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Transmembrane protease serine 3 (EC 3.4.21.-) (Serine protease TADG-12) (Tumor-associated differentially-expressed gene 12 protein)

 TMPS3_HUMAN             Reviewed;         454 AA.
P57727; D3DSJ6; Q5USC7; Q6ZMC3;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
07-NOV-2018, entry version 175.
RecName: Full=Transmembrane protease serine 3;
EC=3.4.21.-;
AltName: Full=Serine protease TADG-12;
AltName: Full=Tumor-associated differentially-expressed gene 12 protein;
Name=TMPRSS3; Synonyms=ECHOS1, TADG12; ORFNames=UNQ323/PRO382;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; E AND T).
TISSUE=Ovarian carcinoma;
PubMed=11068177; DOI=10.1016/S0925-4439(00)00058-2;
Underwood L.J., Shigemasa K., Tanimoto H., Beard J.B., Schneider E.N.,
Wang Y., Parmley T.H., O'Brien T.J.;
"Ovarian tumor cells express a novel multi-domain cell surface serine
protease.";
Biochim. Biophys. Acta 1502:337-350(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND D), AND VARIANT ILE-53.
PubMed=11137999; DOI=10.1038/83768;
Scott H.S., Kudoh J., Wattenhofer M., Shibuya K., Berry A., Chrast R.,
Guipponi M., Wang J., Kawasaki K., Asakawa S., Minoshima S.,
Younus F., Mehdi S.Q., Radhakrishna U., Papasavvas M.P., Gehrig C.,
Rossier C., Korostishevsky M., Gal A., Shimizu N., Bonne-Tamir B.,
Antonarakis S.E.;
"Insertion of beta-satellite repeats identifies a transmembrane
protease causing both congenital and childhood onset autosomal
recessive deafness.";
Nat. Genet. 27:59-63(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AND INVOLVEMENT IN DFNB8.
TISSUE=Retina;
PubMed=15447792; DOI=10.1186/1471-2350-5-24;
Ahmed Z.M., Li X.C., Powell S.D., Riazuddin S., Young T.L., Ramzan K.,
Ahmad Z., Luscombe S., Dhillon K., MacLaren L., Ploplis B.,
Shotland L.I., Ives E., Riazuddin S., Friedman T.B., Morell R.J.,
Wilcox E.R.;
"Characterization of a new full length TMPRSS3 isoform and
identification of mutant alleles responsible for nonsyndromic
recessive deafness in Newfoundland and Pakistan.";
BMC Med. Genet. 5:24-24(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND E).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
SUBCELLULAR LOCATION, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF SER-401,
CHARACTERIZATION OF VARIANTS DFNB8 GLY-103; TRP-109; PHE-194; CYS-251;
LEU-404 AND ARG-407, AND FUNCTION IN ENAC CLEAVAGE.
PubMed=12393794; DOI=10.1093/hmg/11.23.2829;
Guipponi M., Vuagniaux G., Wattenhofer M., Shibuya K., Vazquez M.,
Dougherty L., Scamuffa N., Guida E., Okui M., Rossier C., Hancock M.,
Buchet K., Reymond A., Hummler E., Marzella P.L., Kudoh J.,
Shimizu N., Scott H.S., Antonarakis S.E., Rossier B.C.;
"The transmembrane serine protease (TMPRSS3) mutated in deafness
DFNB8/10 activates the epithelial sodium channel (ENaC) in vitro.";
Hum. Mol. Genet. 11:2829-2836(2002).
[10]
VARIANTS DFNB8 CYS-251 AND LEU-404.
PubMed=11462234; DOI=10.1002/humu.1159;
Masmoudi S., Antonarakis S.E., Schwede T., Ghorbel A.M., Gratri M.,
Pappasavas M.P., Drira M., Elgaied-Boulila A., Wattenhofer M.,
Rossier C., Scott H.S., Ayadi H., Guipponi M.;
"Novel missense mutations of TMPRSS3 in two consanguineous Tunisian
families with non-syndromic autosomal recessive deafness.";
Hum. Mutat. 18:101-108(2001).
[11]
VARIANTS DFNB8 TRP-109; PHE-194 AND ARG-407, AND VARIANTS ILE-53;
SER-111 AND VAL-253.
PubMed=11424922; DOI=10.1136/jmg.38.6.396;
Ben-Yosef T., Wattenhofer M., Riazuddin S., Ahmed Z.M., Scott H.S.,
Kudoh J., Shibuya K., Antonarakis S.E., Bonne-Tamir B.,
Radhakrishna U., Naz S., Ahmed Z., Riazuddin S., Pandya A.,
Nance W.E., Wilcox E.R., Friedman T.B., Morell R.J.;
"Novel mutations of TMPRSS3 in four DFNB8/B10 families segregating
congenital autosomal recessive deafness.";
J. Med. Genet. 38:396-400(2001).
[12]
VARIANT DFNB8 GLY-103, AND VARIANTS ASN-173 AND THR-426.
PubMed=11907649; DOI=10.1007/s00109-001-0310-6;
Wattenhofer M., Di Iorio V., Rabionet R., Dougherty L., Pampanos A.,
Schwede T., Montserrat-Sentis B., Arbones L., Iliades T.,
Pasquadibisceglie A., D'Amelio M., Alwan S., Rossier C., Dahl H.-H.M.,
Petersen M.B., Estivill X., Gasparini P., Scott H.S.,
Antonarakis S.E.;
"Mutations in the TMPRSS3 gene are a rare cause of childhood
nonsyndromic deafness in Caucasian patients.";
J. Mol. Med. 80:124-131(2002).
[13]
VARIANTS DFNB8 LEU-216 AND LEU-404.
PubMed=16021470; DOI=10.1007/s00439-005-1332-x;
Wattenhofer M., Sahin-Calapoglu N., Andreasen D., Kalay E., Caylan R.,
Braillard B., Fowler-Jaeger N., Reymond A., Rossier B.C.,
Karaguzel A., Antonarakis S.E.;
"A novel TMPRSS3 missense mutation in a DFNB8/10 family prevents
proteolytic activation of the protein.";
Hum. Genet. 117:528-535(2005).
-!- FUNCTION: Probable serine protease that plays a role in hearing.
Acts as a permissive factor for cochlear hair cell survival and
activation at the onset of hearing and is required for saccular
hair cell survival (By similarity). Activates ENaC (in vitro).
{ECO:0000250, ECO:0000269|PubMed:12393794}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12393794}; Single-pass type II membrane
protein {ECO:0000269|PubMed:12393794}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=A;
IsoId=P57727-1; Sequence=Displayed;
Name=B; Synonyms=C;
IsoId=P57727-2; Sequence=VSP_005391;
Name=D;
IsoId=P57727-3; Sequence=VSP_005392;
Name=T; Synonyms=Truncated, TADG-12V;
IsoId=P57727-4; Sequence=VSP_005393, VSP_005394;
Name=E;
IsoId=P57727-5; Sequence=VSP_013184;
Name=6; Synonyms=TMPRSS3e;
IsoId=P57727-6; Sequence=VSP_047695;
Note=Has a predicted N-terminal signal sequence, indicating it
may be secreted. Expressed in retina, lung, liver, pancreas,
placenta and kidney.;
-!- TISSUE SPECIFICITY: Expressed in many tissues including fetal
cochlea. Isoform T is found at increased levels in some
carcinomas.
-!- PTM: Undergoes autoproteolytic activation.
-!- DISEASE: Deafness, autosomal recessive, 8 (DFNB8) [MIM:601072]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. {ECO:0000269|PubMed:11424922,
ECO:0000269|PubMed:11462234, ECO:0000269|PubMed:11907649,
ECO:0000269|PubMed:12393794, ECO:0000269|PubMed:15447792,
ECO:0000269|PubMed:16021470}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TMPRSS3ID42593ch21q22.html";
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EMBL; AF201380; AAG37012.1; -; mRNA.
EMBL; AB038157; BAB20077.1; -; mRNA.
EMBL; AB038158; BAB20078.1; -; mRNA.
EMBL; AB038159; BAB20079.1; -; mRNA.
EMBL; AB038160; BAB20080.1; -; mRNA.
EMBL; AY633572; AAT66641.1; -; mRNA.
EMBL; AY358458; AAQ88823.1; -; mRNA.
EMBL; AK172842; BAD18806.1; -; mRNA.
EMBL; AP001623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09564.1; -; Genomic_DNA.
EMBL; CH471079; EAX09566.1; -; Genomic_DNA.
EMBL; BC074846; AAH74846.1; -; mRNA.
EMBL; BC074847; AAH74847.1; -; mRNA.
CCDS; CCDS13686.1; -. [P57727-1]
CCDS; CCDS42939.1; -. [P57727-3]
CCDS; CCDS58790.1; -. [P57727-5]
RefSeq; NP_001243246.1; NM_001256317.1. [P57727-5]
RefSeq; NP_076927.1; NM_024022.2. [P57727-1]
RefSeq; NP_115780.1; NM_032404.2. [P57727-2]
RefSeq; NP_115781.1; NM_032405.1. [P57727-3]
UniGene; Hs.208600; -.
ProteinModelPortal; P57727; -.
SMR; P57727; -.
BioGrid; 122236; 38.
IntAct; P57727; 4.
STRING; 9606.ENSP00000291532; -.
MEROPS; S01.079; -.
iPTMnet; P57727; -.
PhosphoSitePlus; P57727; -.
BioMuta; TMPRSS3; -.
DMDM; 13124582; -.
PaxDb; P57727; -.
PeptideAtlas; P57727; -.
PRIDE; P57727; -.
ProteomicsDB; 57016; -.
ProteomicsDB; 57017; -. [P57727-2]
ProteomicsDB; 57018; -. [P57727-3]
ProteomicsDB; 57019; -. [P57727-4]
ProteomicsDB; 57020; -. [P57727-5]
Ensembl; ENST00000291532; ENSP00000291532; ENSG00000160183. [P57727-1]
Ensembl; ENST00000398397; ENSP00000381434; ENSG00000160183. [P57727-3]
Ensembl; ENST00000433957; ENSP00000411013; ENSG00000160183. [P57727-1]
Ensembl; ENST00000644384; ENSP00000494414; ENSG00000160183. [P57727-5]
GeneID; 64699; -.
KEGG; hsa:64699; -.
UCSC; uc002zbc.4; human. [P57727-1]
CTD; 64699; -.
DisGeNET; 64699; -.
EuPathDB; HostDB:ENSG00000160183.13; -.
GeneCards; TMPRSS3; -.
GeneReviews; TMPRSS3; -.
H-InvDB; HIX0040842; -.
HGNC; HGNC:11877; TMPRSS3.
MalaCards; TMPRSS3; -.
MIM; 601072; phenotype.
MIM; 605511; gene.
neXtProt; NX_P57727; -.
OpenTargets; ENSG00000160183; -.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKB; PA36578; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118962; -.
HOGENOM; HOG000251822; -.
HOVERGEN; HBG013304; -.
InParanoid; P57727; -.
KO; K09634; -.
OMA; FNEMIQP; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P57727; -.
TreeFam; TF351678; -.
ChiTaRS; TMPRSS3; human.
GeneWiki; TMPRSS3; -.
GenomeRNAi; 64699; -.
PRO; PR:P57727; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000160183; Expressed in 143 organ(s), highest expression level in oviduct epithelium.
CleanEx; HS_TMPRSS3; -.
ExpressionAtlas; P57727; baseline and differential.
Genevisible; P57727; HS.
GO; GO:0005783; C:endoplasmic reticulum; HDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
GO; GO:0017080; F:sodium channel regulator activity; IDA:MGI.
GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:MGI.
GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
CDD; cd00112; LDLa; 1.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 3.10.250.10; -; 1.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF15494; SRCR_2; 1.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00192; LDLa; 1.
SMART; SM00202; SR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF56487; SSF56487; 1.
SUPFAM; SSF57424; SSF57424; 1.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 1.
PROSITE; PS00420; SRCR_1; 1.
PROSITE; PS50287; SRCR_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Alternative splicing; Autocatalytic cleavage; Complete proteome;
Deafness; Disease mutation; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Hydrolase; Membrane; Non-syndromic deafness;
Polymorphism; Protease; Reference proteome; Serine protease;
Signal-anchor; Transmembrane; Transmembrane helix; Zymogen.
CHAIN 1 454 Transmembrane protease serine 3.
/FTId=PRO_0000088690.
TOPO_DOM 1 48 Cytoplasmic. {ECO:0000255}.
TRANSMEM 49 69 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 70 454 Extracellular. {ECO:0000255}.
DOMAIN 72 108 LDL-receptor class A.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 109 205 SRCR. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 217 449 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 257 257 Charge relay system. {ECO:0000250}.
ACT_SITE 304 304 Charge relay system. {ECO:0000250}.
ACT_SITE 401 401 Charge relay system. {ECO:0000305}.
SITE 216 217 Cleavage. {ECO:0000255}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 73 85 {ECO:0000250}.
DISULFID 79 98 {ECO:0000250}.
DISULFID 92 107 {ECO:0000250}.
DISULFID 129 194 {ECO:0000250}.
DISULFID 142 204 {ECO:0000250}.
DISULFID 207 324 {ECO:0000250}.
DISULFID 242 258 {ECO:0000250}.
DISULFID 338 407 {ECO:0000250}.
DISULFID 370 386 {ECO:0000250}.
DISULFID 397 425 {ECO:0000250}.
VAR_SEQ 1 127 Missing (in isoform B).
{ECO:0000303|PubMed:11137999}.
/FTId=VSP_005391.
VAR_SEQ 1 1 M -> MQAVGPKPLPTLLCGGRTGHRTARVLSFLIRSCPCE
PGKGCVYGKPVTLWPTISSVVPSTFLGLGNYEVEVEAEPDV
RGPEIVTM (in isoform 6).
{ECO:0000303|PubMed:15447792}.
/FTId=VSP_047695.
VAR_SEQ 261 293 DLYLPKSWTIQVGLVSLLDNPAPSHLVEKIVYH -> EIVA
PRERADRRGRKLLCWRKPTKMKGPRPSHS (in isoform
T). {ECO:0000303|PubMed:11068177}.
/FTId=VSP_005393.
VAR_SEQ 294 454 Missing (in isoform T).
{ECO:0000303|PubMed:11068177}.
/FTId=VSP_005394.
VAR_SEQ 318 454 EMIQPVCLPNSEENFPDGKVCWTSGWGATEDGAGDASPVLN
HAAVPLISNKICNHRDVYGGIISPSMLCAGYLTGGVDSCQG
DSGGPLVCQERRLWKLVGATSFGIGCAEVNKPGVYTRVTSF
LDWIHEQMERDLKT -> GTSGSLCGSAALPLFQEDLQLLI
EAFL (in isoform D).
{ECO:0000303|PubMed:11137999}.
/FTId=VSP_005392.
VAR_SEQ 350 350 Missing (in isoform E).
{ECO:0000303|PubMed:11068177,
ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_013184.
VARIANT 53 53 V -> I (in dbSNP:rs928302).
{ECO:0000269|PubMed:11137999,
ECO:0000269|PubMed:11424922}.
/FTId=VAR_010781.
VARIANT 103 103 D -> G (in DFNB8; fails to undergo
proteolytic cleavage and is unable to
activate ENaC; dbSNP:rs387906915).
{ECO:0000269|PubMed:11907649,
ECO:0000269|PubMed:12393794}.
/FTId=VAR_013490.
VARIANT 109 109 R -> W (in DFNB8; fails to undergo
proteolytic cleavage and is unable to
activate ENaC; dbSNP:rs201632198).
{ECO:0000269|PubMed:11424922,
ECO:0000269|PubMed:12393794}.
/FTId=VAR_013491.
VARIANT 111 111 G -> S (in dbSNP:rs35227181).
{ECO:0000269|PubMed:11424922}.
/FTId=VAR_013492.
VARIANT 173 173 D -> N (in dbSNP:rs766000719).
{ECO:0000269|PubMed:11907649}.
/FTId=VAR_013493.
VARIANT 194 194 C -> F (in DFNB8; fails to undergo
proteolytic cleavage and is unable to
activate ENaC).
{ECO:0000269|PubMed:11424922,
ECO:0000269|PubMed:12393794}.
/FTId=VAR_013494.
VARIANT 216 216 R -> L (in DFNB8; fails to undergo
proteolytic cleavage and is unable to
activate ENaC; dbSNP:rs137853000).
{ECO:0000269|PubMed:16021470}.
/FTId=VAR_025354.
VARIANT 251 251 W -> C (in DFNB8; fails to undergo
proteolytic cleavage and is unable to
activate ENaC; dbSNP:rs137852999).
{ECO:0000269|PubMed:11462234,
ECO:0000269|PubMed:12393794}.
/FTId=VAR_011678.
VARIANT 253 253 I -> V (in dbSNP:rs2839500).
{ECO:0000269|PubMed:11424922}.
/FTId=VAR_013101.
VARIANT 404 404 P -> L (in DFNB8; fails to undergo
proteolytic cleavage and is unable to
activate ENaC; dbSNP:rs28939084).
{ECO:0000269|PubMed:11462234,
ECO:0000269|PubMed:12393794,
ECO:0000269|PubMed:16021470}.
/FTId=VAR_011679.
VARIANT 407 407 C -> R (in DFNB8; fails to undergo
proteolytic cleavage and is unable to
activate ENaC; dbSNP:rs773780151).
{ECO:0000269|PubMed:11424922,
ECO:0000269|PubMed:12393794}.
/FTId=VAR_013495.
VARIANT 426 426 A -> T (in dbSNP:rs56264519).
{ECO:0000269|PubMed:11907649}.
/FTId=VAR_013496.
MUTAGEN 401 401 S->A: Fails to undergo proteolytic
cleavage and is unable to activate ENaC.
{ECO:0000269|PubMed:12393794}.
CONFLICT 46 54 LKFFPIIVI -> FEVFSQSSSL (in Ref. 1;
AAG37012). {ECO:0000305}.
CONFLICT 90 90 A -> T (in Ref. 1; AAG37012).
{ECO:0000305}.
CONFLICT 369 395 ICNHRDVYGGIISPSMLCAGYLTGGVD -> DLQPQGRVRW
HHLPLHALRGLPDGWRWN (in Ref. 1; AAG37012).
{ECO:0000305}.
CONFLICT 427 427 E -> D (in Ref. 1; AAG37012).
{ECO:0000305}.
SEQUENCE 454 AA; 49405 MW; 57ECC3678F7D6AFF CRC64;
MGENDPPAVE APFSFRSLFG LDDLKISPVA PDADAVAAQI LSLLPLKFFP IIVIGIIALI
LALAIGLGIH FDCSGKYRCR SSFKCIELIA RCDGVSDCKD GEDEYRCVRV GGQNAVLQVF
TAASWKTMCS DDWKGHYANV ACAQLGFPSY VSSDNLRVSS LEGQFREEFV SIDHLLPDDK
VTALHHSVYV REGCASGHVV TLQCTACGHR RGYSSRIVGG NMSLLSQWPW QASLQFQGYH
LCGGSVITPL WIITAAHCVY DLYLPKSWTI QVGLVSLLDN PAPSHLVEKI VYHSKYKPKR
LGNDIALMKL AGPLTFNEMI QPVCLPNSEE NFPDGKVCWT SGWGATEDGA GDASPVLNHA
AVPLISNKIC NHRDVYGGII SPSMLCAGYL TGGVDSCQGD SGGPLVCQER RLWKLVGATS
FGIGCAEVNK PGVYTRVTSF LDWIHEQMER DLKT


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