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TM11F_MOUSE
ID   TM11F_MOUSE             Reviewed;         439 AA.
AC   Q8BHM9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Transmembrane protease serine 11F;
DE            EC=3.4.21.-;
DE   AltName: Full=Airway trypsin-like protease 4;
GN   Name=Tmprss11f; Synonyms=Hatl4;
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Probable serine protease. {ECO:0000250}.
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; AK028447; BAC25955.1; -; mRNA.
DR   EMBL; AK028587; BAC26020.1; -; mRNA.
DR   EMBL; AK029032; BAC26254.1; -; mRNA.
DR   EMBL; AK037173; BAC29734.1; -; mRNA.
DR   EMBL; BC132629; AAI32630.1; -; mRNA.
DR   CCDS; CCDS39125.1; -.
DR   RefSeq; NP_848845.1; NM_178730.3.
DR   RefSeq; XP_006534992.1; XM_006534929.2.
DR   AlphaFoldDB; Q8BHM9; -.
DR   SMR; Q8BHM9; -.
DR   BioGRID; 232482; 5.
DR   STRING; 10090.ENSMUSP00000112252; -.
DR   MEROPS; S01.321; -.
DR   iPTMnet; Q8BHM9; -.
DR   PhosphoSitePlus; Q8BHM9; -.
DR   PaxDb; Q8BHM9; -.
DR   PRIDE; Q8BHM9; -.
DR   ProteomicsDB; 259461; -.
DR   Antibodypedia; 12702; 37 antibodies from 14 providers.
DR   DNASU; 243083; -.
DR   Ensembl; ENSMUST00000116553; ENSMUSP00000112252; ENSMUSG00000048764.
DR   GeneID; 243083; -.
DR   KEGG; mmu:243083; -.
DR   UCSC; uc008xxs.1; mouse.
DR   CTD; 389208; -.
DR   MGI; MGI:2442348; Tmprss11f.
DR   VEuPathDB; HostDB:ENSMUSG00000048764; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000161680; -.
DR   HOGENOM; CLU_006842_19_0_1; -.
DR   InParanoid; Q8BHM9; -.
DR   OMA; SQWIATF; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q8BHM9; -.
DR   TreeFam; TF351684; -.
DR   BioGRID-ORCS; 243083; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Tmprss11f; mouse.
DR   PRO; PR:Q8BHM9; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8BHM9; protein.
DR   Bgee; ENSMUSG00000048764; Expressed in esophagus and 19 other tissues.
DR   Genevisible; Q8BHM9; MM.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0033561; P:regulation of water loss via skin; IMP: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   Disulfide bond; Hydrolase; Membrane; Protease; Reference proteome;
KW   Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..439
FT                   /note="Transmembrane protease serine 11F"
FT                   /id="PRO_0000299323"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..439
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          58..176
FT                   /note="SEA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          207..438
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        249
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        294
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        390
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        234..250
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        359..375
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        386..414
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   439 AA;  49776 MW;  028A40E574514BD2 CRC64;
     MMYAPVEFSQ TAYPRIEYQR RQQQFWDPIR LALFTLAIVA IVGITIGIVT HFVVEDDKSF
     YYLASFQVTS IKYRENYGIR SSREFIERSH QIERMMSRIF RRSSGVGRFI KSHVIKISPD
     EQGVNILIVL MFRYPSTDSA ERIKKRIERT FYQSLKIKQL PLTISMPSFS LTPIDSKKMR
     NLLNSRCGIR MSSSNIPLPA SSSTERIVQG RETAMEGEWP WQASLQLIGA GHQCGATLIS
     NTWLLTAAHC FWKNRDPTKW IVTFGTTITP PLVKRSVGKI IIHEEYHRDT NENDIALAQL
     TTRVEFSNVV QRVCLPDSSM KLPPKTSVFV TGFGSIVDDG PTQNKLRQAR VETIGSDVCN
     RKDVYDGLIT PGMLCAGFME GKIDACKGDS GGPLVYDNRD IWYIVGIVSW GQSCALPNKP
     GVYTRVTKYR DWIASKTGL
 
 
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