TM11A_MOUSE
ID TM11A_MOUSE Reviewed; 389 AA.
AC Q3UQ41;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transmembrane protease serine 11A;
DE EC=3.4.21.-;
DE AltName: Full=Airway trypsin-like protease 1;
DE AltName: Full=Serine protease DESC3;
DE Short=DESC-3;
GN Name=Tmprss11a; Synonyms=Desc3, Gm7, Hatl1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [2]
RP IDENTIFICATION.
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 [3]
RP POSSIBLE FUNCTION.
RX PubMed=16380648; DOI=10.1177/153537020623100110;
RA Zhao N., Huang G., Guo L., Lu S.-H.;
RT "ECRG1, a novel candidate of tumor suppressor gene in the esophageal
RT carcinoma, triggers a senescent program in NIH3T3 cells.";
RL Exp. Biol. Med. 231:84-90(2006).
CC -!- FUNCTION: Probable serine protease which may play a role in cellular
CC senescence. Overexpression inhibits cell growth and induce G1 cell
CC cycle arrest.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AK142820; BAE25202.1; -; mRNA.
DR CCDS; CCDS51531.1; -.
DR RefSeq; NP_001028405.1; NM_001033233.2.
DR AlphaFoldDB; Q3UQ41; -.
DR SMR; Q3UQ41; -.
DR BioGRID; 228795; 8.
DR STRING; 10090.ENSMUSP00000098634; -.
DR MEROPS; S01.292; -.
DR GlyGen; Q3UQ41; 1 site.
DR PhosphoSitePlus; Q3UQ41; -.
DR PaxDb; Q3UQ41; -.
DR PRIDE; Q3UQ41; -.
DR ProteomicsDB; 259212; -.
DR Antibodypedia; 57609; 83 antibodies from 20 providers.
DR DNASU; 194597; -.
DR Ensembl; ENSMUST00000101073; ENSMUSP00000098634; ENSMUSG00000072845.
DR GeneID; 194597; -.
DR KEGG; mmu:194597; -.
DR UCSC; uc008xxq.1; mouse.
DR CTD; 339967; -.
DR MGI; MGI:2684853; Tmprss11a.
DR VEuPathDB; HostDB:ENSMUSG00000072845; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161698; -.
DR HOGENOM; CLU_006842_19_0_1; -.
DR InParanoid; Q3UQ41; -.
DR OMA; DIKSGMF; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q3UQ41; -.
DR TreeFam; TF351684; -.
DR BioGRID-ORCS; 194597; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q3UQ41; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3UQ41; protein.
DR Bgee; ENSMUSG00000072845; Expressed in conjunctival fornix and 39 other tissues.
DR Genevisible; Q3UQ41; MM.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell cycle; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..389
FT /note="Transmembrane protease serine 11A"
FT /id="PRO_0000299318"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..389
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 31..148
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 158..388
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 308..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 335..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 389 AA; 43605 MW; 1203DE9DADE964F9 CRC64;
MEVAGYGTHN RDLKQWMVTL LSALSLMMVV VTIGLLALFL VFDIQVNSNS GQKSSNQLKD
LQETNENLVD EIFIDSALNN RYIKNHVVGL TPEEDDTKAD IVMVFQPPAT GRRTVGKKTH
HSILDQKTRN ARALPADVSL VQVKDCGKRA IPLIANRIVS GNPAAKGAWP WQVSLQRSNI
HQCGGTLIGN MWVVTAAHCF RTNSNPRQWT LSFGTTINPP LMKRDVRRII MHERYRPPAR
DHDIALVQFS PRVTFSDEVR RICLPEPSAS FPPNSTVYIT GFGALYYGGE SQNELREARV
QIISNDICKK RHVYGNEIKR GMFCAGFLEG NYDACRGDSG GPLVIRDNKD TWYLIGIVSW
GDNCGQKNKP GVYTQVTYYR HWIASKTGL
