TM11D_MOUSE
ID TM11D_MOUSE Reviewed; 417 AA.
AC Q8VHK8; Q7TNX3; Q8VDV1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transmembrane protease serine 11D;
DE EC=3.4.21.-;
DE AltName: Full=Adrenal secretory serine protease;
DE Short=AsP;
DE AltName: Full=Airway trypsin-like protease;
DE Short=AT;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11D non-catalytic chain;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11D catalytic chain;
DE Flags: Precursor;
GN Name=Tmprss11d; Synonyms=Mat;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=Czech II; TISSUE=Tongue, and Trachea;
RX PubMed=14691009; DOI=10.1210/en.2003-0930;
RA Hansen I.A., Fassnacht M., Hahner S., Hammer F., Schammann M., Meyer S.R.,
RA Bicknell A.B., Allolio B.;
RT "The adrenal secretory serine protease AsP is a short secretory isoform of
RT the transmembrane airway trypsin-like protease.";
RL Endocrinology 145:1898-1905(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Eguchi H., Yamamura S., Yamaoka K., Masegi T., Kamimura T., Yasuoka S.;
RT "Molecular cloning and expression of murine homologue of human airway
RT trypsin-like protease gene.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=24227843; DOI=10.1128/jvi.02202-13;
RA Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O.,
RA Poehlmann S.;
RT "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by
RT TMPRSS2 augments entry driven by the severe acute respiratory syndrome
RT coronavirus spike protein.";
RL J. Virol. 88:1293-1307(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 44-164.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of SEA domain of transmembrane protease from Mus
RT musculus.";
RL Submitted (JUL-2007) to the PDB data bank.
CC -!- FUNCTION: May play some biological role in the host defense system on
CC the mucous membrane independently of or in cooperation with other
CC substances in airway mucous or bronchial secretions. Preferentially
CC cleaves the C-terminal side of arginine residues at the P1 position of
CC certain peptides (By similarity). Plays a role in the proteolytic
CC processing of ACE2. Isoform 2 may play a key role in regulating adrenal
CC proliferation by specifically cleaving N-POMC. {ECO:0000250,
CC ECO:0000269|PubMed:24227843}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protease serine 11D catalytic
CC chain]: Secreted {ECO:0000250}. Note=Activated by cleavage and
CC secreted. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=MAT1;
CC IsoId=Q8VHK8-1; Sequence=Displayed;
CC Name=2; Synonyms=MAT2;
CC IsoId=Q8VHK8-2; Sequence=VSP_014519, VSP_014520;
CC -!- TISSUE SPECIFICITY: Highly expressed in the esophagus, tongue, and
CC trachea, low expression was seen in heart, lung, and adrenal gland.
CC Isoform 2 is also highly expressed in the adrenal gland.
CC {ECO:0000269|PubMed:14691009}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF448809; AAL47139.1; -; mRNA.
DR EMBL; AF539752; AAP97729.1; -; mRNA.
DR EMBL; AB053953; BAD89353.1; -; mRNA.
DR EMBL; BC020151; AAH20151.1; -; mRNA.
DR CCDS; CCDS39124.1; -. [Q8VHK8-1]
DR RefSeq; NP_663536.1; NM_145561.2. [Q8VHK8-1]
DR PDB; 2E7V; X-ray; 1.92 A; A=44-164.
DR PDBsum; 2E7V; -.
DR AlphaFoldDB; Q8VHK8; -.
DR SMR; Q8VHK8; -.
DR STRING; 10090.ENSMUSP00000031175; -.
DR PaxDb; Q8VHK8; -.
DR PRIDE; Q8VHK8; -.
DR ProteomicsDB; 259214; -. [Q8VHK8-1]
DR ProteomicsDB; 259215; -. [Q8VHK8-2]
DR Antibodypedia; 12680; 157 antibodies from 28 providers.
DR DNASU; 231382; -.
DR Ensembl; ENSMUST00000031175; ENSMUSP00000031175; ENSMUSG00000061259. [Q8VHK8-1]
DR Ensembl; ENSMUST00000122377; ENSMUSP00000113079; ENSMUSG00000061259. [Q8VHK8-2]
DR GeneID; 231382; -.
DR KEGG; mmu:231382; -.
DR UCSC; uc008xxo.1; mouse. [Q8VHK8-2]
DR UCSC; uc008xxp.1; mouse. [Q8VHK8-1]
DR CTD; 9407; -.
DR MGI; MGI:2385221; Tmprss11d.
DR VEuPathDB; HostDB:ENSMUSG00000061259; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161719; -.
DR HOGENOM; CLU_006842_19_0_1; -.
DR InParanoid; Q8VHK8; -.
DR OMA; WGYQCGV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8VHK8; -.
DR TreeFam; TF351684; -.
DR BioGRID-ORCS; 231382; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Tmprss11d; mouse.
DR EvolutionaryTrace; Q8VHK8; -.
DR PRO; PR:Q8VHK8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VHK8; protein.
DR Bgee; ENSMUSG00000061259; Expressed in esophagus and 14 other tissues.
DR Genevisible; Q8VHK8; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; ISO:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.960; -; 1.
DR InterPro; IPR017329; Pept_S1A_HAT/DESC1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF037941; TMPRSS11ABCDE; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF82671; SSF82671; 1.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Hydrolase; Membrane; Protease; Reference proteome; Secreted;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zymogen.
FT CHAIN 1..185
FT /note="Transmembrane protease serine 11D non-catalytic
FT chain"
FT /id="PRO_0000027887"
FT CHAIN 186..417
FT /note="Transmembrane protease serine 11D catalytic chain"
FT /id="PRO_0000027888"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 46..162
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 186..417
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 172..291
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 211..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 336..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 363..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14691009"
FT /id="VSP_014519"
FT VAR_SEQ 139..158
FT /note="LRRLSSSGNLEIAPSNEITS -> MIFSFCFVDFVLTFSFLMIA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14691009"
FT /id="VSP_014520"
FT CONFLICT 43
FT /note="F -> L (in Ref. 1; AAL47139)"
FT /evidence="ECO:0000305"
FT STRAND 46..60
FT /evidence="ECO:0007829|PDB:2E7V"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2E7V"
FT HELIX 71..89
FT /evidence="ECO:0007829|PDB:2E7V"
FT TURN 92..96
FT /evidence="ECO:0007829|PDB:2E7V"
FT STRAND 97..108
FT /evidence="ECO:0007829|PDB:2E7V"
FT STRAND 111..122
FT /evidence="ECO:0007829|PDB:2E7V"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:2E7V"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2E7V"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:2E7V"
SQ SEQUENCE 417 AA; 46254 MW; C7FACD21C06FEAEA CRC64;
MYRPRPMLSP SRFFTPFAVA FVVIITVGLL AMMAGLLIHF LAFDKKAYFY HSSFQILNVE
YTEALNSPAT HEYRTLSERI EAMITDEFRG SSLKSEFIRT HVVKLRKEGT GVVADVVMKF
RSSKRNNRKV MKTRIQSVLR RLSSSGNLEI APSNEITSLT DQDTENVLTQ ECGARPDLIT
LSEERIIGGM QAEPGDWPWQ VSLQLNNVHH CGGALISNMW VLTAAHCFKS YPNPQYWTAT
FGVSTMSPRL RVRVRAILAH DGYSSVTRDN DIAVVQLDRS VAFSRNIHRV CLPAATQNII
PGSVAYVTGW GSLTYGGNAV TNLRQGEVRI ISSEECNTPA GYSGSVLPGM LCAGMRSGAV
DACQGDSGGP LVQEDSRRLW FVVGIVSWGY QCGLPNKPGV YTRVTAYRNW IRQQTGI
