TM11E_HUMAN
ID TM11E_HUMAN Reviewed; 423 AA.
AC Q9UL52; A6NL71; Q14DC8; Q6UW31;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Transmembrane protease serine 11E;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease DESC1;
DE AltName: Full=Transmembrane protease serine 11E2;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11E non-catalytic chain;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11E catalytic chain;
DE Flags: Precursor;
GN Name=TMPRSS11E; Synonyms=DESC1, TMPRSS11E2; ORFNames=UNQ742/PRO1461;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11161383; DOI=10.1054/bjoc.2000.1586;
RA Lang J.C., Schuller D.E.;
RT "Differential expression of a novel serine protease homologue in squamous
RT cell carcinoma of the head and neck.";
RL Br. J. Cancer 84:237-243(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
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].
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 [5]
RP ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
RX PubMed=14696115; DOI=10.1002/ijc.11594;
RA Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K.,
RA Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.;
RT "Regulation of carcinoma cell invasion by protein C inhibitor whose
RT expression is decreased in renal cell carcinoma.";
RL Int. J. Cancer 108:516-523(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 192-423, ACTIVE SITE, AND
RP DISULFIDE BONDS.
RX PubMed=17388811; DOI=10.1111/j.1742-4658.2007.05756.x;
RA Kyrieleis O.J., Huber R., Ong E., Oehler R., Hunter M., Madison E.L.,
RA Jacob U.;
RT "Crystal structure of the catalytic domain of DESC1, a new member of the
RT type II transmembrane serine proteinase family.";
RL FEBS J. 274:2148-2160(2007).
CC -!- FUNCTION: Serine protease which possesses both gelatinolytic and
CC caseinolytic activities. Shows a preference for Arg in the P1 position.
CC {ECO:0000250|UniProtKB:Q5S248}.
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5.
CC {ECO:0000269|PubMed:14696115}.
CC -!- SUBUNIT: Forms a heterodimer with SERPINA5 and SERPINE1.
CC -!- INTERACTION:
CC Q9UL52; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12324579, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5S248};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q5S248}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protease serine 11E catalytic
CC chain]: Secreted {ECO:0000250|UniProtKB:Q5S248}. Note=Activated by
CC cleavage and secreted. {ECO:0000250|UniProtKB:Q5S248}.
CC -!- TISSUE SPECIFICITY: Expression can only be detected in tissues derived
CC from the head and neck, and in skin, prostate and testis.
CC {ECO:0000269|PubMed:11161383}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF064819; AAF04328.1; -; mRNA.
DR EMBL; AY359017; AAQ89376.1; -; mRNA.
DR EMBL; AC140484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113412; AAI13413.1; -; mRNA.
DR EMBL; BC113414; AAI13415.1; -; mRNA.
DR CCDS; CCDS33993.1; -.
DR RefSeq; NP_054777.2; NM_014058.3.
DR PDB; 2OQ5; X-ray; 1.61 A; A=192-423.
DR PDBsum; 2OQ5; -.
DR AlphaFoldDB; Q9UL52; -.
DR SMR; Q9UL52; -.
DR BioGRID; 118804; 12.
DR IntAct; Q9UL52; 2.
DR STRING; 9606.ENSP00000307519; -.
DR MEROPS; S01.021; -.
DR GlyGen; Q9UL52; 3 sites.
DR iPTMnet; Q9UL52; -.
DR PhosphoSitePlus; Q9UL52; -.
DR BioMuta; TMPRSS11E; -.
DR DMDM; 57015324; -.
DR jPOST; Q9UL52; -.
DR MassIVE; Q9UL52; -.
DR PaxDb; Q9UL52; -.
DR PeptideAtlas; Q9UL52; -.
DR PRIDE; Q9UL52; -.
DR ProteomicsDB; 84952; -.
DR ABCD; Q9UL52; 3 sequenced antibodies.
DR Antibodypedia; 57640; 150 antibodies from 20 providers.
DR DNASU; 28983; -.
DR Ensembl; ENST00000305363.9; ENSP00000307519.4; ENSG00000087128.10.
DR GeneID; 28983; -.
DR KEGG; hsa:28983; -.
DR MANE-Select; ENST00000305363.9; ENSP00000307519.4; NM_014058.4; NP_054777.2.
DR UCSC; uc003hdz.4; human.
DR CTD; 28983; -.
DR DisGeNET; 28983; -.
DR GeneCards; TMPRSS11E; -.
DR HGNC; HGNC:24465; TMPRSS11E.
DR HPA; ENSG00000087128; Tissue enhanced (esophagus, vagina).
DR MIM; 610399; gene.
DR neXtProt; NX_Q9UL52; -.
DR OpenTargets; ENSG00000087128; -.
DR PharmGKB; PA142670729; -.
DR VEuPathDB; HostDB:ENSG00000087128; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161786; -.
DR HOGENOM; CLU_006842_19_0_1; -.
DR InParanoid; Q9UL52; -.
DR OMA; HCFRTYK; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9UL52; -.
DR TreeFam; TF351684; -.
DR PathwayCommons; Q9UL52; -.
DR SignaLink; Q9UL52; -.
DR BioGRID-ORCS; 28983; 9 hits in 1059 CRISPR screens.
DR EvolutionaryTrace; Q9UL52; -.
DR GenomeRNAi; 28983; -.
DR Pharos; Q9UL52; Tbio.
DR PRO; PR:Q9UL52; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UL52; protein.
DR Bgee; ENSG00000087128; Expressed in lower esophagus mucosa and 69 other tissues.
DR ExpressionAtlas; Q9UL52; baseline and differential.
DR Genevisible; Q9UL52; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW Membrane; Protease; Reference proteome; Secreted; Serine protease;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..191
FT /note="Transmembrane protease serine 11E non-catalytic
FT chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027891"
FT CHAIN 192..423
FT /note="Transmembrane protease serine 11E catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027892"
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..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 49..167
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 192..422
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17388811"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17388811"
FT ACT_SITE 373
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17388811"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 177..297
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 217..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:17388811"
FT DISULFID 342..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:17388811"
FT DISULFID 369..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:17388811"
FT VARIANT 303
FT /note="Y -> C (in dbSNP:rs976002)"
FT /id="VAR_051847"
FT CONFLICT 158
FT /note="H -> Q (in Ref. 3; AC019173)"
FT /evidence="ECO:0000305"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2OQ5"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:2OQ5"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:2OQ5"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2OQ5"
FT TURN 345..350
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:2OQ5"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:2OQ5"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:2OQ5"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:2OQ5"
SQ SEQUENCE 423 AA; 47696 MW; EB1476807C0B613D CRC64;
MMYRPDVVRA RKRVCWEPWV IGLVIFISLI VLAVCIGLTV HYVRYNQKKT YNYYSTLSFT
TDKLYAEFGR EASNNFTEMS QRLESMVKNA FYKSPLREEF VKSQVIKFSQ QKHGVLAHML
LICRFHSTED PETVDKIVQL VLHEKLQDAV GPPKVDPHSV KIKKINKTET DSYLNHCCGT
RRSKTLGQSL RIVGGTEVEE GEWPWQASLQ WDGSHRCGAT LINATWLVSA AHCFTTYKNP
ARWTASFGVT IKPSKMKRGL RRIIVHEKYK HPSHDYDISL AELSSPVPYT NAVHRVCLPD
ASYEFQPGDV MFVTGFGALK NDGYSQNHLR QAQVTLIDAT TCNEPQAYND AITPRMLCAG
SLEGKTDACQ GDSGGPLVSS DARDIWYLAG IVSWGDECAK PNKPGVYTRV TALRDWITSK
TGI
