TMPS2_HUMAN
ID TMPS2_HUMAN Reviewed; 492 AA.
AC O15393; A8K6Z8; B2R8E5; B7Z459; D3DSJ2; F8WES1; Q6GTK7; Q9BXX1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Transmembrane protease serine 2 {ECO:0000305};
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 10 {ECO:0000305};
DE Contains:
DE RecName: Full=Transmembrane protease serine 2 non-catalytic chain;
DE Contains:
DE RecName: Full=Transmembrane protease serine 2 catalytic chain;
DE Flags: Precursor;
GN Name=TMPRSS2 {ECO:0000312|HGNC:HGNC:11876}; Synonyms=PRSS10;
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 1), AND VARIANTS MET-160 AND GLN-329.
RX PubMed=9325052; DOI=10.1006/geno.1997.4845;
RA Paoloni-Giacobino A., Chen H., Peitsch M.C., Rossier C., Antonarakis S.E.;
RT "Cloning of the TMPRSS2 gene, which encodes a novel serine protease with
RT transmembrane, LDLRA, and SRCR domains and maps to 21q22.3.";
RL Genomics 44:309-320(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-160.
RX PubMed=11414763; DOI=10.1006/geno.2001.6551;
RA Teng D.-H., Chen Y., Lian L., Ha P.C., Tavtigian S.V., Wong A.K.C.;
RT "Mutation analyses of 268 candidate genes in human tumor cell lines.";
RL Genomics 74:352-364(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-441, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11245484;
RA Afar D.E.H., Vivanco I., Hubert R.S., Kuo J., Chen E., Saffran D.C.,
RA Raitano A.B., Jakobovits A.;
RT "Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in
RT its secretion by prostate and prostate cancer epithelia.";
RL Cancer Res. 61:1686-1692(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Prostate, Testis, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=PNS;
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=11169526;
RX DOI=10.1002/1096-9896(2000)9999:9999<::aid-path743>3.0.co;2-t;
RA Vaarala M.H., Porvari K.S., Kellokumpu S., Kyllonen A.P., Vihko P.T.;
RT "Expression of transmembrane serine protease TMPRSS2 in mouse and human
RT tissues.";
RL J. Pathol. 193:134-140(2001).
RN [10]
RP FUNCTION.
RX PubMed=15537383; DOI=10.1042/bj20041066;
RA Wilson S., Greer B., Hooper J., Zijlstra A., Walker B., Quigley J.,
RA Hawthorne S.;
RT "The membrane-anchored serine protease, TMPRSS2, activates PAR-2 in
RT prostate cancer cells.";
RL Biochem. J. 388:967-972(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=20382709; DOI=10.2353/ajpath.2010.090665;
RA Chen Y.W., Lee M.S., Lucht A., Chou F.P., Huang W., Havighurst T.C.,
RA Kim K., Wang J.K., Antalis T.M., Johnson M.D., Lin C.Y.;
RT "TMPRSS2, a serine protease expressed in the prostate on the apical surface
RT of luminal epithelial cells and released into semen in prostasomes, is
RT misregulated in prostate cancer cells.";
RL Am. J. Pathol. 176:2986-2996(2010).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AUTOCATALYTIC
RP CLEAVAGE, AND INTERACTION WITH ACE2.
RX PubMed=21068237; DOI=10.1128/jvi.02062-10;
RA Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S.,
RA Gallagher T.;
RT "A transmembrane serine protease is linked to the severe acute respiratory
RT syndrome coronavirus receptor and activates virus entry.";
RL J. Virol. 85:873-882(2011).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RX PubMed=21325420; DOI=10.1128/jvi.02232-10;
RA Glowacka I., Bertram S., Muller M.A., Allen P., Soilleux E., Pfefferle S.,
RA Steffen I., Tsegaye T.S., He Y., Gnirss K., Niemeyer D., Schneider H.,
RA Drosten C., Pohlmann S.;
RT "Evidence that TMPRSS2 activates the severe acute respiratory syndrome
RT coronavirus spike protein for membrane fusion and reduces viral control by
RT the humoral immune response.";
RL J. Virol. 85:4122-4134(2011).
RN [14]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=23536651; DOI=10.1128/jvi.03372-12;
RA Bertram S., Dijkman R., Habjan M., Heurich A., Gierer S., Glowacka I.,
RA Welsch K., Winkler M., Schneider H., Hofmann-Winkler H., Thiel V.,
RA Pohlmann S.;
RT "TMPRSS2 activates the human coronavirus 229E for cathepsin-independent
RT host cell entry and is expressed in viral target cells in the respiratory
RT epithelium.";
RL J. Virol. 87:6150-6160(2013).
RN [15]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=23966399; DOI=10.1128/jvi.01490-13;
RA Abe M., Tahara M., Sakai K., Yamaguchi H., Kanou K., Shirato K., Kawase M.,
RA Noda M., Kimura H., Matsuyama S., Fukuhara H., Mizuta K., Maenaka K.,
RA Ami Y., Esumi M., Kato A., Takeda M.;
RT "TMPRSS2 is an activating protease for respiratory parainfluenza viruses.";
RL J. Virol. 87:11930-11935(2013).
RN [16]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=24027332; DOI=10.1128/jvi.01890-13;
RA Shirato K., Kawase M., Matsuyama S.;
RT "Middle East respiratory syndrome coronavirus infection mediated by the
RT transmembrane serine protease TMPRSS2.";
RL J. Virol. 87:12552-12561(2013).
RN [17]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=24227843; DOI=10.1128/jvi.02202-13;
RA Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O.,
RA Poehlmann S.;
RT "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by
RT TMPRSS2 augments entry driven by the severe acute respiratory syndrome
RT coronavirus spike protein.";
RL J. Virol. 88:1293-1307(2014).
RN [18]
RP FUNCTION, AND INDUCTION.
RX PubMed=25122198; DOI=10.1158/2159-8290.cd-13-1010;
RA Lucas J.M., Heinlein C., Kim T., Hernandez S.A., Malik M.S., True L.D.,
RA Morrissey C., Corey E., Montgomery B., Mostaghel E., Clegg N., Coleman I.,
RA Brown C.M., Schneider E.L., Craik C., Simon J.A., Bedalov A., Nelson P.S.;
RT "The androgen-regulated protease TMPRSS2 activates a proteolytic cascade
RT involving components of the tumor microenvironment and promotes prostate
RT cancer metastasis.";
RL Cancer Discov. 4:1310-1325(2014).
RN [19]
RP FUNCTION.
RX PubMed=26018085; DOI=10.1158/0008-5472.can-14-3297;
RA Ko C.J., Huang C.C., Lin H.Y., Juan C.P., Lan S.W., Shyu H.Y., Wu S.R.,
RA Hsiao P.W., Huang H.P., Shun C.T., Lee M.S.;
RT "Androgen-Induced TMPRSS2 activates matriptase and promotes extracellular
RT matrix degradation, prostate cancer cell invasion, tumor growth, and
RT metastasis.";
RL Cancer Res. 75:2949-2960(2015).
RN [20]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=32142651; DOI=10.1016/j.cell.2020.02.052;
RA Hoffmann M., Kleine-Weber H., Schroeder S., Krueger N., Herrler T.,
RA Erichsen S., Schiergens T.S., Herrler G., Wu N.H., Nitsche A.,
RA Mueller M.A., Drosten C., Poehlmann S.;
RT "SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a
RT clinically proven protease inhibitor.";
RL Cell 181:1-10(2020).
RN [21]
RP TISSUE SPECIFICITY.
RX DOI=10.1016/j.cell.2020.04.035;
RA Ziegler C.G.K., Allon S.J., Nyquist S.K., Mbano I.M., Miao V.N.,
RA Tzouanas C.N., Cao Y., Yousif A.S., Bals J., Hauser B.M., Feldman J.,
RA Muus C., Wadsworth M.H., Kazer S.W., Hughes T.K., Doran B., Gatter G.J.,
RA Vukovic M., Taliaferro F., Mead B.E., Guo Z., Wang J.P., Gras D.,
RA Plaisant M., Ansari M., Angelidis I., Adler H., Sucre J.M.S., Taylor C.J.,
RA Lin B., Waghray A., Mitsialis V., Dwyer D.F., Buchheit K.M., Boyce J.A.,
RA Barrett N.A., Laidlaw T.M., Carroll S.L., Colonna L., Tkachev V.,
RA Peterson C.W., Yu A., Zheng H.B., Gideon H.P., Winchell C.G., Lin P.L.,
RA Bingle C.D., Snapper S.B., Kropski J.A., Theis F.J., Schiller H.B.,
RA Zaragosi L.E., Barbry P., Leslie A., Kiem H.P., Flynn J.L., Fortune S.M.,
RA Berger B., Finberg R.W., Kean L.S., Garber M., Schmidt A.G., Lingwood D.,
RA Shalek A.K., Ordovas-Montanes J.;
RT "SARS-CoV-2 receptor ACE2 is an interferon-stimulated gene in human airway
RT epithelial cells and is detected in specific cell subsets across tissues.";
RL Cell 0:0-0(2020).
RN [22]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=33051876; DOI=10.15252/embj.2020106267;
RA Buchrieser J., Dufloo J., Hubert M., Monel B., Planas D., Rajah M.M.,
RA Planchais C., Porrot F., Guivel-Benhassine F., Van der Werf S.,
RA Casartelli N., Mouquet H., Bruel T., Schwartz O.;
RT "Syncytia formation by SARS-CoV-2-infected cells.";
RL EMBO J. 39:e106267-e106267(2020).
RN [23]
RP ERRATUM OF PUBMED:33051876.
RX PubMed=33522642; DOI=10.15252/embj.2020107405;
RA Buchrieser J., Dufloo J., Hubert M., Monel B., Planas D., Rajah M.M.,
RA Planchais C., Porrot F., Guivel-Benhassine F., Van der Werf S.,
RA Casartelli N., Mouquet H., Bruel T., Schwartz O.;
RT "Syncytia formation by SARS-CoV-2-infected cells.";
RL EMBO J. 40:e107405-e107405(2021).
RN [24]
RP TISSUE SPECIFICITY.
RX PubMed=32327758; DOI=10.1038/s41591-020-0868-6;
RG HCA Lung Biological Network;
RA Sungnak W., Huang N., Becavin C., Berg M., Queen R., Litvinukova M.,
RA Talavera-Lopez C., Maatz H., Reichart D., Sampaziotis F., Worlock K.B.,
RA Yoshida M., Barnes J.L.;
RT "SARS-CoV-2 entry factors are highly expressed in nasal epithelial cells
RT together with innate immune genes.";
RL Nat. Med. 26:681-687(2020).
RN [25]
RP FUNCTION (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RX PubMed=32404436; DOI=10.1126/sciimmunol.abc3582;
RA Zang R., Gomez Castro M.F., McCune B.T., Zeng Q., Rothlauf P.W.,
RA Sonnek N.M., Liu Z., Brulois K.F., Wang X., Greenberg H.B., Diamond M.S.,
RA Ciorba M.A., Whelan S.P.J., Ding S.;
RT "TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal
RT enterocytes.";
RL Sci. Immunol. 5:0-0(2020).
RN [26]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=34159616; DOI=10.15252/embj.2021107821;
RA Koch J., Uckeley Z.M., Doldan P., Stanifer M., Boulant S., Lozach P.Y.;
RT "TMPRSS2 expression dictates the entry route used by SARS-CoV-2 to infect
RT host cells.";
RL EMBO J. 40:1-20(2021).
RN [27]
RP VARIANTS MET-160; CYS-254; GLN-329 AND ASN-491.
RX PubMed=17918732; DOI=10.1002/humu.20617;
RA Guipponi M., Toh M.-Y., Tan J., Park D., Hanson K., Ballana E., Kwong D.,
RA Cannon P.Z.F., Wu Q., Gout A., Delorenzi M., Speed T.P., Smith R.J.H.,
RA Dahl H.-H.M., Petersen M., Teasdale R.D., Estivill X., Park W.J.,
RA Scott H.S.;
RT "An integrated genetic and functional analysis of the role of type II
RT transmembrane serine proteases (TMPRSSs) in hearing loss.";
RL Hum. Mutat. 29:130-141(2008).
RN [28]
RP VARIANTS THR-28; ARG-74 AND MET-160.
RX PubMed=32867305; DOI=10.3390/genes11091010;
RA Latini A., Agolini E., Novelli A., Borgiani P., Giannini R., Gravina P.,
RA Smarrazzo A., Dauri M., Andreoni M., Rogliani P., Bernardini S.,
RA Helmer-Citterich M., Biancolella M., Novelli G.;
RT "COVID-19 and Genetic Variants of Protein Involved in the SARS-CoV-2 Entry
RT into the Host Cells.";
RL Genes (Basel) 11:0-0(2020).
CC -!- FUNCTION: Plasma membrane-anchored serine protease that participates in
CC proteolytic cascades of relevance for the normal physiologic function
CC of the prostate (PubMed:25122198). Androgen-induced TMPRSS2 activates
CC several substrates that include pro-hepatocyte growth factor/HGF, the
CC protease activated receptor-2/F2RL1 or matriptase/ST14 leading to
CC extracellular matrix disruption and metastasis of prostate cancer cells
CC (PubMed:15537383, PubMed:26018085, PubMed:25122198). In addition,
CC activates trigeminal neurons and contribute to both spontaneous pain
CC and mechanical allodynia (By similarity).
CC {ECO:0000250|UniProtKB:Q9JIQ8, ECO:0000269|PubMed:15537383,
CC ECO:0000269|PubMed:25122198, ECO:0000269|PubMed:26018085}.
CC -!- FUNCTION: (Microbial infection) Facilitates human coronaviruses SARS-
CC CoV and SARS-CoV-2 infections via two independent mechanisms,
CC proteolytic cleavage of ACE2 receptor which promotes viral uptake, and
CC cleavage of coronavirus spike glycoproteins which activates the
CC glycoprotein for host cell entry (PubMed:24227843, PubMed:32142651,
CC PubMed:32404436, PubMed:34159616, PubMed:33051876). Upon SARS-CoV-2
CC infection, increases syncytia formation by accelerating the fusion
CC process (PubMed:34159616, PubMed:33051876). Proteolytically cleaves and
CC activates the spike glycoproteins of human coronavirus 229E (HCoV-229E)
CC and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of
CC Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza
CC 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and
CC pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9);
CC involved in proteolytic cleavage and activation of hemagglutinin (HA)
CC protein which is essential for viral infectivity.
CC {ECO:0000269|PubMed:21068237, ECO:0000269|PubMed:21325420,
CC ECO:0000269|PubMed:23536651, ECO:0000269|PubMed:23966399,
CC ECO:0000269|PubMed:24027332, ECO:0000269|PubMed:24227843,
CC ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32404436,
CC ECO:0000269|PubMed:33051876, ECO:0000269|PubMed:34159616}.
CC -!- SUBUNIT: The catalytically active form interacts with ACE2.
CC {ECO:0000269|PubMed:21068237}.
CC -!- INTERACTION:
CC O15393; Q9BYF1: ACE2; NbExp=3; IntAct=EBI-12549863, EBI-7730807;
CC O15393; P01009: SERPINA1; NbExp=2; IntAct=EBI-12549863, EBI-986224;
CC O15393-2; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-12345267, EBI-10827839;
CC O15393-2; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-12345267, EBI-12109402;
CC O15393-2; P29972: AQP1; NbExp=3; IntAct=EBI-12345267, EBI-745213;
CC O15393-2; O95393: BMP10; NbExp=3; IntAct=EBI-12345267, EBI-3922513;
CC O15393-2; Q12982: BNIP2; NbExp=3; IntAct=EBI-12345267, EBI-752094;
CC O15393-2; Q12983: BNIP3; NbExp=3; IntAct=EBI-12345267, EBI-749464;
CC O15393-2; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-12345267, EBI-12244618;
CC O15393-2; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-12345267, EBI-12062109;
CC O15393-2; O14523: C2CD2L; NbExp=3; IntAct=EBI-12345267, EBI-12822627;
CC O15393-2; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-12345267, EBI-11579371;
CC O15393-2; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-12345267, EBI-11989440;
CC O15393-2; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-12345267, EBI-6165897;
CC O15393-2; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-12345267, EBI-2807956;
CC O15393-2; Q6PI25: CNIH2; NbExp=3; IntAct=EBI-12345267, EBI-12815321;
CC O15393-2; Q8TBE1: CNIH3; NbExp=3; IntAct=EBI-12345267, EBI-12208021;
CC O15393-2; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-12345267, EBI-12019274;
CC O15393-2; Q07325: CXCL9; NbExp=3; IntAct=EBI-12345267, EBI-3911467;
CC O15393-2; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-12345267, EBI-2680384;
CC O15393-2; P81534: DEFB103B; NbExp=3; IntAct=EBI-12345267, EBI-12074168;
CC O15393-2; P56851: EDDM3B; NbExp=3; IntAct=EBI-12345267, EBI-10215665;
CC O15393-2; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12345267, EBI-711490;
CC O15393-2; Q92520: FAM3C; NbExp=3; IntAct=EBI-12345267, EBI-2876774;
CC O15393-2; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-12345267, EBI-12142299;
CC O15393-2; P24593: IGFBP5; NbExp=3; IntAct=EBI-12345267, EBI-720480;
CC O15393-2; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-12345267, EBI-2858252;
CC O15393-2; O75425: MOSPD3; NbExp=3; IntAct=EBI-12345267, EBI-12179105;
CC O15393-2; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-12345267, EBI-10317425;
CC O15393-2; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-12345267, EBI-12092917;
CC O15393-2; Q9Y342: PLLP; NbExp=3; IntAct=EBI-12345267, EBI-3919291;
CC O15393-2; P26678: PLN; NbExp=3; IntAct=EBI-12345267, EBI-692836;
CC O15393-2; P60201-2: PLP1; NbExp=3; IntAct=EBI-12345267, EBI-12188331;
CC O15393-2; Q04941: PLP2; NbExp=4; IntAct=EBI-12345267, EBI-608347;
CC O15393-2; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-12345267, EBI-14199621;
CC O15393-2; P53801: PTTG1IP; NbExp=3; IntAct=EBI-12345267, EBI-3906138;
CC O15393-2; O00767: SCD; NbExp=4; IntAct=EBI-12345267, EBI-2684237;
CC O15393-2; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12345267, EBI-8652744;
CC O15393-2; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-12345267, EBI-9679163;
CC O15393-2; P11686: SFTPC; NbExp=3; IntAct=EBI-12345267, EBI-10197617;
CC O15393-2; P78382: SLC35A1; NbExp=3; IntAct=EBI-12345267, EBI-12870360;
CC O15393-2; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-12345267, EBI-10314552;
CC O15393-2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-12345267, EBI-12188413;
CC O15393-2; O15400: STX7; NbExp=4; IntAct=EBI-12345267, EBI-3221827;
CC O15393-2; Q9UNK0: STX8; NbExp=3; IntAct=EBI-12345267, EBI-727240;
CC O15393-2; P17152: TMEM11; NbExp=3; IntAct=EBI-12345267, EBI-723946;
CC O15393-2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-12345267, EBI-10171534;
CC O15393-2; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-12345267, EBI-10694905;
CC O15393-2; A2RU14: TMEM218; NbExp=3; IntAct=EBI-12345267, EBI-10173151;
CC O15393-2; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-12345267, EBI-347385;
CC O15393-2; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-12345267, EBI-12195227;
CC O15393-2; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-12345267, EBI-12887458;
CC O15393-2; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-12345267, EBI-2852148;
CC O15393-2; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-12345267, EBI-8649725;
CC O15393-2; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-12345267, EBI-12015604;
CC O15393-2; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-12345267, EBI-2548832;
CC O15393-2; P01375: TNF; NbExp=3; IntAct=EBI-12345267, EBI-359977;
CC O15393-2; Q5BVD1: TTMP; NbExp=5; IntAct=EBI-12345267, EBI-10243654;
CC O15393-2; O00526: UPK2; NbExp=3; IntAct=EBI-12345267, EBI-10179682;
CC O15393-2; O95183: VAMP5; NbExp=3; IntAct=EBI-12345267, EBI-10191195;
CC O15393-2; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-12345267, EBI-6256462;
CC O15393-2; O95159: ZFPL1; NbExp=3; IntAct=EBI-12345267, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20382709,
CC ECO:0000269|PubMed:21068237}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:20382709, ECO:0000269|PubMed:21068237}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protease serine 2 catalytic
CC chain]: Secreted {ECO:0000269|PubMed:20382709}. Note=Activated by
CC cleavage and secreted. {ECO:0000269|PubMed:11245484,
CC ECO:0000269|PubMed:20382709}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15393-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15393-2; Sequence=VSP_045083;
CC -!- TISSUE SPECIFICITY: Expressed in several tissues that comprise large
CC populations of epithelial cells with the highest level of transcripts
CC measured in the prostate gland. Expressed in type II pneumocytes in the
CC lung (at protein level). Expressed strongly in small intestine. Also
CC expressed in colon, stomach and salivary gland. Coexpressed with ACE2
CC within lung type II pneumocytes, ileal absorptive enterocytes,
CC intestinal epithelial cells, cornea, gallbladder and nasal goblet
CC secretory cells (Ref.21). {ECO:0000269|PubMed:11169526,
CC ECO:0000269|PubMed:20382709, ECO:0000269|PubMed:21325420,
CC ECO:0000269|PubMed:32404436, ECO:0000269|Ref.21}.
CC -!- INDUCTION: By androgenic hormones in vivo.
CC {ECO:0000269|PubMed:25122198}.
CC -!- PTM: Proteolytically processed; by an autocatalytic mechanism.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TMPRSS2ID42592ch21q22.html";
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DR EMBL; U75329; AAC51784.1; -; mRNA.
DR EMBL; AF123453; AAD37117.1; -; mRNA.
DR EMBL; AF270487; AAK29280.1; -; mRNA.
DR EMBL; AK291813; BAF84502.1; -; mRNA.
DR EMBL; AK296860; BAH12445.1; -; mRNA.
DR EMBL; AK313338; BAG36142.1; -; mRNA.
DR EMBL; AK222784; BAD96504.1; -; mRNA.
DR EMBL; AP001610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09597.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09598.1; -; Genomic_DNA.
DR EMBL; BC051839; AAH51839.1; -; mRNA.
DR CCDS; CCDS33564.1; -. [O15393-1]
DR CCDS; CCDS54486.1; -. [O15393-2]
DR RefSeq; NP_001128571.1; NM_001135099.1. [O15393-2]
DR RefSeq; NP_005647.3; NM_005656.3. [O15393-1]
DR RefSeq; XP_011528033.1; XM_011529731.2.
DR PDB; 7MEQ; X-ray; 1.95 A; A=109-492.
DR PDBsum; 7MEQ; -.
DR AlphaFoldDB; O15393; -.
DR SMR; O15393; -.
DR BioGRID; 112968; 338.
DR IntAct; O15393; 62.
DR STRING; 9606.ENSP00000381588; -.
DR BindingDB; O15393; -.
DR ChEMBL; CHEMBL1795140; -.
DR DrugBank; DB09019; Bromhexine.
DR DrugBank; DB13729; Camostat.
DR DrugBank; DB16737; MM3122.
DR GuidetoPHARMACOLOGY; 2421; -.
DR MEROPS; S01.247; -.
DR TCDB; 8.A.131.1.6; the transmembrane protease serine 3 (tmprss3) family.
DR GlyConnect; 1848; 4 N-Linked glycans (2 sites).
DR GlyGen; O15393; 2 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; O15393; -.
DR PhosphoSitePlus; O15393; -.
DR SwissPalm; O15393; -.
DR BioMuta; TMPRSS2; -.
DR EPD; O15393; -.
DR jPOST; O15393; -.
DR MassIVE; O15393; -.
DR MaxQB; O15393; -.
DR PaxDb; O15393; -.
DR PeptideAtlas; O15393; -.
DR PRIDE; O15393; -.
DR ProteomicsDB; 31938; -.
DR ProteomicsDB; 48634; -. [O15393-1]
DR ABCD; O15393; 1 sequenced antibody.
DR Antibodypedia; 2685; 294 antibodies from 35 providers.
DR DNASU; 7113; -.
DR Ensembl; ENST00000332149.10; ENSP00000330330.5; ENSG00000184012.14. [O15393-1]
DR Ensembl; ENST00000398585.7; ENSP00000381588.3; ENSG00000184012.14. [O15393-2]
DR Ensembl; ENST00000454499.6; ENSP00000389006.2; ENSG00000184012.14. [O15393-1]
DR Ensembl; ENST00000458356.6; ENSP00000391216.1; ENSG00000184012.14. [O15393-1]
DR Ensembl; ENST00000676973.1; ENSP00000504705.1; ENSG00000184012.14. [O15393-1]
DR Ensembl; ENST00000678348.1; ENSP00000503556.1; ENSG00000184012.14. [O15393-1]
DR Ensembl; ENST00000679054.1; ENSP00000502928.1; ENSG00000184012.14. [O15393-1]
DR GeneID; 7113; -.
DR KEGG; hsa:7113; -.
DR MANE-Select; ENST00000332149.10; ENSP00000330330.5; NM_005656.4; NP_005647.3.
DR UCSC; uc002yzj.4; human. [O15393-1]
DR CTD; 7113; -.
DR DisGeNET; 7113; -.
DR GeneCards; TMPRSS2; -.
DR HGNC; HGNC:11876; TMPRSS2.
DR HPA; ENSG00000184012; Tissue enhanced (prostate, stomach).
DR MIM; 602060; gene.
DR neXtProt; NX_O15393; -.
DR OpenTargets; ENSG00000184012; -.
DR PharmGKB; PA36577; -.
DR VEuPathDB; HostDB:ENSG00000184012; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000155207; -.
DR InParanoid; O15393; -.
DR OMA; AQRKSWH; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; O15393; -.
DR TreeFam; TF351678; -.
DR BRENDA; 3.4.21.B60; 2681.
DR PathwayCommons; O15393; -.
DR Reactome; R-HSA-9678110; Attachment and Entry.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR SABIO-RK; O15393; -.
DR SignaLink; O15393; -.
DR SIGNOR; O15393; -.
DR BioGRID-ORCS; 7113; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; TMPRSS2; human.
DR GeneWiki; TMPRSS2; -.
DR GenomeRNAi; 7113; -.
DR Pharos; O15393; Tchem.
DR PRO; PR:O15393; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; O15393; protein.
DR Bgee; ENSG00000184012; Expressed in mucosa of transverse colon and 157 other tissues.
DR ExpressionAtlas; O15393; baseline and differential.
DR Genevisible; O15393; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50287; SRCR_2; 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; Alternative splicing; Autocatalytic cleavage; Cell membrane;
KW Disulfide bond; Glycoprotein; Host-virus interaction; Hydrolase; Membrane;
KW Protease; Reference proteome; Secreted; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..255
FT /note="Transmembrane protease serine 2 non-catalytic chain"
FT /id="PRO_0000027855"
FT CHAIN 256..492
FT /note="Transmembrane protease serine 2 catalytic chain"
FT /id="PRO_0000027856"
FT TOPO_DOM 1..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 112..149
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 150..242
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 256..489
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 441
FT /note="Charge relay system"
FT SITE 255..256
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:11245484"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..126
FT /evidence="ECO:0000250"
FT DISULFID 120..139
FT /evidence="ECO:0000250"
FT DISULFID 133..148
FT /evidence="ECO:0000250"
FT DISULFID 172..231
FT /evidence="ECO:0000250"
FT DISULFID 185..241
FT /evidence="ECO:0000250"
FT DISULFID 244..365
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000255|PROSITE-ProRule:PRU00196, ECO:0000255|PROSITE-
FT ProRule:PRU00274"
FT DISULFID 281..297
FT /evidence="ECO:0000250"
FT DISULFID 410..426
FT /evidence="ECO:0000250"
FT DISULFID 437..465
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MPPAPPGGESGCEERGAAGHIEHSRYLSLLDAVDNSKM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045083"
FT VARIANT 28
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:32867305"
FT /id="VAR_084538"
FT VARIANT 74
FT /note="G -> R"
FT /evidence="ECO:0000269|PubMed:32867305"
FT /id="VAR_084539"
FT VARIANT 160
FT /note="V -> M (in dbSNP:rs12329760)"
FT /evidence="ECO:0000269|PubMed:11414763,
FT ECO:0000269|PubMed:17918732, ECO:0000269|PubMed:32867305,
FT ECO:0000269|PubMed:9325052"
FT /id="VAR_027674"
FT VARIANT 254
FT /note="S -> C"
FT /evidence="ECO:0000269|PubMed:17918732"
FT /id="VAR_038002"
FT VARIANT 329
FT /note="E -> Q (in dbSNP:rs775137340)"
FT /evidence="ECO:0000269|PubMed:17918732,
FT ECO:0000269|PubMed:9325052"
FT /id="VAR_038003"
FT VARIANT 449
FT /note="K -> N (in dbSNP:rs1056602)"
FT /id="VAR_011692"
FT VARIANT 491
FT /note="D -> N (in dbSNP:rs779875214)"
FT /evidence="ECO:0000269|PubMed:17918732"
FT /id="VAR_038004"
FT MUTAGEN 255
FT /note="R->Q: Loss of cleavage."
FT /evidence="ECO:0000269|PubMed:11245484"
FT MUTAGEN 441
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11245484"
FT CONFLICT 26
FT /note="Y -> H (in Ref. 4; BAF84502)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="N -> S (in Ref. 4; BAH12445)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> P (in Ref. 4; BAF84502)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="I -> L (in Ref. 1; AAC51784)"
FT /evidence="ECO:0000305"
FT CONFLICT 489..491
FT /note="RAD -> KAN (in Ref. 1; AAC51784)"
FT /evidence="ECO:0000305"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:7MEQ"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:7MEQ"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:7MEQ"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 278..293
FT /evidence="ECO:0007829|PDB:7MEQ"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:7MEQ"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:7MEQ"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:7MEQ"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:7MEQ"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:7MEQ"
FT TURN 413..418
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 452..461
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:7MEQ"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:7MEQ"
FT HELIX 477..490
FT /evidence="ECO:0007829|PDB:7MEQ"
FT VARIANT O15393-2:8
FT /note="G -> R (in dbSNP:rs200291871)"
FT /evidence="ECO:0000269|PubMed:32867305"
FT /id="VAR_084541"
FT VARIANT O15393-2:8
FT /note="G -> V (in dbSNP:rs75603675)"
FT /evidence="ECO:0000269|PubMed:32867305"
FT /id="VAR_084540"
SQ SEQUENCE 492 AA; 53859 MW; C05B5531C8A311C7 CRC64;
MALNSGSPPA IGPYYENHGY QPENPYPAQP TVVPTVYEVH PAQYYPSPVP QYAPRVLTQA
SNPVVCTQPK SPSGTVCTSK TKKALCITLT LGTFLVGAAL AAGLLWKFMG SKCSNSGIEC
DSSGTCINPS NWCDGVSHCP GGEDENRCVR LYGPNFILQV YSSQRKSWHP VCQDDWNENY
GRAACRDMGY KNNFYSSQGI VDDSGSTSFM KLNTSAGNVD IYKKLYHSDA CSSKAVVSLR
CIACGVNLNS SRQSRIVGGE SALPGAWPWQ VSLHVQNVHV CGGSIITPEW IVTAAHCVEK
PLNNPWHWTA FAGILRQSFM FYGAGYQVEK VISHPNYDSK TKNNDIALMK LQKPLTFNDL
VKPVCLPNPG MMLQPEQLCW ISGWGATEEK GKTSEVLNAA KVLLIETQRC NSRYVYDNLI
TPAMICAGFL QGNVDSCQGD SGGPLVTSKN NIWWLIGDTS WGSGCAKAYR PGVYGNVMVF
TDWIYRQMRA DG
