TM11A_HUMAN
ID TM11A_HUMAN Reviewed; 418 AA.
AC Q6ZMR5; J3KNQ8; Q2NKI9; Q6JE90; Q7RTY4; Q86TK8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Transmembrane protease serine 11A;
DE EC=3.4.21.-;
DE AltName: Full=Airway trypsin-like protease 1;
DE AltName: Full=Epidermal type-II transmembrane serine protease;
DE AltName: Full=Esophageal cancer-susceptibility gene 1 protein;
GN Name=TMPRSS11A; Synonyms=ECRG1, HATL1, HESP;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Esophagus;
RX PubMed=10920976;
RA Su T., Liu H., Lu S.-H.;
RT "Cloning and identification of cDNA fragments related to human esophageal
RT cancer.";
RL Zhonghua Zhong Liu Za Zhi 20:254-257(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT GLN-290.
RA Mariotti F., Mastrogiacomo A.;
RT "Identification and characterization of a novel human type II transmembrane
RT serine protease.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP IDENTIFICATION.
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
RN [7]
RP INTERACTION WITH ZBTB17.
RX PubMed=15095404; DOI=10.1002/jcb.20025;
RA Zhao N., Wang J., Cui Y., Guo L., Lu S.-H.;
RT "Induction of G1 cell cycle arrest and P15INK4b expression by ECRG1 through
RT interaction with Miz-1.";
RL J. Cell. Biochem. 92:65-76(2004).
RN [8]
RP VARIANT GLN-290.
RX PubMed=16267096; DOI=10.1093/carcin/bgi258;
RA Li Y., Zhang X., Huang G., Miao X., Guo L., Lin D., Lu S.-H.;
RT "Identification of a novel polymorphism Arg290Gln of esophageal cancer
RT related gene 1 (ECRG1) and its related risk to esophageal squamous cell
RT carcinoma.";
RL Carcinogenesis 27:798-802(2006).
CC -!- FUNCTION: Probable serine protease which may play a role in cellular
CC senescence. Overexpression inhibits cell growth and induce G1 cell
CC cycle arrest.
CC -!- SUBUNIT: May interact with ZBTB17.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q6ZMR5-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q6ZMR5-1; Sequence=VSP_061449;
CC -!- TISSUE SPECIFICITY: Expressed in esophagus, liver, colon and lung.
CC Down-regulated in esophagus cancers. {ECO:0000269|PubMed:10920976}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD41463.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD67985.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF071882; AAD41463.1; ALT_FRAME; mRNA.
DR EMBL; AY498712; AAS78642.1; -; mRNA.
DR EMBL; AK131518; BAD18660.1; -; mRNA.
DR EMBL; AC096653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111796; AAI11797.1; -; mRNA.
DR EMBL; BN000133; CAD67985.1; ALT_SEQ; mRNA.
DR CCDS; CCDS3519.1; -. [Q6ZMR5-1]
DR CCDS; CCDS47065.1; -. [Q6ZMR5-2]
DR RefSeq; NP_001107859.1; NM_001114387.1.
DR RefSeq; NP_872412.3; NM_182606.3.
DR AlphaFoldDB; Q6ZMR5; -.
DR SMR; Q6ZMR5; -.
DR BioGRID; 130971; 14.
DR IntAct; Q6ZMR5; 7.
DR STRING; 9606.ENSP00000334611; -.
DR MEROPS; S01.292; -.
DR TCDB; 8.A.131.1.7; the transmembrane protease serine 3 (tmprss3) family.
DR GlyGen; Q6ZMR5; 2 sites.
DR iPTMnet; Q6ZMR5; -.
DR PhosphoSitePlus; Q6ZMR5; -.
DR BioMuta; TMPRSS11A; -.
DR DMDM; 74758674; -.
DR MassIVE; Q6ZMR5; -.
DR PaxDb; Q6ZMR5; -.
DR PeptideAtlas; Q6ZMR5; -.
DR PRIDE; Q6ZMR5; -.
DR ProteomicsDB; 67906; -. [Q6ZMR5-1]
DR ProteomicsDB; 67907; -. [Q6ZMR5-2]
DR TopDownProteomics; Q6ZMR5-2; -. [Q6ZMR5-2]
DR Antibodypedia; 57609; 83 antibodies from 20 providers.
DR DNASU; 339967; -.
DR Ensembl; ENST00000508048.6; ENSP00000426911.2; ENSG00000187054.16.
DR GeneID; 339967; -.
DR KEGG; hsa:339967; -.
DR UCSC; uc003hds.2; human. [Q6ZMR5-2]
DR CTD; 339967; -.
DR DisGeNET; 339967; -.
DR GeneCards; TMPRSS11A; -.
DR HGNC; HGNC:27954; TMPRSS11A.
DR HPA; ENSG00000187054; Group enriched (esophagus, lymphoid tissue, vagina).
DR MIM; 611704; gene.
DR neXtProt; NX_Q6ZMR5; -.
DR PharmGKB; PA142670726; -.
DR VEuPathDB; HostDB:ENSG00000187054; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q6ZMR5; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q6ZMR5; -.
DR TreeFam; TF351684; -.
DR BRENDA; 3.4.21.B61; 2681.
DR PathwayCommons; Q6ZMR5; -.
DR SignaLink; Q6ZMR5; -.
DR BioGRID-ORCS; 339967; 7 hits in 1067 CRISPR screens.
DR ChiTaRS; TMPRSS11A; human.
DR GenomeRNAi; 339967; -.
DR Pharos; Q6ZMR5; Tbio.
DR PRO; PR:Q6ZMR5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6ZMR5; protein.
DR Bgee; ENSG00000187054; Expressed in esophagus mucosa and 32 other tissues.
DR ExpressionAtlas; Q6ZMR5; baseline and differential.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Disulfide bond; Glycoprotein; Hydrolase;
KW Membrane; Protease; Reference proteome; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..418
FT /note="Transmembrane protease serine 11A"
FT /id="PRO_5000095974"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..418
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 47..164
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 187..417
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 227
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 368
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 212..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 337..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 364..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 84
FT /note="L -> LVSQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10920976,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_061449"
FT VARIANT 290
FT /note="R -> Q (may be a susceptibility factor for
FT developing esophageal cancer especially in smoking
FT population; dbSNP:rs353163)"
FT /evidence="ECO:0000269|PubMed:16267096, ECO:0000269|Ref.2"
FT /id="VAR_034797"
FT CONFLICT 50
FT /note="Y -> F (in Ref. 1; AAD41463)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="H -> P (in Ref. 1; AAD41463)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="T -> I (in Ref. 1; AAD41463)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="Y -> C (in Ref. 1; AAD41463)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="A -> P (in Ref. 1; AAD41463)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> K (in Ref. 1; AAD41463)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="S -> P (in Ref. 1; AAD41463)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="A -> V (in Ref. 1; AAD41463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47254 MW; 96674ECABCA9B301 CRC64;
MMYRTVGFGT RSRNLKPWMI AVLIVLSLTV VAVTIGLLVH FLVFDQKKEY YHGSFKILDP
QINNNFGQSN TYQLKDLRET TENLVDEIFI DSAWKKNYIK NQVVRLTPEE DGVKVDVIMV
FQFPSTEQRA VREKKIQSIL NQKIRNLRAL PINASSVQVN AMSSSTGELT VQASCGKRVV
PLNVNRIASG VIAPKAAWPW QASLQYDNIH QCGATLISNT WLVTAAHCFQ KYKNPHQWTV
SFGTKINPPL MKRNVRRFII HEKYRSAARE YDIAVVQVSS RVTFSDDIRR ICLPEASASF
QPNLTVHITG FGALYYGGES QNDLREARVK IISDDVCKQP QVYGNDIKPG MFCAGYMEGI
YDACRGDSGG PLVTRDLKDT WYLIGIVSWG DNCGQKDKPG VYTQVTYYRN WIASKTGI
