide bondi212 ↔ 228PROSITE-ProRule annotation
    Disulfide bondi337 ↔ 353PROSITE-ProRule annotation
    Disulfide bondi364 ↔ 393PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiO60235.
    PRIDEiO60235.

    Expressioni

    Tissue specificityi

    Located in the cells of the submucosal serous glands of the bronchi and trachea.

    Gene expression databases

    ArrayExpressiO60235.
    BgeeiO60235.
    CleanExiHS_TMPRSS11D.
    GenevestigatoriO60235.

    Organism-specific databases

    HPAiHPA052834.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    IntActiO60235. 1 interaction.
    MINTiMINT-8302106.
    STRINGi9606.ENSP00000283916.

    Structurei

    3D structure databases

    ProteinModelPortaliO60235.
    SMRiO60235. Positions 45-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini42 – 418377ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 4121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 163118SEAPROSITE-ProRule annotationAdd
    BLAST
    Domaini187 – 417231Peptidase 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

    eggNOGiCOG5640.
    HOGENOMiHOG000251823.
    HOVERGENiHBG013304.
    InParanoidiO60235.
    KOiK09641.
    OMAiSNLRNQF.
    OrthoDBiEOG75B84T.
    PhylomeDBiO60235.
    TreeFamiTF351684.

    Family and domain databases

    Gene3Di3.30.70.960. 1 hit.
    InterProiIPR017329. Pept_S1A_HAT/DESC1.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR000082. SEA_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF01390. SEA. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037941. TMPRSS11ABCDE. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00200. SEA. 1 hit.
    SM00020. 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.

    O60235-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRPARVTST SRFLNPYVVC FIVVAGVVIL AVTIALLVYF LAFDQKSYFY    50
    RSSFQLLNVE YNSQLNSPAT QEYRTLSGRI ESLITKTFKE SNLRNQFIRA 100
    HVAKLRQDGS GVRADVVMKF QFTRNNNGAS MKSRIESVLR QMLNNSGNLE 150
    INPSTEITSL TDQAAANWLI NECGAGPDLI TLSEQRILGG TEAEEGSWPW 200
    QVSLRLNNAH HCGGSLINNM WILTAAHCFR SNSNPRDWIA TSGISTTFPK 250
    LRMRVRNILI HNNYKSATHE NDIALVRLEN SVTFTKDIHS VCLPAATQNI 300
    PPGSTAYVTG WGAQEYAGHT VPELRQGQVR IISNDVCNAP HSYNGAILSG 350
    MLCAGVPQGG VDACQGDSGG PLVQEDSRRL WFIVGIVSWG DQCGLPDKPG 400
    VYTRVTAYLD WIRQQTGI 418
    Length:418
    Mass (Da):46,263
    Last modified:August 1, 1998 - v1
    Checksum:iF4BC1DB020CFBBD0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002134 mRNA. Translation: BAA28691.1.
    BC125195 mRNA. Translation: AAI25196.1.
    BC125196 mRNA. Translation: AAI25197.1.
    CCDSiCCDS3518.1.
    RefSeqiNP_004253.1. NM_004262.2.
    UniGeneiHs.132195.

    Genome annotation databases

    EnsembliENST00000283916; ENSP00000283916; ENSG00000153802.
    GeneIDi9407.
    KEGGihsa:9407.
    UCSCiuc003hdq.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002134 mRNA. Translation: BAA28691.1 .
    BC125195 mRNA. Translation: AAI25196.1 .
    BC125196 mRNA. Translation: AAI25197.1 .
    CCDSi CCDS3518.1.
    RefSeqi NP_004253.1. NM_004262.2.
    UniGenei Hs.132195.

    3D structure databases

    ProteinModelPortali O60235.
    SMRi O60235. Positions 45-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O60235. 1 interaction.
    MINTi MINT-8302106.
    STRINGi 9606.ENSP00000283916.

    Chemistry

    BindingDBi O60235.
    ChEMBLi CHEMBL1795138.

    Protein family/group databases

    MEROPSi S01.047.

    Proteomic databases

    PaxDbi O60235.
    PRIDEi O60235.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000283916 ; ENSP00000283916 ; ENSG00000153802 .
    GeneIDi 9407.
    KEGGi hsa:9407.
    UCSCi uc003hdq.3. human.

    Organism-specific databases

    CTDi 9407.
    GeneCardsi GC04M068686.
    HGNCi HGNC:24059. TMPRSS11D.
    HPAi HPA052834.
    MIMi 605369. gene.
    neXtProti NX_O60235.
    PharmGKBi PA142670728.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251823.
    HOVERGENi HBG013304.
    InParanoidi O60235.
    KOi K09641.
    OMAi SNLRNQF.
    OrthoDBi EOG75B84T.
    PhylomeDBi O60235.
    TreeFami TF351684.

    Miscellaneous databases

    GeneWikii TMPRSS11D.
    GenomeRNAii 9407.
    NextBioi 35242.
    PROi O60235.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60235.
    Bgeei O60235.
    CleanExi HS_TMPRSS11D.
    Genevestigatori O60235.

    Family and domain databases

    Gene3Di 3.30.70.960. 1 hit.
    InterProi IPR017329. Pept_S1A_HAT/DESC1.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR000082. SEA_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF01390. SEA. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037941. TMPRSS11ABCDE. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00200. SEA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF82671. SSF82671. 1 hit.
    PROSITEi PS50024. SEA. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the cDNA for human airway trypsin-like protease."
      Yamaoka K., Masuda K., Ogawa H., Takagi K., Umemoto N., Yasuoka S.
      J. Biol. Chem. 273:11895-11901(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
    3. "Purification, characterization, and localization of a novel trypsin-like protease found in the human airway."
      Yasuoka S., Ohnishi T., Kawano S., Tsuchihashi S., Ogawara M., Masuda K., Yamaoka K., Takahashi M., Sano T.
      Am. J. Respir. Cell Mol. Biol. 16:300-308(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 187-206, CHARACTERIZATION.
    4. "TMPRSS2 activates the human coronavirus 229E for cathepsin-independent host cell entry and is expressed in viral target cells in the respiratory epithelium."
      Bertram S., Dijkman R., Habjan M., Heurich A., Gierer S., Glowacka I., Welsch K., Winkler M., Schneider H., Hofmann-Winkler H., Thiel V., Pohlmann S.
      J. Virol. 87:6150-6160(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "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 nameiTM11D_HUMAN
    AccessioniPrimary (citable) accession number: O60235
    Secondary accession number(s): Q08AF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3