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Transmembrane protease serine 11D (EC 3.4.21.-) (Airway trypsin-like protease) [Cleaved into: Transmembrane protease serine 11D non-catalytic chain; Transmembrane protease serine 11D catalytic chain]

 TM11D_HUMAN             Reviewed;         418 AA.
O60235; Q08AF6;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 149.
RecName: Full=Transmembrane protease serine 11D;
EC=3.4.21.-;
AltName: Full=Airway trypsin-like protease;
Contains:
RecName: Full=Transmembrane protease serine 11D non-catalytic chain;
Contains:
RecName: Full=Transmembrane protease serine 11D catalytic chain;
Flags: Precursor;
Name=TMPRSS11D; Synonyms=HAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9565616; DOI=10.1074/jbc.273.19.11895;
Yamaoka K., Masuda K., Ogawa H., Takagi K., Umemoto N., Yasuoka S.;
"Cloning and characterization of the cDNA for human airway trypsin-
like protease.";
J. Biol. Chem. 273:11895-11901(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 187-206, AND CHARACTERIZATION.
PubMed=9070615; DOI=10.1165/ajrcmb.16.3.9070615;
Yasuoka S., Ohnishi T., Kawano S., Tsuchihashi S., Ogawara M.,
Masuda K., Yamaoka K., Takahashi M., Sano T.;
"Purification, characterization, and localization of a novel trypsin-
like protease found in the human airway.";
Am. J. Respir. Cell Mol. Biol. 16:300-308(1997).
[4]
FUNCTION.
PubMed=23536651; DOI=10.1128/JVI.03372-12;
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.;
"TMPRSS2 activates the human coronavirus 229E for cathepsin-
independent host cell entry and is expressed in viral target cells in
the respiratory epithelium.";
J. Virol. 87:6150-6160(2013).
[5]
FUNCTION.
PubMed=24227843; DOI=10.1128/JVI.02202-13;
Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O.,
Poehlmann S.;
"TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by
TMPRSS2 augments entry driven by the severe acute respiratory syndrome
coronavirus spike protein.";
J. Virol. 88:1293-1307(2014).
-!- FUNCTION: 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. 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.
{ECO:0000269|PubMed:23536651, ECO:0000269|PubMed:24227843}.
-!- ENZYME REGULATION: Strongly inhibited by diisopropyl
fluorophosphate, leupeptin, antipain, aprotinin, and soybean
trypsin inhibitor, but hardly inhibited by secretory leukocyte
protease inhibitor at 10 microM.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein. Note=Activated by cleavage and secreted.
-!- SUBCELLULAR LOCATION: Transmembrane protease serine 11D catalytic
chain: Secreted. Note=Activated by cleavage and secreted.
-!- TISSUE SPECIFICITY: Located in the cells of the submucosal serous
glands of the bronchi and trachea.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; AB002134; BAA28691.1; -; mRNA.
EMBL; BC125195; AAI25196.1; -; mRNA.
EMBL; BC125196; AAI25197.1; -; mRNA.
CCDS; CCDS3518.1; -.
RefSeq; NP_004253.1; NM_004262.2.
UniGene; Hs.132195; -.
ProteinModelPortal; O60235; -.
IntAct; O60235; 2.
MINT; MINT-8302106; -.
STRING; 9606.ENSP00000283916; -.
BindingDB; O60235; -.
ChEMBL; CHEMBL1795138; -.
GuidetoPHARMACOLOGY; 2420; -.
MEROPS; S01.047; -.
BioMuta; TMPRSS11D; -.
MaxQB; O60235; -.
PaxDb; O60235; -.
PeptideAtlas; O60235; -.
PRIDE; O60235; -.
Ensembl; ENST00000283916; ENSP00000283916; ENSG00000153802.
GeneID; 9407; -.
KEGG; hsa:9407; -.
UCSC; uc003hdq.4; human.
CTD; 9407; -.
DisGeNET; 9407; -.
EuPathDB; HostDB:ENSG00000153802.11; -.
GeneCards; TMPRSS11D; -.
HGNC; HGNC:24059; TMPRSS11D.
HPA; HPA052834; -.
MIM; 605369; gene.
neXtProt; NX_O60235; -.
OpenTargets; ENSG00000153802; -.
PharmGKB; PA142670728; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00900000140784; -.
HOGENOM; HOG000251823; -.
HOVERGEN; HBG013304; -.
InParanoid; O60235; -.
KO; K09641; -.
OMA; AFDQKSY; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; O60235; -.
TreeFam; TF351684; -.
GeneWiki; TMPRSS11D; -.
GenomeRNAi; 9407; -.
PRO; PR:O60235; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000153802; -.
CleanEx; HS_TMPRSS11D; -.
ExpressionAtlas; O60235; baseline and differential.
Genevisible; O60235; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0007585; P:respiratory gaseous exchange; TAS:ProtInc.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 3.30.70.960; -; 1.
InterPro; IPR017329; Pept_S1A_HAT/DESC1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF01390; SEA; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF037941; TMPRSS11ABCDE; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00200; SEA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF82671; SSF82671; 1.
PROSITE; PS50024; SEA; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
Reference proteome; Secreted; Serine protease; Signal-anchor;
Transmembrane; Transmembrane helix; Zymogen.
CHAIN 1 186 Transmembrane protease serine 11D non-
catalytic chain.
/FTId=PRO_0000027885.
CHAIN 187 418 Transmembrane protease serine 11D
catalytic chain.
/FTId=PRO_0000027886.
TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.
TRANSMEM 21 41 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 42 418 Extracellular. {ECO:0000255}.
DOMAIN 46 163 SEA. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 187 417 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 227 227 Charge relay system. {ECO:0000250}.
ACT_SITE 272 272 Charge relay system. {ECO:0000250}.
ACT_SITE 368 368 Charge relay system. {ECO:0000250}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 173 292 Interchain (between non-catalytic and
catalytic chains). {ECO:0000255|PROSITE-
ProRule:PRU00274}.
DISULFID 212 228 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 337 353 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 364 393 {ECO:0000255|PROSITE-ProRule:PRU00274}.
SEQUENCE 418 AA; 46263 MW; F4BC1DB020CFBBD0 CRC64;
MYRPARVTST SRFLNPYVVC FIVVAGVVIL AVTIALLVYF LAFDQKSYFY RSSFQLLNVE
YNSQLNSPAT QEYRTLSGRI ESLITKTFKE SNLRNQFIRA HVAKLRQDGS GVRADVVMKF
QFTRNNNGAS MKSRIESVLR QMLNNSGNLE INPSTEITSL TDQAAANWLI NECGAGPDLI
TLSEQRILGG TEAEEGSWPW QVSLRLNNAH HCGGSLINNM WILTAAHCFR SNSNPRDWIA
TSGISTTFPK LRMRVRNILI HNNYKSATHE NDIALVRLEN SVTFTKDIHS VCLPAATQNI
PPGSTAYVTG WGAQEYAGHT VPELRQGQVR IISNDVCNAP HSYNGAILSG MLCAGVPQGG
VDACQGDSGG PLVQEDSRRL WFIVGIVSWG DQCGLPDKPG VYTRVTAYLD WIRQQTGI


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