ID TM11G_MOUSE Reviewed; 417 AA.
AC Q8BZ10; Q8BZ04;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Transmembrane protease serine 11G;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease DESC4;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11G non-catalytic chain;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11G catalytic chain;
DE Flags: Precursor;
GN Name=Tmprss11g; Synonyms=Desc4;
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=Vagina;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29676.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK036981; BAC29657.1; -; mRNA.
DR EMBL; AK037029; BAC29676.1; ALT_INIT; mRNA.
DR EMBL; AC103930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51532.1; -.
DR RefSeq; NP_796136.2; NM_177162.4.
DR AlphaFoldDB; Q8BZ10; -.
DR SMR; Q8BZ10; -.
DR STRING; 10090.ENSMUSP00000122709; -.
DR MEROPS; S01.436; -.
DR GlyCosmos; Q8BZ10; 1 site, No reported glycans.
DR GlyGen; Q8BZ10; 1 site.
DR PaxDb; 10090-ENSMUSP00000122709; -.
DR ProteomicsDB; 259217; -.
DR DNASU; 320454; -.
DR Ensembl; ENSMUST00000134179.8; ENSMUSP00000122709.2; ENSMUSG00000079451.10.
DR GeneID; 320454; -.
DR KEGG; mmu:320454; -.
DR UCSC; uc008xxr.2; mouse.
DR AGR; MGI:2444058; -.
DR CTD; 320454; -.
DR MGI; MGI:2444058; Tmprss11g.
DR VEuPathDB; HostDB:ENSMUSG00000079451; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000163094; -.
DR InParanoid; Q8BZ10; -.
DR OMA; AFDQKFY; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; Q8BZ10; -.
DR TreeFam; TF351684; -.
DR BioGRID-ORCS; 320454; 2 hits in 79 CRISPR screens.
DR PRO; PR:Q8BZ10; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BZ10; Protein.
DR Bgee; ENSMUSG00000079451; Expressed in esophagus and 23 other cell types or tissues.
DR ExpressionAtlas; Q8BZ10; baseline and differential.
DR Genevisible; Q8BZ10; MM.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
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; SSF82671; SEA domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..185
FT /note="Transmembrane protease serine 11G non-catalytic
FT chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027837"
FT CHAIN 186..417
FT /note="Transmembrane protease serine 11G catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027838"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 46..165
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 186..416
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P10144"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P10144"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P10144"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 211..227
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 336..352
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 363..392
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 52
FT /note="A -> V (in Ref. 1; BAC29657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46614 MW; CD3D36219EA5A8D5 CRC64;
MYQPGILVRR KRVWKPWTVA LITVALLLAL AVLIGLLVYF LVYDEKTHYY QASFWIPSIN
YSSDLSKEQS KFRTGLKQKI SNEIDVIFQR SSLKHHYVKS QVVNFRPSND GVKADVLIKF
QIPRKNAGTL KRQADNILQE KLQSSQSILK RDASLPYLRE MNAAQAEHIL NSDCGSGMEY
PPIARIADGK PADKASWPWQ SSLQVEGIHL CGASLIGSQW LVTSAHCFDN YKNPKLWTVS
FGRTLSSPLT TRKVESIIVH ENYASHKHDD DIAVVKLSSP VLFSENLHRV CLPDATFQVL
PKSKVFVTGW GALKANGPFP NSLQEVEIEI ISNDVCNQVN VYGGAISSGM ICAGFLTGKL
DACEGDSGGP LVISDNRNKW YLLGIVSWGI DCGKENKPGI YTRVTHYRDW IKSKTSI
//
