TM11E_MOUSE
ID TM11E_MOUSE Reviewed; 423 AA.
AC Q5S248; A4FUP5; Q8BM10;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Transmembrane protease serine 11E;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease DESC1;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11E non-catalytic chain;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11E catalytic chain;
DE Flags: Precursor;
GN Name=Tmprss11e; Synonyms=Desc1;
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], FUNCTION, HETERODIMER WITH SERPINE1 AND
RP SERPINA5, GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAV52922.1};
RX PubMed=15328353; DOI=10.1074/jbc.m403299200;
RA Hobson J.P., Netzel-Arnett S., Szabo R., Rehault S.M., Church F.C.,
RA Strickland D.K., Lawrence D.A., Antalis T.M., Bugge T.H.;
RT "Mouse DESC1 is located within a cluster of seven DESC1-like genes and
RT encodes a type II transmembrane serine protease that forms serpin
RT inhibitory complexes.";
RL J. Biol. Chem. 279:46981-46994(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Serine protease which possesses both gelatinolytic and
CC caseinolytic activities. Shows a preference for Arg in the P1 position.
CC {ECO:0000269|PubMed:15328353}.
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SERPINA5 and SERPINE1.
CC -!- INTERACTION:
CC Q5S248; P70458: Serpina5; NbExp=2; IntAct=EBI-490889, EBI-490966;
CC Q5S248; P22777: Serpine1; NbExp=2; IntAct=EBI-490889, EBI-490898;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15328353};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:15328353}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protease serine 11E catalytic
CC chain]: Secreted {ECO:0000269|PubMed:15328353}. Note=Activated by
CC cleavage and secreted. {ECO:0000269|PubMed:15328353}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermal, oral and male reproductive
CC tissues. {ECO:0000269|PubMed:15328353}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15328353}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV52922.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY787860; AAV52922.1; ALT_INIT; mRNA.
DR EMBL; AK037235; BAC29770.1; -; mRNA.
DR EMBL; BC115432; AAI15433.1; -; mRNA.
DR EMBL; BC115433; AAI15434.1; -; mRNA.
DR CCDS; CCDS51533.1; -.
DR RefSeq; NP_766468.1; NM_172880.2.
DR AlphaFoldDB; Q5S248; -.
DR SMR; Q5S248; -.
DR BioGRID; 232483; 4.
DR IntAct; Q5S248; 2.
DR STRING; 10090.ENSMUSP00000124534; -.
DR MEROPS; S01.021; -.
DR GlyGen; Q5S248; 4 sites.
DR iPTMnet; Q5S248; -.
DR PhosphoSitePlus; Q5S248; -.
DR PaxDb; Q5S248; -.
DR PRIDE; Q5S248; -.
DR ProteomicsDB; 259216; -.
DR Antibodypedia; 57640; 150 antibodies from 20 providers.
DR DNASU; 243084; -.
DR Ensembl; ENSMUST00000161306; ENSMUSP00000124534; ENSMUSG00000054537.
DR GeneID; 243084; -.
DR KEGG; mmu:243084; -.
DR UCSC; uc008xxv.1; mouse.
DR CTD; 28983; -.
DR MGI; MGI:3513175; Tmprss11e.
DR VEuPathDB; HostDB:ENSMUSG00000054537; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161786; -.
DR HOGENOM; CLU_006842_19_0_1; -.
DR InParanoid; Q5S248; -.
DR OMA; HCFRTYK; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q5S248; -.
DR TreeFam; TF351684; -.
DR BioGRID-ORCS; 243084; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q5S248; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q5S248; protein.
DR Bgee; ENSMUSG00000054537; Expressed in tail skin and 18 other tissues.
DR Genevisible; Q5S248; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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 Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Secreted; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..191
FT /note="Transmembrane protease serine 11E non-catalytic
FT chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027893"
FT CHAIN 192..423
FT /note="Transmembrane protease serine 11E catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027894"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 48..166
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 192..422
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 373
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 176..297
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 217..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 342..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 369..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 423 AA; 48065 MW; D71BF4F0283BB896 CRC64;
MYRSCVVRAR KRTCVEPWVI GIISFLSLIV LAVCIGLTVH YVRYNHRRTY NYYSTLSFTS
DKLYSEFGRE ASKNFTEMSQ RIETMVKHAF HKSPLRGQLV KAHIIKFSKE DDGVLAHMLL
IFRIRSTEDP ETVHKIIEYV LHEKLKYATG PPNVDPESVK IKKINKTESD NYFNHCCGTR
RNKSTVQTSV RIVGGTPVEE EEWPWQSSLR WDGSHRCGAT LINNTWLVTA AHCFRTHKDP
SRWSATFGAT LQPRKLTTGI RRIIVHEKYK YPSHDYDIAL AELSKPVPCT NAVHKVCLPD
ANHEFQPGQR MFVTGFGALK NDGFTQNNLR QVQVDYIDTQ TCNQPQSYNG AITPRMLCAG
FLKGEKDACQ GDSGGPLVTA DVRDIWYLAG VVSWGDECGQ PNKPGVYTRV TAFRHWIASN
TGI
