TM11B_MOUSE
ID TM11B_MOUSE Reviewed; 416 AA.
AC Q14C59; Q8BZ13; Q8BZ30;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transmembrane protease serine 11B-like protein;
DE EC=3.4.21.-;
DE AltName: Full=Airway trypsin-like protease 5;
DE AltName: Full=Transmembrane protease serine 11B;
GN Name=Tmprss11b; Synonyms=Hatl5, Tmprss11bnl;
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 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).
RN [3]
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=24498351; DOI=10.1371/journal.pone.0087675;
RA Miller G.S., Zoratti G.L., Murray A.S., Bergum C., Tanabe L.M., List K.;
RT "HATL5: a cell surface serine protease differentially expressed in
RT epithelial cancers.";
RL PLoS ONE 9:E87675-E87675(2014).
CC -!- FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q86T26}.
CC -!- ACTIVITY REGULATION: Inhibited by aprotinin, leupeptin, benzamidine,
CC SERPINA1, SPINT1 and SPINT2. {ECO:0000250|UniProtKB:Q86T26}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86T26};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in esophagus, cervix, tongue, and testes.
CC {ECO:0000269|PubMed:24498351}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AK036858; BAC29606.1; -; mRNA.
DR EMBL; AK036968; BAC29652.1; -; mRNA.
DR EMBL; AK137654; BAE23447.1; -; mRNA.
DR EMBL; BC115419; AAI15420.1; -; mRNA.
DR EMBL; BC115420; AAI15421.1; -; mRNA.
DR CCDS; CCDS39126.1; -.
DR RefSeq; NP_795998.2; NM_177024.4.
DR AlphaFoldDB; Q14C59; -.
DR SMR; Q14C59; -.
DR BioGRID; 235589; 3.
DR STRING; 10090.ENSMUSP00000042406; -.
DR MEROPS; S01.207; -.
DR GlyGen; Q14C59; 2 sites.
DR iPTMnet; Q14C59; -.
DR PhosphoSitePlus; Q14C59; -.
DR PaxDb; Q14C59; -.
DR PRIDE; Q14C59; -.
DR ProteomicsDB; 259460; -.
DR DNASU; 319875; -.
DR Ensembl; ENSMUST00000038448; ENSMUSP00000042406; ENSMUSG00000035861.
DR GeneID; 319875; -.
DR KEGG; mmu:319875; -.
DR UCSC; uc008xxu.1; mouse.
DR CTD; 132724; -.
DR MGI; MGI:2442893; Tmprss11b.
DR VEuPathDB; HostDB:ENSMUSG00000035861; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000163621; -.
DR HOGENOM; CLU_006842_19_0_1; -.
DR InParanoid; Q14C59; -.
DR OMA; WQASLKK; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q14C59; -.
DR TreeFam; TF351684; -.
DR BioGRID-ORCS; 319875; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Tmprss11b; mouse.
DR PRO; PR:Q14C59; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q14C59; protein.
DR Bgee; ENSMUSG00000035861; Expressed in esophagus and 4 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..416
FT /note="Transmembrane protease serine 11B-like protein"
FT /id="PRO_0000299320"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 44..161
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 185..415
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 210..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 335..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 362..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 56
FT /note="D -> N (in Ref. 2; AAI15420)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="S -> Y (in Ref. 1; BAC29606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 46713 MW; 5185C42C39BAB9F2 CRC64;
MYRPVIASRK SIPPWLIILC VLGVLAALGI IIGLLVHFLA VENKIYYYQG GFKVLDIPYD
RNYERETSLE SNYLSKILEN KMVEAFQNSN IYKQYINSQV ITLVPDNNSV TAHIWLVFKD
PWSNKENLRR RIESILRQML ENNPESLTTD PGSLKLTEIS KVDAEKIINN RCGRRPRMSA
TYDRITGGST AHKGEWPWQA SLRVNGKHYC GASLIGERFL LTAAHCFQGT NNPKNLTVSF
GTRVTPAYMQ HSVQEIIIHE DYVKGEHHDD VAVIKLTEKV SFNNDVHRVC LPESTQIFPP
GEGVVVTGWG SFSYNGKSPL LLQKASIKII DTNTCNSEEA YGGRIVDTML CAGYLEGSID
ACQGDSGGPL VHPNSRDIWY LVGIVSWGHE CGRVNKPGVY MRVTSYRNWI ASKTGI
