P37088 (SCNNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amiloride-sensitive sodium channel subunit alpha

Alternative name(s):
Alpha-NaCH
Epithelial Na(+) channel subunit alpha
Short name=Alpha-ENaC
Short name=ENaCA
Nonvoltage-gated sodium channel 1 subunit alpha
SCNEA

Gene names

Name:	SCNN1A
Synonyms:	SCNN1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	669 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception. Ref.22
Enzyme regulation	Activated by WNK1, WNK2, WNK3 and WNK4 By similarity.
Subunit structure	Probable heterotrimer containing one alpha, one beta and one gamma subunit. A delta subunit can replace the alpha subunit. Interacts with the WW domains of NEDD4, NEDD4L, WWP1 and WWP2. Interacts with the full length immature form of PCSK9 (pro-PCSK9). Ref.15 Ref.16 Ref.17 Ref.21 Ref.22 Ref.26
Subcellular location	Apical cell membrane; Multi-pass membrane protein. Cell projection › cilium. Note: In the oviduct and bronchus, located on cilia in multi-ciliated cells. In endometrial non-ciliated epithelial cells, restricted to apical surfaces. Ref.20 Ref.22
Tissue specificity	Expressed in the female reproductive tract, from the fimbrial end of the fallopian tube to the endometrium (at protein level). Expressed in kidney (at protein level). In the respiratory tract, expressed in the bronchial epithelium (at protein level). Highly expressed in lung. Detected at intermediate levels in pancreas and liver, and at low levels in heart and placenta. Isoform 1 and isoform 2 predominate in all tissues. Expression of isoform 3, isoform 4 and isoform 5 is very low or not detectable, except in lung and heart. Ref.14 Ref.20
Induction	By aldosterone. Ref.12
Post-translational modification	Ubiquitinated; this targets individual subunits for endocytosis and proteasome-mediated degradation By similarity. ENaC cleavage by furin, and subsequently by prostasin (PRSS8), leads to a stepwise increase in the open probability of the channel as a result of release of the alpha and gamma subunit inhibitory tracts, respectively. Interaction of ENaC subunit SCNN1B with BPIFA1 protects ENaC against proteolytic activation.
Involvement in disease	Pseudohypoaldosteronism 1, autosomal recessive (PHA1B) [MIM:264350]: A rare salt wasting disease resulting from target organ unresponsiveness to mineralocorticoids. PHA1B is a severe form involving multiple organ systems, and characterized by an often fulminant presentation in the neonatal period with dehydration, hyponatremia, hyperkalemia, metabolic acidosis, failure to thrive and weight loss. Note: The disease is caused by mutations affecting the gene represented in this entry. The degree of channel function impairment differentially affects the renin-aldosterone system and urinary Na/K ratios, resulting in distinct genotype-phenotype relationships in PHA1 patients. Loss-of-function mutations are associated with a severe clinical course and age-dependent hyperactivation of the renin-aldosterone system. This feature is not observed in patients with missense mutations that reduce but do not eliminate channel function. Markedly reduced channel activity results in impaired linear growth and delayed puberty (Ref.19). Ref.19 Ref.28 Ref.31 Bronchiectasis with or without elevated sweat chloride 2 (BESC2) [MIM:613021]: A debilitating respiratory disease characterized by chronic, abnormal dilatation of the bronchi and other cystic fibrosis-like symptoms in the absence of known causes of bronchiectasis (cystic fibrosis, autoimmune diseases, ciliary dyskinesia, common variable immunodeficiency, foreign body obstruction). Clinical features include sub-normal lung function, sinopulmonary infections, chronic productive cough, excessive sputum production, and elevated sweat chloride in some cases. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33
Sequence similarities	Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. SCNN1A subfamily. [View classification]
Sequence caution	The sequence AAH06526.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Ion transport Sensory transduction Sodium transport Taste Transport
Cellular component	Cell membrane Cell projection Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	Sodium
Molecular function	Ion channel Sodium channel
PTM	Glycoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	excretion Traceable author statement PubMed 8589714. Source: ProtInc ion transmembrane transport Traceable author statement. Source: Reactome multicellular organismal water homeostasis Inferred from direct assay Ref.22. Source: UniProtKB response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW sensory perception of taste Inferred from electronic annotation. Source: UniProtKB-KW sodium ion homeostasis Inferred from direct assay Ref.22. Source: UniProtKB sodium ion transmembrane transport Inferred from direct assay Ref.22. Source: UniProtKB sodium ion transport Traceable author statement PubMed 8589714. Source: ProtInc transmembrane transport Traceable author statement. Source: Reactome
Cellular_component	apical plasma membrane Inferred from direct assay Ref.20. Source: UniProtKB ciliary membrane Inferred from direct assay Ref.20. Source: UniProtKB cortical actin cytoskeleton Inferred from electronic annotation. Source: Ensembl cytosol Inferred from electronic annotation. Source: Ensembl external side of plasma membrane Inferred from electronic annotation. Source: Ensembl extracellular vesicular exosome Inferred from direct assay PubMed 15326289. Source: UniProt integral component of plasma membrane Inferred from direct assay Ref.22. Source: UniProtKB motile cilium Inferred from direct assay Ref.20. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome sodium channel complex Inferred from direct assay Ref.22. Source: UniProtKB
Molecular_function	WW domain binding Inferred from physical interaction PubMed 10642508. Source: BHF-UCL ligand-gated sodium channel activity Inferred from electronic annotation. Source: Ensembl protein binding Inferred from physical interaction Ref.16Ref.21. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P37088-1)

Also known as: Alpha ENAC1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P37088-2)

Also known as: Alpha ENAC2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGMARGSLTRVPGVMGEGTQGPELSLDPDPCSPQSTPGLMKGNKLEEQDPRPLQPIPGLM

Isoform 3 (identifier: P37088-3)

Also known as: Alpha ENACx;

The sequence of this isoform differs from the canonical sequence as follows:
     229-245: CNQNKSDCFYQTYSSGV → ELLSLPPPDVWKLLYFG
     246-669: Missing.

Note: Does not give rise to amiloride-sensitive ion current. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 4 (identifier: P37088-4)

Also known as: Alpha ENAC-19;

The sequence of this isoform differs from the canonical sequence as follows:
     327-345: Missing.

Note: Amiloride-sensitive ion current is nearly abolished.

Isoform 5 (identifier: P37088-5)

Also known as: Alpha ENAC+22;

The sequence of this isoform differs from the canonical sequence as follows:
     454-454: G → GQVRSLTPVIPALWEAEAGGSRG

Note: Does not give rise to amiloride-sensitive ion current.

Isoform 6 (identifier: P37088-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSSIKGNKLEEQDPRPLQPIPGLM

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 669

669

Amiloride-sensitive sodium channel subunit alpha

PRO_0000181261

Regions

Topological domain

1 – 86

86

Cytoplasmic By similarity

Transmembrane

87 – 110

24

Helical; By similarity

Topological domain

111 – 543

433

Extracellular By similarity

Transmembrane

544 – 574

31

Helical; By similarity

Topological domain

575 – 669

95

Cytoplasmic By similarity

Amino acid modifications

Glycosylation

232

1

N-linked (GlcNAc...) Potential

Glycosylation

293

1

N-linked (GlcNAc...) Potential

Glycosylation

312

1

N-linked (GlcNAc...) Potential

Glycosylation

397

1

N-linked (GlcNAc...) Potential

Glycosylation

511

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1

1

M → MGMARGSLTRVPGVMGEGTQ GPELSLDPDPCSPQSTPGLM KGNKLEEQDPRPLQPIPGLM in isoform 2.

VSP_007719

Alternative sequence

1

1

M → MSSIKGNKLEEQDPRPLQPI PGLM in isoform 6.

VSP_043667

Alternative sequence

229 – 245

17

CNQNK…YSSGV → ELLSLPPPDVWKLLYFG in isoform 3.

VSP_007720

Alternative sequence

246 – 669

424

Missing in isoform 3.

VSP_007721

Alternative sequence

327 – 345

19

Missing in isoform 4.

VSP_007722

Alternative sequence

454

1

G → GQVRSLTPVIPALWEAEAGG SRG in isoform 5.

VSP_007723

Natural variant

61

1

F → L in BESC2; hypoactive mutation resulting in reduction of protein expression and a significant decrease of amiloride-sensitive sodium currents. Ref.33
Corresponds to variant rs61758859 [ dbSNP | Ensembl ].

VAR_060793

Natural variant

114

1

V → I in BESC2; hyperactive mutation resulting in a significant increase of amiloride-sensitive sodium currents. Ref.33
Corresponds to variant rs61759861 [ dbSNP | Ensembl ].

VAR_060794

Natural variant

181

1

R → W Functional polymorphism; significant increase of amiloride-sensitive sodium currents. Ref.32 Ref.33
Corresponds to variant rs55797039 [ dbSNP | Ensembl ].

VAR_060795

Natural variant

327

1

G → C in PHA1B; results in a significant reduction of channel function as compared to wild-type; significantly lowers both Li+ and Na+ ion currents. Ref.19 Ref.31

VAR_026518

Natural variant

334

1

A → T Functional polymorphism; significant decrease of amiloride-sensitive sodium currents. Ref.24 Ref.33
Corresponds to variant rs11542844 [ dbSNP | Ensembl ].

VAR_060796

Natural variant

402

1

P → H.
Corresponds to variant rs13306616 [ dbSNP | Ensembl ].

VAR_052035

Natural variant

493

1

W → R Functional polymorphism resulting in a 4-fold increase of amiloride-sensitive sodium currents; found in BESC2 patients at higher frequency than in controls; associated with an incresed risk for ischemic cerebrovascular events. Ref.28 Ref.30 Ref.33
Corresponds to variant rs5742912 [ dbSNP | Ensembl ].

VAR_015833

Natural variant

562

1

S → L in PHA1B. Ref.28

VAR_015834

Natural variant

573

1

V → I.
Corresponds to variant rs59142484 [ dbSNP | Ensembl ].

VAR_060797

Natural variant

618

1

C → F. Ref.24
Corresponds to variant rs3741913 [ dbSNP | Ensembl ].

VAR_022142

Natural variant

663

1

T → A. Ref.5 Ref.10 Ref.24 Ref.27 Ref.29 Ref.30 Ref.33
Corresponds to variant rs2228576 [ dbSNP | Ensembl ].

VAR_015835

Secondary structure

1

.

.

.

669

Helix Strand Turn

Details...

Helix

644 – 647

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha ENAC1) [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 2CCF342E7DF32E72	FASTA	669	75,704
	10 20 30 40 50 60 MEGNKLEEQD SSPPQSTPGL MKGNKREEQG LGPEPAAPQQ PTAEEEALIE FHRSYRELFE 70 80 90 100 110 120 FFCNNTTIHG AIRLVCSQHN RMKTAFWAVL WLCTFGMMYW QFGLLFGEYF SYPVSLNINL 130 140 150 160 170 180 NSDKLVFPAV TICTLNPYRY PEIKEELEEL DRITEQTLFD LYKYSSFTTL VAGSRSRRDL 190 200 210 220 230 240 RGTLPHPLQR LRVPPPPHGA RRARSVASSL RDNNPQVDWK DWKIGFQLCN QNKSDCFYQT 250 260 270 280 290 300 YSSGVDAVRE WYRFHYINIL SRLPETLPSL EEDTLGNFIF ACRFNQVSCN QANYSHFHHP 310 320 330 340 350 360 MYGNCYTFND KNNSNLWMSS MPGINNGLSL MLRAEQNDFI PLLSTVTGAR VMVHGQDEPA 370 380 390 400 410 420 FMDDGGFNLR PGVETSISMR KETLDRLGGD YGDCTKNGSD VPVENLYPSK YTQQVCIHSC 430 440 450 460 470 480 FQESMIKECG CAYIFYPRPQ NVEYCDYRKH SSWGYCYYKL QVDFSSDHLG CFTKCRKPCS 490 500 510 520 530 540 VTSYQLSAGY SRWPSVTSQE WVFQMLSRQN NYTVNNKRNG VAKVNIFFKE LNYKTNSESP 550 560 570 580 590 600 SVTMVTLLSN LGSQWSLWFG SSVLSVVEMA ELVFDLLVIM FLMLLRRFRS RYWSPGRGGR 610 620 630 640 650 660 GAQEVASTLA SSPPSHFCPH PMSLSLSQPG PAPSPALTAP PPAYATLGPR PSPGGSAGAS SSTCPLGGP
	Isoform 2 (Alpha ENAC2) [UniParc]. Checksum: 206613374DFB1800	FASTA	728	81,856
	10 20 30 40 50 60 MGMARGSLTR VPGVMGEGTQ GPELSLDPDP CSPQSTPGLM KGNKLEEQDP RPLQPIPGLM 70 80 90 100 110 120 EGNKLEEQDS SPPQSTPGLM KGNKREEQGL GPEPAAPQQP TAEEEALIEF HRSYRELFEF 130 140 150 160 170 180 FCNNTTIHGA IRLVCSQHNR MKTAFWAVLW LCTFGMMYWQ FGLLFGEYFS YPVSLNINLN 190 200 210 220 230 240 SDKLVFPAVT ICTLNPYRYP EIKEELEELD RITEQTLFDL YKYSSFTTLV AGSRSRRDLR 250 260 270 280 290 300 GTLPHPLQRL RVPPPPHGAR RARSVASSLR DNNPQVDWKD WKIGFQLCNQ NKSDCFYQTY 310 320 330 340 350 360 SSGVDAVREW YRFHYINILS RLPETLPSLE EDTLGNFIFA CRFNQVSCNQ ANYSHFHHPM 370 380 390 400 410 420 YGNCYTFNDK NNSNLWMSSM PGINNGLSLM LRAEQNDFIP LLSTVTGARV MVHGQDEPAF 430 440 450 460 470 480 MDDGGFNLRP GVETSISMRK ETLDRLGGDY GDCTKNGSDV PVENLYPSKY TQQVCIHSCF 490 500 510 520 530 540 QESMIKECGC AYIFYPRPQN VEYCDYRKHS SWGYCYYKLQ VDFSSDHLGC FTKCRKPCSV 550 560 570 580 590 600 TSYQLSAGYS RWPSVTSQEW VFQMLSRQNN YTVNNKRNGV AKVNIFFKEL NYKTNSESPS 610 620 630 640 650 660 VTMVTLLSNL GSQWSLWFGS SVLSVVEMAE LVFDLLVIMF LMLLRRFRSR YWSPGRGGRG 670 680 690 700 710 720 AQEVASTLAS SPPSHFCPHP MSLSLSQPGP APSPALTAPP PAYATLGPRP SPGGSAGASS STCPLGGP
	Isoform 3 (Alpha ENACx) [UniParc]. Checksum: FFDC0622FFA37329	FASTA	245	28,328
	10 20 30 40 50 60 MEGNKLEEQD SSPPQSTPGL MKGNKREEQG LGPEPAAPQQ PTAEEEALIE FHRSYRELFE 70 80 90 100 110 120 FFCNNTTIHG AIRLVCSQHN RMKTAFWAVL WLCTFGMMYW QFGLLFGEYF SYPVSLNINL 130 140 150 160 170 180 NSDKLVFPAV TICTLNPYRY PEIKEELEEL DRITEQTLFD LYKYSSFTTL VAGSRSRRDL 190 200 210 220 230 240 RGTLPHPLQR LRVPPPPHGA RRARSVASSL RDNNPQVDWK DWKIGFQLEL LSLPPPDVWK LLYFG
	Isoform 4 (Alpha ENAC-19) [UniParc]. Checksum: 5866D42CCAF6F8B4	FASTA	650	73,603
	10 20 30 40 50 60 MEGNKLEEQD SSPPQSTPGL MKGNKREEQG LGPEPAAPQQ PTAEEEALIE FHRSYRELFE 70 80 90 100 110 120 FFCNNTTIHG AIRLVCSQHN RMKTAFWAVL WLCTFGMMYW QFGLLFGEYF SYPVSLNINL 130 140 150 160 170 180 NSDKLVFPAV TICTLNPYRY PEIKEELEEL DRITEQTLFD LYKYSSFTTL VAGSRSRRDL 190 200 210 220 230 240 RGTLPHPLQR LRVPPPPHGA RRARSVASSL RDNNPQVDWK DWKIGFQLCN QNKSDCFYQT 250 260 270 280 290 300 YSSGVDAVRE WYRFHYINIL SRLPETLPSL EEDTLGNFIF ACRFNQVSCN QANYSHFHHP 310 320 330 340 350 360 MYGNCYTFND KNNSNLWMSS MPGINNVTGA RVMVHGQDEP AFMDDGGFNL RPGVETSISM 370 380 390 400 410 420 RKETLDRLGG DYGDCTKNGS DVPVENLYPS KYTQQVCIHS CFQESMIKEC GCAYIFYPRP 430 440 450 460 470 480 QNVEYCDYRK HSSWGYCYYK LQVDFSSDHL GCFTKCRKPC SVTSYQLSAG YSRWPSVTSQ 490 500 510 520 530 540 EWVFQMLSRQ NNYTVNNKRN GVAKVNIFFK ELNYKTNSES PSVTMVTLLS NLGSQWSLWF 550 560 570 580 590 600 GSSVLSVVEM AELVFDLLVI MFLMLLRRFR SRYWSPGRGG RGAQEVASTL ASSPPSHFCP 610 620 630 640 650 HPMSLSLSQP GPAPSPALTA PPPAYATLGP RPSPGGSAGA SSSTCPLGGP
	Isoform 5 (Alpha ENAC+22) [UniParc]. Checksum: 07B981FBE74AE30B	FASTA	691	77,980
	10 20 30 40 50 60 MEGNKLEEQD SSPPQSTPGL MKGNKREEQG LGPEPAAPQQ PTAEEEALIE FHRSYRELFE 70 80 90 100 110 120 FFCNNTTIHG AIRLVCSQHN RMKTAFWAVL WLCTFGMMYW QFGLLFGEYF SYPVSLNINL 130 140 150 160 170 180 NSDKLVFPAV TICTLNPYRY PEIKEELEEL DRITEQTLFD LYKYSSFTTL VAGSRSRRDL 190 200 210 220 230 240 RGTLPHPLQR LRVPPPPHGA RRARSVASSL RDNNPQVDWK DWKIGFQLCN QNKSDCFYQT 250 260 270 280 290 300 YSSGVDAVRE WYRFHYINIL SRLPETLPSL EEDTLGNFIF ACRFNQVSCN QANYSHFHHP 310 320 330 340 350 360 MYGNCYTFND KNNSNLWMSS MPGINNGLSL MLRAEQNDFI PLLSTVTGAR VMVHGQDEPA 370 380 390 400 410 420 FMDDGGFNLR PGVETSISMR KETLDRLGGD YGDCTKNGSD VPVENLYPSK YTQQVCIHSC 430 440 450 460 470 480 FQESMIKECG CAYIFYPRPQ NVEYCDYRKH SSWGQVRSLT PVIPALWEAE AGGSRGYCYY 490 500 510 520 530 540 KLQVDFSSDH LGCFTKCRKP CSVTSYQLSA GYSRWPSVTS QEWVFQMLSR QNNYTVNNKR 550 560 570 580 590 600 NGVAKVNIFF KELNYKTNSE SPSVTMVTLL SNLGSQWSLW FGSSVLSVVE MAELVFDLLV 610 620 630 640 650 660 IMFLMLLRRF RSRYWSPGRG GRGAQEVAST LASSPPSHFC PHPMSLSLSQ PGPAPSPALT 670 680 690 APPPAYATLG PRPSPGGSAG ASSSTCPLGG P
	Isoform 6 [UniParc]. Checksum: 3AD7710E69D1BE54	FASTA	692	78,234
	10 20 30 40 50 60 MSSIKGNKLE EQDPRPLQPI PGLMEGNKLE EQDSSPPQST PGLMKGNKRE EQGLGPEPAA 70 80 90 100 110 120 PQQPTAEEEA LIEFHRSYRE LFEFFCNNTT IHGAIRLVCS QHNRMKTAFW AVLWLCTFGM 130 140 150 160 170 180 MYWQFGLLFG EYFSYPVSLN INLNSDKLVF PAVTICTLNP YRYPEIKEEL EELDRITEQT 190 200 210 220 230 240 LFDLYKYSSF TTLVAGSRSR RDLRGTLPHP LQRLRVPPPP HGARRARSVA SSLRDNNPQV 250 260 270 280 290 300 DWKDWKIGFQ LCNQNKSDCF YQTYSSGVDA VREWYRFHYI NILSRLPETL PSLEEDTLGN 310 320 330 340 350 360 FIFACRFNQV SCNQANYSHF HHPMYGNCYT FNDKNNSNLW MSSMPGINNG LSLMLRAEQN 370 380 390 400 410 420 DFIPLLSTVT GARVMVHGQD EPAFMDDGGF NLRPGVETSI SMRKETLDRL GGDYGDCTKN 430 440 450 460 470 480 GSDVPVENLY PSKYTQQVCI HSCFQESMIK ECGCAYIFYP RPQNVEYCDY RKHSSWGYCY 490 500 510 520 530 540 YKLQVDFSSD HLGCFTKCRK PCSVTSYQLS AGYSRWPSVT SQEWVFQMLS RQNNYTVNNK 550 560 570 580 590 600 RNGVAKVNIF FKELNYKTNS ESPSVTMVTL LSNLGSQWSL WFGSSVLSVV EMAELVFDLL 610 620 630 640 650 660 VIMFLMLLRR FRSRYWSPGR GGRGAQEVAS TLASSPPSHF CPHPMSLSLS QPGPAPSPAL 670 680 690 TAPPPAYATL GPRPSPGGSA GASSSTCPLG GP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The lung amiloride-sensitive Na+ channel: biophysical properties, pharmacology, ontogenesis, and molecular cloning." Voilley N., Lingueglia E., Champigny G., Mattei M.-G., Waldmann R., Lazdunski M., Barbry P. Proc. Natl. Acad. Sci. U.S.A. 91:247-251(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lung.
[2]	"Cloning, expression, and tissue distribution of a human amiloride-sensitive Na+ channel." McDonald F.J., Snyder P.M., McCray P.B. Jr., Welsh M.J. Am. J. Physiol. 266:L728-L734(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Kidney.
[3]	"Structural organisation of the gene encoding the alpha-subunit of the human amiloride-sensitive epithelial sodium channel." Ludwig M., Bolkenius U., Wickert L., Marynen P., Bidlingmaier F. Hum. Genet. 102:576-581(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Hormonal regulation and genomic organization of the human amiloride-sensitive epithelial sodium channel alpha subunit gene." Chow Y.H., Wang Y., Plumb J., O'Brodovich H., Hu J. Pediatr. Res. 46:208-214(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Upregulated expression of ENaC in human CF nasal epithelium." Bangel N., Dahlhoff C., Sobczak K., Weber W.M., Kusche-Vihrog K. J. Cyst. Fibros. 7:197-205(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-663. Tissue: Nasal epithelium.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Tissue: Trachea.
[7]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-663. Tissue: Colon and Lung.
[11]	"5' heterogeneity in epithelial sodium channel alpha-subunit mRNA leads to distinct NH2-terminal variant proteins." Thomas C.P., Auerbach S.D., Stokes J.B., Volk K.A. Am. J. Physiol. 274:C1312-C1323(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2). Tissue: Kidney.
[12]	"The alpha-subunit of the epithelial sodium channel is an aldosterone-induced transcript in mammalian collecting ducts, and this transcriptional response is mediated via distinct cis-elements in the 5'-flanking region of the gene." Mick V.E., Itani O.A., Loftus R.W., Husted R.F., Schmidt T.J., Thomas C.P. Mol. Endocrinol. 15:575-588(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50 (ISOFORMS 1 AND 2), INDUCTION. Tissue: Placenta.
[13]	"Type I pseudohypoaldosteronism includes two clinically and genetically distinct entities with either renal or multiple target organ defects." Hanukoglu A. J. Clin. Endocrinol. Metab. 73:936-944(1991) [PubMed] [Europe PMC] [Abstract] Cited for: DEFINITION OF DIFFERENT FORMS OF PSEUDOHYPOALDOSTERONISM TYPE 1.
[14]	"Cloning and functional studies of splice variants of the alpha-subunit of the amiloride-sensitive Na+ channel." Tucker J.K., Tamba K., Lee Y.-J., Shen L.-L., Warnock D.G., Oh Y. Am. J. Physiol. 274:C1081-C1089(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 3; 4 AND 5), TISSUE SPECIFICITY.
[15]	"Identification of novel human WW domain-containing proteins by cloning of ligand targets." Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B., Kay B.K., Fowlkes D.M. J. Biol. Chem. 272:14611-14616(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWP1 AND WWP2.
[16]	"The Nedd4-like protein KIAA0439 is a potential regulator of the epithelial sodium channel." Harvey K.F., Dinudom A., Cook D.I., Kumar S. J. Biol. Chem. 276:8597-8601(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEDD4 AND NEDD4L.
[17]	"Ubiquitin-protein ligase WWP2 binds to and downregulates the epithelial Na(+) channel." McDonald F.J., Western A.H., McNeil J.D., Thomas B.C., Olson D.R., Snyder P.M. Am. J. Physiol. 283:F431-F436(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEDD4 AND WWP2.
[18]	"Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation." Carattino M.D., Hughey R.P., Kleyman T.R. J. Biol. Chem. 283:25290-25295(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[19]	"Renin-aldosterone response, urinary Na/K ratio and growth in pseudohypoaldosteronism patients with mutations in epithelial sodium channel (ENaC) subunit genes." Hanukoglu A., Edelheit O., Shriki Y., Gizewska M., Dascal N., Hanukoglu I. J. Steroid Biochem. Mol. Biol. 111:268-274(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GENOTYPE-PHENOTYPE RELATIONSHIPS IN PHA1B, LONG-TERM EFFECTS OF MUTATIONS ON PHA1B, VARIANT PHA1B CYS-327, CHARACTERIZATION OF VARIANT PHA1B CYS-327.
[20]	"Epithelial sodium channels (ENaC) are uniformly distributed on motile cilia in the oviduct and the respiratory airways." Enuka Y., Hanukoglu I., Edelheit O., Vaknine H., Hanukoglu A. Histochem. Cell Biol. 137:339-353(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[21]	"Regulation of epithelial sodium channel trafficking by proprotein convertase subtilisin/kexin type 9 (PCSK9)." Sharotri V., Collier D.M., Olson D.R., Zhou R., Snyder P.M. J. Biol. Chem. 287:19266-19274(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCSK9.
[22]	"Identification of the SPLUNC1 ENaC-inhibitory domain yields novel strategies to treat sodium hyperabsorption in cystic fibrosis airway epithelial cultures." Hobbs C.A., Blanchard M.G., Alijevic O., Tan C.D., Kellenberger S., Bencharit S., Cao R., Kesimer M., Walton W.G., Henderson A.G., Redinbo M.R., Stutts M.J., Tarran R. Am. J. Physiol. 305:L990-L1001(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[23]	"ENaC modulators and renal disease." Alvarez de la Rosa D., Navarro-Gonzalez J.F., Giraldez T. Curr. Mol. Pharmacol. 6:35-43(2013) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[24]	"Genetic variants in the epithelial sodium channel in relation to aldosterone and potassium excretion and risk for hypertension." Ambrosius W.T., Bloem L.J., Zhou L., Rebhun J.F., Snyder P.M., Wagner M.A., Guo C., Pratt J.H. Hypertension 34:631-637(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS THR-334; PHE-618 AND ALA-663.
[25]	Erratum Ambrosius W.T., Bloem L.J., Zhou L., Rebhun J.F., Snyder P.M., Wagner M.A., Guo C., Pratt J.H. Hypertension 41:1E-1E(2003)
[26]	"Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel." Snyder P.M., Olson D.R., Thomas B.C. J. Biol. Chem. 277:5-8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEDD4 AND NEDD4L.
[27]	"Polymorphisms of amiloride-sensitive sodium channel subunits in five sporadic cases of pseudohypoaldosteronism: do they have pathologic potential?" Arai K., Zachman K., Shibasaki T., Chrousos G.P. J. Clin. Endocrinol. Metab. 84:2434-2437(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-663.
[28]	"Lung symptoms in pseudohypoaldosteronism type 1 are associated with deficiency of the alpha-subunit of the epithelial sodium channel." Schaedel C., Marthinsen L., Kristoffersson A.-C., Kornfalt R., Nilsson K.O., Orlenius B., Holmberg L. J. Pediatr. 135:739-745(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PHA1B LEU-562, VARIANT ARG-493.
[29]	"Novel mutations responsible for autosomal recessive multisystem pseudohypoaldosteronism and sequence variants in epithelial sodium channel alpha-, beta-, and gamma-subunit genes." Saxena A., Hanukoglu I., Saxena D., Thompson R.J., Gardiner R.M., Hanukoglu A. J. Clin. Endocrinol. Metab. 87:3344-3350(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-663.
[30]	"Impact of alphaENaC polymorphisms on the risk of ischemic cerebrovascular events: a multicenter case-control study." Hsieh K., Lalouschek W., Schillinger M., Endler G., Reisinger M., Janisiw M., Lang W., Cheng S., Wagner O., Mannhalter C. Clin. Chem. 51:952-956(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-663, ASSOCIATION OF VARIANT ARG-493 WITH RISK FOR ISCHEMIC CEREBROVASCULAR EVENTS.
[31]	"Novel mutations in epithelial sodium channel (ENaC) subunit genes and phenotypic expression of multisystem pseudohypoaldosteronism." Edelheit O., Hanukoglu I., Gizewska M., Kandemir N., Tenenbaum-Rakover Y., Yurdakoek M., Zajaczek S., Hanukoglu A. Clin. Endocrinol. (Oxf.) 62:547-553(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PHA1B CYS-327.
[32]	"Mutations in the beta-subunit of the epithelial Na+ channel in patients with a cystic fibrosis-like syndrome." Sheridan M.B., Fong P., Groman J.D., Conrad C., Flume P., Diaz R., Harris C., Knowles M., Cutting G.R. Hum. Mol. Genet. 14:3493-3498(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TRP-181.
[33]	"Mutations in the amiloride-sensitive epithelial sodium channel in patients with cystic fibrosis-like disease." Azad A.K., Rauh R., Vermeulen F., Jaspers M., Korbmacher J., Boissier B., Bassinet L., Fichou Y., des Georges M., Stanke F., De Boeck K., Dupont L., Balascakova M., Hjelte L., Lebecque P., Radojkovic D., Castellani C., Schwartz M. , Stuhrmann M., Schwarz M., Skalicka V., de Monestrol I., Girodon E., Ferec C., Claustres M., Tuemmler B., Cassiman J.-J., Korbmacher C., Cuppens H. Hum. Mutat. 30:1093-1103(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BESC2 LEU-61 AND ILE-114, VARIANTS TRP-181; THR-334; ARG-493 AND ALA-663, CHARACTERIZATION OF VARIANTS BESC2 LEU-61 AND ILE-114, CHARACTERIZATION OF VARIANTS TRP-181; THR-334 AND ARG-493.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X76180 mRNA. Translation: CAA53773.1.
L29007 Genomic DNA. Translation: AAA21813.1.
Z92978 , Z92979, Z92980, Z92981 Genomic DNA. Translation: CAB07505.1.
AF060913 , AF060910, AF060911, AF060912 Genomic DNA. Translation: AAD28355.1.
DQ402522 mRNA. Translation: ABD72218.1.
AK304379 mRNA. Translation: BAG65217.1.
FJ515830 Genomic DNA. Translation: ACS13721.1.
AC005840 Genomic DNA. No translation available.
AC006057 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88804.1.
BC006526 mRNA. Translation: AAH06526.2. Different initiation.
BC062613 mRNA. Translation: AAH62613.1.
U81961 Genomic DNA. Translation: AAC31773.1.
U81961 Genomic DNA. Translation: AAC31774.1.

CCDS

CCDS53738.1. [P37088-2]
CCDS53739.1. [P37088-6]
CCDS8543.1. [P37088-1]

PIR

A49585.

RefSeq

NP_001029.1. NM_001038.5. [P37088-1]
NP_001153047.1. NM_001159575.1. [P37088-6]
NP_001153048.1. NM_001159576.1. [P37088-2]

UniGene

Hs.591047.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2M3O	NMR	-	P	638-648	[»]

ProteinModelPortal

P37088.

SMR

P37088. Positions 279-566.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

112241. 20 interactions.

MINT

MINT-198663.

STRING

9606.ENSP00000228916.

Chemistry

BindingDB

P37088.

ChEMBL

CHEMBL1791.

DrugBank

DB00594. Amiloride.
DB00384. Triamterene.

Protein family/group databases

TCDB

1.A.6.1.1. the epithelial na(+) channel (enac) family.

PTM databases

PhosphoSite

P37088.

Polymorphism databases

DMDM

585966.

Proteomic databases

PaxDb

P37088.

PRIDE

P37088.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000228916; ENSP00000228916; ENSG00000111319. [P37088-1]
ENST00000360168; ENSP00000353292; ENSG00000111319. [P37088-2]
ENST00000543768; ENSP00000438739; ENSG00000111319. [P37088-6]

GeneID

6337.

KEGG

hsa:6337.

UCSC

uc001qnv.3. human. [P37088-1]
uc001qnw.3. human. [P37088-2]
uc010sfb.2. human. [P37088-6]

Organism-specific databases

CTD

6337.

GeneCards

GC12M006456.

HGNC

HGNC:10599. SCNN1A.

HPA

HPA012743.
HPA012939.

MIM

264350. phenotype.
600228. gene.
613021. phenotype.

neXtProt

NX_P37088.

Orphanet

171876. Generalized pseudohypoaldosteronism type 1.
60033. Idiopathic bronchiectasis.

PharmGKB

PA305.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG288544.

HOGENOM

HOG000236286.

HOVERGEN

HBG058435.

InParanoid

P37088.

KO

K04824.

OMA

SRQNNYT.

OrthoDB

EOG7T1R9N.

PhylomeDB

P37088.

TreeFam

TF330663.

Enzyme and pathway databases

Reactome

REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P37088.

Bgee

P37088.

CleanEx

HS_SCNN1A.

Genevestigator

P37088.

Family and domain databases

InterPro

IPR004724. EnaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]

PANTHER

PTHR11690. PTHR11690. 1 hit.

Pfam

PF00858. ASC. 1 hit.
[Graphical view]

PRINTS

PR01078. AMINACHANNEL.

TIGRFAMs

TIGR00859. ENaC. 1 hit.

PROSITE

PS01206. ASC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SCNN1A. human.

GeneWiki

SCNN1A.

GenomeRNAi

6337.

NextBio

24608.

PRO

P37088.

SOURCE

Search...

Entry information

Entry name

SCNNA_HUMAN

Accession

Primary (citable) accession number: P37088
Secondary accession number(s): A5X2U9 , B4E2Q5, C5HTZ0, O43271, Q6GSQ6, Q9UM64

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	July 9, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.