TM11L_RAT
ID TM11L_RAT Reviewed; 420 AA.
AC Q6IE14;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=Tmprss11bnl; Synonyms=Hatl5, Tmprss11b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=15060002; DOI=10.1101/gr.1946304;
RA Puente X.S., Lopez-Otin C.;
RT "A genomic analysis of rat proteases and protease inhibitors.";
RL Genome Res. 14:609-622(2004).
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: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:Q86T26}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AABR03092659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03092237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000379; CAE51905.1; -; mRNA.
DR RefSeq; NP_001004020.1; NM_001004020.1.
DR AlphaFoldDB; Q6IE14; -.
DR SMR; Q6IE14; -.
DR STRING; 10116.ENSRNOP00000002743; -.
DR MEROPS; S01.321; -.
DR GlyGen; Q6IE14; 3 sites.
DR PaxDb; Q6IE14; -.
DR PRIDE; Q6IE14; -.
DR GeneID; 365265; -.
DR KEGG; rno:365265; -.
DR UCSC; RGD:1303278; rat.
DR CTD; 132724; -.
DR RGD; 1303278; Tmprss11bnl.
DR VEuPathDB; HostDB:ENSRNOG00000002002; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_19_0_1; -.
DR InParanoid; Q6IE14; -.
DR OMA; WQASLKK; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q6IE14; -.
DR TreeFam; TF351684; -.
DR PRO; PR:Q6IE14; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002002; Expressed in esophagus and 1 other tissue.
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..420
FT /note="Transmembrane protease serine 11B-like protein"
FT /id="PRO_0000299321"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 48..165
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 189..419
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 370
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 214..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 339..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 366..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 420 AA; 47242 MW; BC0D61CB9761AD2F CRC64;
MTVSKLRPVI ASRKSFPPWM IILGVLGVLA ILGLIIGLLV HFLAVENKIY YYQGSFKVLN
IPYDRNYERE TSLESNYLSK ILEIKMVDAF ESSNIYKQYI NSQIITLVPE NNSVTAHIWL
VFKDPWSNKE NLRRRIESIL HQMLENNSGS LTTDPGSLKL TEITKVDAEK IINNRCGRRP
RMSATYDRIT GGSTAQKGEW PWQASLRVNG KHHCGASLIG ERFLLTAAHC FLRTNNPKNL
TVSFGTRVTP AYMQHYVEEV IIHEDYVKGQ HHDDVAIIKL TEKVSFRNDV HRVCLPEATQ
VFPPGEGVVV TGWGSLSYNG KSPLLLQKAS IKIIDTNACN SEEAYGGRIM DTMLCAGYME
GYVDACQGDS GGPLVHPNSR DIWYLVGIVS WGHECGRVNK PGVYMRVTSY RDWIASKTGI
