TM11B_HUMAN
ID TM11B_HUMAN Reviewed; 416 AA.
AC Q86T26; A8K4D9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Transmembrane protease serine 11B;
DE EC=3.4.21.-;
DE AltName: Full=Airway trypsin-like protease 5;
GN Name=TMPRSS11B; Synonyms=HATL5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-242.
RC TISSUE=Esophagus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-242; ALA-325 AND
RP SER-348.
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-242; ALA-325 AND
RP SER-348.
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 [5]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
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:0000269|PubMed:24498351}.
CC -!- ACTIVITY REGULATION: Inhibited by aprotinin, leupeptin, benzamidine,
CC SERPINA1, SPINT1 and SPINT2. {ECO:0000269|PubMed:24498351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24498351};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AK290904; BAF83593.1; -; mRNA.
DR EMBL; AL833167; CAD91168.1; -; mRNA.
DR EMBL; BX537945; CAD97913.1; -; mRNA.
DR EMBL; AC098799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126195; AAI26196.1; -; mRNA.
DR CCDS; CCDS3521.1; -.
DR RefSeq; NP_872308.2; NM_182502.3.
DR RefSeq; XP_011529910.1; XM_011531608.2.
DR AlphaFoldDB; Q86T26; -.
DR SMR; Q86T26; -.
DR BioGRID; 126334; 433.
DR IntAct; Q86T26; 52.
DR MEROPS; S01.365; -.
DR GlyGen; Q86T26; 3 sites.
DR PhosphoSitePlus; Q86T26; -.
DR BioMuta; TMPRSS11B; -.
DR DMDM; 317373502; -.
DR MassIVE; Q86T26; -.
DR PaxDb; Q86T26; -.
DR PeptideAtlas; Q86T26; -.
DR PRIDE; Q86T26; -.
DR ProteomicsDB; 69661; -.
DR Antibodypedia; 24170; 70 antibodies from 15 providers.
DR DNASU; 132724; -.
DR Ensembl; ENST00000332644.6; ENSP00000330475.5; ENSG00000185873.8.
DR GeneID; 132724; -.
DR KEGG; hsa:132724; -.
DR MANE-Select; ENST00000332644.6; ENSP00000330475.5; NM_182502.3; NP_872308.2.
DR UCSC; uc003hdw.5; human.
DR CTD; 132724; -.
DR DisGeNET; 132724; -.
DR GeneCards; TMPRSS11B; -.
DR HGNC; HGNC:25398; TMPRSS11B.
DR HPA; ENSG00000185873; Tissue enhanced (esophagus, lymphoid tissue, vagina).
DR neXtProt; NX_Q86T26; -.
DR OpenTargets; ENSG00000185873; -.
DR PharmGKB; PA142670727; -.
DR VEuPathDB; HostDB:ENSG00000185873; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000163500; -.
DR HOGENOM; CLU_006842_19_0_1; -.
DR InParanoid; Q86T26; -.
DR OMA; NNCCGRQ; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q86T26; -.
DR TreeFam; TF351684; -.
DR PathwayCommons; Q86T26; -.
DR SignaLink; Q86T26; -.
DR BioGRID-ORCS; 132724; 8 hits in 1062 CRISPR screens.
DR ChiTaRS; TMPRSS11B; human.
DR GenomeRNAi; 132724; -.
DR Pharos; Q86T26; Tdark.
DR PRO; PR:Q86T26; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q86T26; protein.
DR Bgee; ENSG00000185873; Expressed in lower esophagus mucosa and 93 other tissues.
DR Genevisible; Q86T26; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA: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 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.
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"
FT /id="PRO_0000299319"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 43..160
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 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
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 VARIANT 242
FT /note="I -> V (in dbSNP:rs12331141)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_034798"
FT VARIANT 325
FT /note="D -> A (in dbSNP:rs2319796)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_047675"
FT VARIANT 348
FT /note="T -> S (in dbSNP:rs2319797)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_034799"
SQ SEQUENCE 416 AA; 46337 MW; 0A9C369EA6F348A3 CRC64;
MYRHGISSQR SWPLWTTIFI FLGVAAILGV TIGLLVHFLA VEKTYYYQGD FHISGVTYND
NCENAASQAS TNLSKDIETK MLNAFQNSSI YKEYVKSEVI KLLPNANGSN VQLQLKFKFP
PAEGVSMRTK IKAKLHQMLK NNMASWNAVP ASIKLMEISK AASEMLTNNC CGRQVANSII
TGNKIVNGKS SLEGAWPWQA SMQWKGRHYC GASLISSRWL LSAAHCFAKK NNSKDWTVNF
GIVVNKPYMT RKVQNIIFHE NYSSPGLHDD IALVQLAEEV SFTEYIRKIC LPEAKMKLSE
NDNVVVTGWG TLYMNGSFPV ILQEDFLKII DNKICNASYA YSGFVTDTML CAGFMSGEAD
ACQNDSGGPL AYPDSRNIWH LVGIVSWGDG CGKKNKPGVY TRVTSYRNWI TSKTGL
