GENTAUR Molecular Products.

 SCNNG_HUMAN             Reviewed;         649 AA.
 P51170; P78437; Q6PCC2; Q93023; Q93024; Q93025; Q93026; Q93027;
 Q96TD2;
 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
 30-MAY-2006, sequence version 4.
 05-DEC-2018, entry version 184.
 RecName: Full=Amiloride-sensitive sodium channel subunit gamma;
 AltName: Full=Epithelial Na(+) channel subunit gamma;
          Short=ENaCG;
          Short=Gamma-ENaC;
 AltName: Full=Gamma-NaCH;
 AltName: Full=Nonvoltage-gated sodium channel 1 subunit gamma;
 AltName: Full=SCNEG;
 Name=SCNN1G;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
 LOCATION.
 TISSUE=Lung;
 PubMed=7490094; DOI=10.1006/geno.1995.1188;
 Voilley N., Bassilana F., Mignon C., Merscher S., Mattei M.-G.,
 Carle G.F., Lazdunski M., Barbry P.;
 "Cloning, chromosomal localization, and physical linkage of the beta
 and gamma subunits (SCNN1B and SCNN1G) of the human epithelial
 amiloride-sensitive sodium channel.";
 Genomics 28:560-565(1995).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TRP-178; PRO-502 AND SER-614, AND
 SUBUNIT.
 TISSUE=Kidney;
 PubMed=7762608;
 McDonald F.J., Snyder P.M., Price M.P., Welsh M.J.;
 "Cloning and expression of the beta- and gamma-subunits of the human
 epithelial sodium channel.";
 Am. J. Physiol. 268:C1157-C1163(1995).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-502.
 PubMed=12107247; DOI=10.1210/jc.87.7.3344;
 Saxena A., Hanukoglu I., Saxena D., Thompson R.J., Gardiner R.M.,
 Hanukoglu A.;
 "Novel mutations responsible for autosomal recessive multisystem
 pseudohypoaldosteronism and sequence variants in epithelial sodium
 channel alpha-, beta-, and gamma-subunit genes.";
 J. Clin. Endocrinol. Metab. 87:3344-3350(2002).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Placenta;
 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).
 [5]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-105; 218-269; 306-392;
 433-463 AND 499-515, AND VARIANT PRO-502.
 PubMed=8824247; DOI=10.1074/jbc.271.42.26062;
 Thomas C.P., Doggett N.A., Fisher R., Stokes J.B.;
 "Genomic organization and the 5' flanking region of the gamma subunit
 of the human amiloride-sensitive epithelial sodium channel.";
 J. Biol. Chem. 271:26062-26066(1996).
 [6]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 524-649, AND INVOLVEMENT IN
 LIDLS.
 PubMed=7550319; DOI=10.1038/ng0995-76;
 Hansson J.H., Nelson-Williams C., Suzuki H., Schild L., Shimkets R.A.,
 Lu Y., Canessa C.M., Iwasaki T., Rossier B.C., Lifton R.P.;
 "Hypertension caused by a truncated epithelial sodium channel gamma
 subunit: genetic heterogeneity of Liddle syndrome.";
 Nat. Genet. 11:76-82(1995).
 [7]
 INTERACTION WITH WWP1 AND WWP2.
 PubMed=9169421; DOI=10.1074/jbc.272.23.14611;
 Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B.,
 Kay B.K., Fowlkes D.M.;
 "Identification of novel human WW domain-containing proteins by
 cloning of ligand targets.";
 J. Biol. Chem. 272:14611-14616(1997).
 [8]
 INTERACTION WITH NEDD4 AND NEDD4L.
 PubMed=11244092; DOI=10.1074/jbc.C000906200;
 Harvey K.F., Dinudom A., Cook D.I., Kumar S.;
 "The Nedd4-like protein KIAA0439 is a potential regulator of the
 epithelial sodium channel.";
 J. Biol. Chem. 276:8597-8601(2001).
 [9]
 INTERACTION WITH NEDD4 AND WWP2.
 PubMed=12167593; DOI=10.1152/ajprenal.00080.2002;
 McDonald F.J., Western A.H., McNeil J.D., Thomas B.C., Olson D.R.,
 Snyder P.M.;
 "Ubiquitin-protein ligase WWP2 binds to and downregulates the
 epithelial Na(+) channel.";
 Am. J. Physiol. 283:F431-F436(2002).
 [10]
 PROTEOLYTIC PROCESSING.
 PubMed=18650438; DOI=10.1074/jbc.M803931200;
 Carattino M.D., Hughey R.P., Kleyman T.R.;
 "Proteolytic processing of the epithelial sodium channel gamma subunit
 has a dominant role in channel activation.";
 J. Biol. Chem. 283:25290-25295(2008).
 [11]
 INVOLVEMENT IN BESC3.
 PubMed=19017867; DOI=10.1378/chest.08-2246;
 Mutesa L., Azad A.K., Verhaeghe C., Segers K., Vanbellinghen J.F.,
 Ngendahayo L., Rusingiza E.K., Mutwa P.R., Rulisa S., Koulischer L.,
 Cassiman J.J., Cuppens H., Bours V.;
 "Genetic analysis of Rwandan patients with cystic fibrosis-like
 symptoms: identification of novel cystic fibrosis transmembrane
 conductance regulator and epithelial sodium channel gene variants.";
 Chest 135:1233-1242(2009).
 [12]
 TISSUE SPECIFICITY.
 PubMed=22207244; DOI=10.1007/s00418-011-0904-1;
 Enuka Y., Hanukoglu I., Edelheit O., Vaknine H., Hanukoglu A.;
 "Epithelial sodium channels (ENaC) are uniformly distributed on motile
 cilia in the oviduct and the respiratory airways.";
 Histochem. Cell Biol. 137:339-353(2012).
 [13]
 INTERACTION WITH PCSK9.
 PubMed=22493497; DOI=10.1074/jbc.M112.363382;
 Sharotri V., Collier D.M., Olson D.R., Zhou R., Snyder P.M.;
 "Regulation of epithelial sodium channel trafficking by proprotein
 convertase subtilisin/kexin type 9 (PCSK9).";
 J. Biol. Chem. 287:19266-19274(2012).
 [14]
 PROTEOLYTIC PROCESSING, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
 PubMed=24124190; DOI=10.1152/ajplung.00103.2013;
 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.;
 "Identification of the SPLUNC1 ENaC-inhibitory domain yields novel
 strategies to treat sodium hyperabsorption in cystic fibrosis airway
 epithelial cultures.";
 Am. J. Physiol. 305:L990-L1001(2013).
 [15]
 REVIEW.
 PubMed=23547933;
 Alvarez de la Rosa D., Navarro-Gonzalez J.F., Giraldez T.;
 "ENaC modulators and renal disease.";
 Curr. Mol. Pharmacol. 6:35-43(2013).
 [16]
 PHYLOGENETIC ANALYSIS, AND NOMENCLATURE.
 PubMed=26772908; DOI=10.1016/j.gene.2015.12.061;
 Hanukoglu I., Hanukoglu A.;
 "Epithelial sodium channel (ENaC) family: Phylogeny, structure-
 function, tissue distribution, and associated inherited diseases.";
 Gene 579:95-132(2016).
 [17]
 VARIANTS TRP-178; PRO-502 AND SER-614.
 PubMed=10404817; DOI=10.1210/jcem.84.7.5857;
 Arai K., Zachman K., Shibasaki T., Chrousos G.P.;
 "Polymorphisms of amiloride-sensitive sodium channel subunits in five
 sporadic cases of pseudohypoaldosteronism: do they have pathologic
 potential?";
 J. Clin. Endocrinol. Metab. 84:2434-2437(1999).
 [18]
 VARIANTS CYS-49 AND SER-183.
 PubMed=10391210; DOI=10.1038/10297;
 Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
 Cooper R., Lipshutz R., Chakravarti A.;
 "Patterns of single-nucleotide polymorphisms in candidate genes for
 blood-pressure homeostasis.";
 Nat. Genet. 22:239-247(1999).
 [19]
 VARIANT [LARGE SCALE ANALYSIS] ARG-58.
 PubMed=16959974; DOI=10.1126/science.1133427;
 Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
 Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
 Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
 Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
 Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
 Vogelstein B., Kinzler K.W., Velculescu V.E.;
 "The consensus coding sequences of human breast and colorectal
 cancers.";
 Science 314:268-274(2006).
 [20]
 VARIANTS SER-183 AND LYS-197, AND INVOLVEMENT IN BESC3.
 PubMed=18507830; DOI=10.1186/1465-9921-9-46;
 Fajac I., Viel M., Sublemontier S., Hubert D., Bienvenu T.;
 "Could a defective epithelial sodium channel lead to bronchiectasis.";
 Respir. Res. 9:46-46(2008).
 -!- 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. {ECO:0000269|PubMed:24124190,
     ECO:0000303|PubMed:7490094}.
 -!- ACTIVITY REGULATION: Activated by WNK1, WNK2, WNK3 and WNK4.
     {ECO:0000250|UniProtKB:Q9WU39}.
 -!- SUBUNIT: Heterotrimer containing an alpha/SCNN1A, a beta/SCNN1B
     and a gamma/SCNN1G subunit. An additional delta/SCNN1D subunit
     exists only in some organisms and can replace the alpha/SCNN1A
     subunit to form an alternative channel with specific properties
     (PubMed:7762608). Interacts with NEDD4; via the WW domains
     (PubMed:11244092, PubMed:12167593). Interacts with NEDD4L; via the
     WW domains (PubMed:11244092). Interacts with WWP1; via the WW
     domains (PubMed:9169421). Interacts with WWP2; via the WW domains
     (PubMed:9169421, PubMed:12167593). Interacts with the full-length
     immature form of PCSK9 (pro-PCSK9) (PubMed:22493497).
     {ECO:0000269|PubMed:11244092, ECO:0000269|PubMed:12167593,
     ECO:0000269|PubMed:22493497, ECO:0000269|PubMed:24124190,
     ECO:0000269|PubMed:7490094, ECO:0000269|PubMed:7762608,
     ECO:0000269|PubMed:9169421}.
 -!- INTERACTION:
     P37088:SCNN1A; NbExp=3; IntAct=EBI-2547354, EBI-7845444;
 -!- SUBCELLULAR LOCATION: Apical cell membrane
     {ECO:0000269|PubMed:24124190, ECO:0000303|PubMed:7490094}; Multi-
     pass membrane protein {ECO:0000250|UniProtKB:P37089}. Note=Apical
     membrane of epithelial cells. {ECO:0000303|PubMed:7490094}.
 -!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
     {ECO:0000269|PubMed:22207244}.
 -!- PTM: Phosphorylated on serine and threonine residues. Aldosterone
     and insulin increase the basal level of phosphorylation.
     {ECO:0000250|UniProtKB:P37091}.
 -!- PTM: Ubiquitinated; this targets individual subunits for
     endocytosis and proteasome-mediated degradation.
     {ECO:0000250|UniProtKB:P37091}.
 -!- PTM: 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.
     {ECO:0000269|PubMed:18650438, ECO:0000269|PubMed:24124190}.
 -!- DISEASE: Liddle syndrome (LIDLS) [MIM:177200]: An autosomal
     dominant disorder characterized by hypertension, hypokalemic
     alkalosis, and suppression of plasma renin activity and
     aldosterone secretion. {ECO:0000269|PubMed:7550319}. Note=The
     disease is caused by mutations affecting the gene represented in
     this entry.
 -!- DISEASE: Bronchiectasis with or without elevated sweat chloride 3
     (BESC3) [MIM:613071]: 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.
     {ECO:0000269|PubMed:18507830, ECO:0000269|PubMed:19017867}.
     Note=The disease is caused by mutations affecting the gene
     represented in this entry.
 -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
     1.A.6) family. SCNN1G subfamily. {ECO:0000305}.
 -----------------------------------------------------------------------
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 -----------------------------------------------------------------------
 EMBL; X87160; CAA60633.1; -; mRNA.
 EMBL; L36592; AAA75460.1; -; mRNA.
 EMBL; AF356502; AAK50910.1; -; Genomic_DNA.
 EMBL; AF356493; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; AF356494; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; AF356495; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; AF356496; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; AF356497; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; AF356498; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; AF356499; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; AF356500; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; AF356501; AAK50910.1; JOINED; Genomic_DNA.
 EMBL; BC059391; AAH59391.1; -; mRNA.
 EMBL; BC069652; AAH69652.1; -; mRNA.
 EMBL; U48936; AAC50737.1; -; mRNA.
 EMBL; U53836; AAC50744.1; -; Genomic_DNA.
 EMBL; U53837; AAC50745.1; -; Genomic_DNA.
 EMBL; U53841; AAC50749.1; -; Genomic_DNA.
 EMBL; U53844; AAC50752.1; -; Genomic_DNA.
 EMBL; U53845; AAC50753.1; -; Genomic_DNA.
 EMBL; U53846; AAC50754.1; -; Genomic_DNA.
 EMBL; U53847; AAC50755.1; -; Genomic_DNA.
 EMBL; U53850; AAC50758.1; -; Genomic_DNA.
 EMBL; U53852; AAC50760.1; -; Genomic_DNA.
 EMBL; U35630; AAC50217.1; -; Genomic_DNA.
 CCDS; CCDS10608.1; -.
 PIR; I38204; I38204.
 PIR; I64847; I64847.
 RefSeq; NP_001030.2; NM_001039.3.
 UniGene; Hs.371727; -.
 ProteinModelPortal; P51170; -.
 BioGrid; 112244; 14.
 ComplexPortal; CPX-2188; Amiloride-sensitive sodium channel complex, alpha-beta-gamma.
 ComplexPortal; CPX-312; Amiloride-sensitive sodium channel complex, delta-alpha-beta-gamma.
 ComplexPortal; CPX-313; Amiloride-sensitive sodium channel complex, delta-beta-gamma.
 CORUM; P51170; -.
 ELM; P51170; -.
 IntAct; P51170; 3.
 MINT; P51170; -.
 STRING; 9606.ENSP00000300061; -.
 ChEMBL; CHEMBL2107836; -.
 DrugBank; DB00594; Amiloride.
 DrugBank; DB00384; Triamterene.
 GuidetoPHARMACOLOGY; 741; -.
 TCDB; 1.A.6.1.1; the epithelial na(+) channel (enac) family.
 iPTMnet; P51170; -.
 PhosphoSitePlus; P51170; -.
 BioMuta; SCNN1G; -.
 DMDM; 108885072; -.
 EPD; P51170; -.
 PaxDb; P51170; -.
 PeptideAtlas; P51170; -.
 PRIDE; P51170; -.
 ProteomicsDB; 56297; -.
 Ensembl; ENST00000300061; ENSP00000300061; ENSG00000166828.
 GeneID; 6340; -.
 KEGG; hsa:6340; -.
 UCSC; uc002dlm.2; human.
 CTD; 6340; -.
 DisGeNET; 6340; -.
 EuPathDB; HostDB:ENSG00000166828.2; -.
 GeneCards; SCNN1G; -.
 HGNC; HGNC:10602; SCNN1G.
 HPA; HPA071194; -.
 MalaCards; SCNN1G; -.
 MIM; 177200; phenotype.
 MIM; 600761; gene.
 MIM; 613071; phenotype.
 neXtProt; NX_P51170; -.
 OpenTargets; ENSG00000166828; -.
 Orphanet; 171876; Generalized pseudohypoaldosteronism type 1.
 Orphanet; 60033; Idiopathic bronchiectasis.
 Orphanet; 526; Liddle syndrome.
 PharmGKB; PA307; -.
 eggNOG; KOG4294; Eukaryota.
 eggNOG; ENOG410ZNFK; LUCA.
 GeneTree; ENSGT00940000160352; -.
 HOVERGEN; HBG058435; -.
 InParanoid; P51170; -.
 KO; K04827; -.
 OMA; AQWPSVV; -.
 OrthoDB; EOG091G0KW6; -.
 PhylomeDB; P51170; -.
 TreeFam; TF330663; -.
 Reactome; R-HSA-2672351; Stimuli-sensing channels.
 SIGNOR; P51170; -.
 GeneWiki; SCNN1G; -.
 GenomeRNAi; 6340; -.
 PRO; PR:P51170; -.
 Proteomes; UP000005640; Chromosome 16.
 Bgee; ENSG00000166828; Expressed in 94 organ(s), highest expression level in adult mammalian kidney.
 ExpressionAtlas; P51170; baseline and differential.
 Genevisible; P51170; HS.
 GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
 GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
 GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
 GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
 GO; GO:0005654; C:nucleoplasm; IDA:HPA.
 GO; GO:0005886; C:plasma membrane; IDA:HPA.
 GO; GO:0034706; C:sodium channel complex; IDA:UniProtKB.
 GO; GO:0005216; F:ion channel activity; IMP:CACAO.
 GO; GO:0015280; F:ligand-gated sodium channel activity; TAS:ProtInc.
 GO; GO:0005272; F:sodium channel activity; TAS:ProtInc.
 GO; GO:0050699; F:WW domain binding; IPI:BHF-UCL.
 GO; GO:0007588; P:excretion; TAS:ProtInc.
 GO; GO:0050891; P:multicellular organismal water homeostasis; IDA:UniProtKB.
 GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
 GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
 GO; GO:0055078; P:sodium ion homeostasis; IDA:UniProtKB.
 GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
 GO; GO:0006814; P:sodium ion transport; TAS:ProtInc.
 InterPro; IPR001873; ENaC.
 InterPro; IPR004724; ENaC_chordates.
 InterPro; IPR020903; ENaC_CS.
 PANTHER; PTHR11690; PTHR11690; 1.
 Pfam; PF00858; ASC; 1.
 PRINTS; PR01078; AMINACHANNEL.
 TIGRFAMs; TIGR00859; ENaC; 1.
 PROSITE; PS01206; ASC; 1.
 1: Evidence at protein level;
 Cell membrane; Complete proteome; Glycoprotein; Ion channel;
 Ion transport; Membrane; Phosphoprotein; Polymorphism;
 Reference proteome; Sensory transduction; Sodium; Sodium channel;
 Sodium transport; Taste; Transmembrane; Transmembrane helix;
 Transport; Ubl conjugation.
 CHAIN         1    649       Amiloride-sensitive sodium channel
                              subunit gamma.
                              /FTId=PRO_0000181276.
 TOPO_DOM      1     55       Cytoplasmic.
                              {ECO:0000250|UniProtKB:P37089}.
 TRANSMEM     56     76       Helical; Name=1. {ECO:0000255}.
 TOPO_DOM     77    541       Extracellular.
                              {ECO:0000250|UniProtKB:P37089}.
 TRANSMEM    542    562       Helical; Name=2. {ECO:0000255}.
 TOPO_DOM    563    649       Cytoplasmic.
                              {ECO:0000250|UniProtKB:P37089}.
 CARBOHYD    209    209       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    497    497       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 VARIANT      49     49       G -> C (in dbSNP:rs5733).
                              {ECO:0000269|PubMed:10391210}.
                              /FTId=VAR_014893.
 VARIANT      58     58       G -> R (in a colorectal cancer sample;
                              somatic mutation; dbSNP:rs1183385193).
                              {ECO:0000269|PubMed:16959974}.
                              /FTId=VAR_036483.
 VARIANT     178    178       R -> W. {ECO:0000269|PubMed:10404817,
                              ECO:0000269|PubMed:7762608}.
                              /FTId=VAR_015842.
 VARIANT     183    183       G -> S (in a patient with bronchiectasis;
                              dbSNP:rs5736).
                              {ECO:0000269|PubMed:10391210,
                              ECO:0000269|PubMed:18507830}.
                              /FTId=VAR_014894.
 VARIANT     197    197       E -> K (in a patient with bronchiectasis;
                              dbSNP:rs5738).
                              {ECO:0000269|PubMed:18507830}.
                              /FTId=VAR_034485.
 VARIANT     502    502       A -> P. {ECO:0000269|PubMed:10404817,
                              ECO:0000269|PubMed:12107247,
                              ECO:0000269|PubMed:7762608,
                              ECO:0000269|PubMed:8824247}.
                              /FTId=VAR_015843.
 VARIANT     614    614       A -> S. {ECO:0000269|PubMed:10404817,
                              ECO:0000269|PubMed:7762608}.
                              /FTId=VAR_015844.
 CONFLICT    339    339       F -> S (in Ref. 1; CAA60633).
                              {ECO:0000305}.
 CONFLICT    350    350       A -> T (in Ref. 1; CAA60633).
                              {ECO:0000305}.
 CONFLICT    369    369       Y -> S (in Ref. 1; CAA60633).
                              {ECO:0000305}.
 CONFLICT    375    375       D -> G (in Ref. 1; CAA60633).
                              {ECO:0000305}.
 CONFLICT    458    458       S -> R (in Ref. 1; CAA60633).
                              {ECO:0000305}.
 CONFLICT    461    463       EWT -> DGH (in Ref. 5; AAC50758).
                              {ECO:0000305}.
 SEQUENCE   649 AA;  74270 MW;  F67ED45F03A9BF3F CRC64;
 MAPGEKIKAK IKKNLPVTGP QAPTIKELMR WYCLNTNTHG CRRIVVSRGR LRRLLWIGFT
 LTAVALILWQ CALLVFSFYT VSVSIKVHFR KLDFPAVTIC NINPYKYSTV RHLLADLEQE
 TREALKSLYG FPESRKRREA ESWNSVSEGK QPRFSHRIPL LIFDQDEKGK ARDFFTGRKR
 KVGGSIIHKA SNVMHIESKQ VVGFQLCSND TSDCATYTFS SGINAIQEWY KLHYMNIMAQ
 VPLEKKINMS YSAEELLVTC FFDGVSCDAR NFTLFHHPMH GNCYTFNNRE NETILSTSMG
 GSEYGLQVIL YINEEEYNPF LVSSTGAKVI IHRQDEYPFV EDVGTEIETA MVTSIGMHLT
 ESFKLSEPYS QCTEDGSDVP IRNIYNAAYS LQICLHSCFQ TKMVEKCGCA QYSQPLPPAA
 NYCNYQQHPN WMYCYYQLHR AFVQEELGCQ SVCKEACSFK EWTLTTSLAQ WPSVVSEKWL
 LPVLTWDQGR QVNKKLNKTD LAKLLIFYKD LNQRSIMESP ANSIEMLLSN FGGQLGLWMS
 CSVVCVIEII EVFFIDFFSI IARRQWQKAK EWWAWKQAPP CPEAPRSPQG QDNPALDIDD
 DLPTFNSALH LPPALGTQVP GTPPPKYNTL RLERAFSNQL TDTQMLDEL

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