SCNND_HUMAN
ID SCNND_HUMAN Reviewed; 802 AA.
AC P51172; A6NNF7; A9Z1X6; B1PS44; B3KSD7; Q08AQ3; Q09HT0; Q5T7L3; Q8NA24;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Amiloride-sensitive sodium channel subunit delta;
DE AltName: Full=Delta-NaCH;
DE AltName: Full=Epithelial Na(+) channel subunit delta;
DE Short=Delta-ENaC;
DE Short=ENaCD;
DE AltName: Full=Nonvoltage-gated sodium channel 1 subunit delta;
DE AltName: Full=SCNED;
GN Name=SCNN1D; Synonyms=DNACH;
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), VARIANT TYR-696, FUNCTION, AND
RP SUBUNIT.
RX PubMed=7499195; DOI=10.1074/jbc.270.46.27411;
RA Waldmann R., Champigny G., Bassilana F., Voilley N., Lazdunski M.;
RT "Molecular cloning and functional expression of a novel amiloride-sensitive
RT Na+ channel.";
RL J. Biol. Chem. 270:27411-27414(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBUNIT.
RC TISSUE=Lung;
RX PubMed=16423824; DOI=10.1074/jbc.m512293200;
RA Ji H.L., Su X.F., Kedar S., Li J., Barbry P., Smith P.R., Matalon S.,
RA Benos D.J.;
RT "Delta-subunit confers novel biophysical features to alpha beta gamma-human
RT epithelial sodium channel (ENaC) via a physical interaction.";
RL J. Biol. Chem. 281:8233-8241(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TOPOLOGY.
RC TISSUE=Nasal epithelium;
RX PubMed=19520916; DOI=10.1165/rcmb.2009-0053oc;
RA Bangel-Ruland N., Sobczak K., Christmann T., Kentrup D., Langhorst H.,
RA Kusche-Vihrog K., Weber W.M.;
RT "Characterization of the epithelial sodium channel delta-subunit in human
RT nasal epithelium.";
RL Am. J. Respir. Cell Mol. Biol. 42:498-505(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP SER-726 AND ARG-770.
RC TISSUE=Hippocampus, and Testis;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-344
RP AND GLN-544.
RC TISSUE=Brain;
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 [7]
RP ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=22505667; DOI=10.1152/ajplung.00331.2011;
RA Zhao R.Z., Nie H.G., Su X.F., Han D.Y., Lee A., Huang Y., Chang Y.,
RA Matalon S., Ji H.L.;
RT "Characterization of a novel splice variant of delta ENaC subunit in human
RT lungs.";
RL Am. J. Physiol. 302:L1262-L1272(2012).
RN [8]
RP PHYLOGENETIC ANALYSIS, AND NOMENCLATURE.
RX PubMed=26772908; DOI=10.1016/j.gene.2015.12.061;
RA Hanukoglu I., Hanukoglu A.;
RT "Epithelial sodium channel (ENaC) family: Phylogeny, structure-function,
RT tissue distribution, and associated inherited diseases.";
RL Gene 579:95-132(2016).
CC -!- FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited
CC by the diuretic amiloride. Mediates the electrodiffusion of the luminal
CC sodium (and water, which follows osmotically) through the apical
CC membrane of epithelial cells. Controls the reabsorption of sodium in
CC kidney, colon, lung and sweat glands. Also plays a role in taste
CC perception. {ECO:0000269|PubMed:16423824, ECO:0000269|PubMed:7499195}.
CC -!- SUBUNIT: Heterotrimer containing a delta/SCNN1D, a beta/SCNN1B and a
CC gamma/SCNN1G subunit. The additional delta/SCNN1D subunit exists only
CC in some organisms and can replace the alpha/SCNN1A subunit to form an
CC alternative channel with specific properties.
CC {ECO:0000269|PubMed:16423824, ECO:0000269|PubMed:7499195}.
CC -!- INTERACTION:
CC P51172; Q8N668: COMMD1; NbExp=3; IntAct=EBI-2547114, EBI-1550112;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19520916};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19520916}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=P51172-3; Sequence=Displayed;
CC Name=1; Synonyms=delta1;
CC IsoId=P51172-1; Sequence=VSP_060000, VSP_060002;
CC Name=2; Synonyms=delta2;
CC IsoId=P51172-2; Sequence=VSP_060001;
CC -!- MISCELLANEOUS: [Isoform 2]: Channels including isoform 2 exhibit
CC greater conductance than those containing isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. SCNN1D subfamily. {ECO:0000305}.
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DR EMBL; U38254; AAC50283.1; -; mRNA.
DR EMBL; DQ898176; ABI64069.1; -; mRNA.
DR EMBL; EU489064; ACA51868.1; -; mRNA.
DR EMBL; AK093239; BAC04105.1; -; mRNA.
DR EMBL; AK127357; BAG54495.1; -; mRNA.
DR EMBL; AL162741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036752; AAH36752.1; -; mRNA.
DR EMBL; BC125074; AAI25075.1; -; mRNA.
DR CCDS; CCDS44037.2; -. [P51172-3]
DR PIR; I39196; I39196.
DR RefSeq; NP_001123885.2; NM_001130413.3. [P51172-3]
DR RefSeq; XP_011540227.1; XM_011541925.2.
DR RefSeq; XP_011540234.1; XM_011541932.2.
DR RefSeq; XP_011540235.1; XM_011541933.2.
DR AlphaFoldDB; P51172; -.
DR SMR; P51172; -.
DR BioGRID; 112243; 73.
DR ComplexPortal; CPX-312; Amiloride-sensitive sodium channel complex, delta-alpha-beta-gamma.
DR ComplexPortal; CPX-313; Amiloride-sensitive sodium channel complex, delta-beta-gamma.
DR CORUM; P51172; -.
DR IntAct; P51172; 21.
DR STRING; 9606.ENSP00000368411; -.
DR DrugBank; DB00594; Amiloride.
DR DrugBank; DB00384; Triamterene.
DR TCDB; 1.A.6.1.1; the epithelial na(+) channel (enac) family.
DR GlyGen; P51172; 2 sites.
DR iPTMnet; P51172; -.
DR PhosphoSitePlus; P51172; -.
DR BioMuta; SCNN1D; -.
DR DMDM; 116242784; -.
DR MassIVE; P51172; -.
DR PaxDb; P51172; -.
DR PeptideAtlas; P51172; -.
DR PRIDE; P51172; -.
DR ProteomicsDB; 1607; -.
DR ProteomicsDB; 56298; -. [P51172-1]
DR ProteomicsDB; 56299; -. [P51172-2]
DR Antibodypedia; 4029; 261 antibodies from 31 providers.
DR DNASU; 6339; -.
DR Ensembl; ENST00000325425.12; ENSP00000321594.8; ENSG00000162572.21. [P51172-2]
DR Ensembl; ENST00000338555.6; ENSP00000339504.2; ENSG00000162572.21. [P51172-1]
DR Ensembl; ENST00000379116.10; ENSP00000368411.5; ENSG00000162572.21. [P51172-3]
DR Ensembl; ENST00000400928.7; ENSP00000383717.3; ENSG00000162572.21. [P51172-1]
DR GeneID; 6339; -.
DR KEGG; hsa:6339; -.
DR MANE-Select; ENST00000379116.10; ENSP00000368411.5; NM_001130413.4; NP_001123885.2.
DR UCSC; uc001adw.3; human. [P51172-3]
DR CTD; 6339; -.
DR DisGeNET; 6339; -.
DR GeneCards; SCNN1D; -.
DR HGNC; HGNC:10601; SCNN1D.
DR HPA; ENSG00000162572; Tissue enhanced (testis).
DR MIM; 601328; gene.
DR neXtProt; NX_P51172; -.
DR OpenTargets; ENSG00000162572; -.
DR PharmGKB; PA35011; -.
DR VEuPathDB; HostDB:ENSG00000162572; -.
DR eggNOG; KOG4294; Eukaryota.
DR GeneTree; ENSGT00940000162685; -.
DR InParanoid; P51172; -.
DR OMA; DCFYRSY; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; P51172; -.
DR TreeFam; TF330663; -.
DR PathwayCommons; P51172; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-9730628; Sensory perception of salty taste.
DR SignaLink; P51172; -.
DR BioGRID-ORCS; 6339; 16 hits in 1072 CRISPR screens.
DR GeneWiki; SCNN1D; -.
DR GenomeRNAi; 6339; -.
DR Pharos; P51172; Tbio.
DR PRO; PR:P51172; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P51172; protein.
DR Bgee; ENSG00000162572; Expressed in right hemisphere of cerebellum and 89 other tissues.
DR ExpressionAtlas; P51172; baseline and differential.
DR Genevisible; P51172; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0034706; C:sodium channel complex; IDA:ComplexPortal.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:ComplexPortal.
DR GO; GO:1904045; P:cellular response to aldosterone; IC:ComplexPortal.
DR GO; GO:0036254; P:cellular response to amiloride; IDA:ComplexPortal.
DR GO; GO:1904117; P:cellular response to vasopressin; IC:ComplexPortal.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0008217; P:regulation of blood pressure; IC:ComplexPortal.
DR GO; GO:0050914; P:sensory perception of salty taste; IC:ComplexPortal.
DR GO; GO:0050915; P:sensory perception of sour taste; IC:ComplexPortal.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IDA:ComplexPortal.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; TAS:ProtInc.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR004724; ENaC_chordates.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
DR PROSITE; PS01206; ASC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Reference proteome; Sensory transduction; Sodium;
KW Sodium channel; Sodium transport; Taste; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..802
FT /note="Amiloride-sensitive sodium channel subunit delta"
FT /id="PRO_0000181282"
FT TOPO_DOM 1..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19520916"
FT TRANSMEM 251..271
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..694
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19520916"
FT TRANSMEM 695..715
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19520916"
FT REGION 145..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 1)"
FT /id="VSP_060000"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 2)"
FT /id="VSP_060001"
FT VAR_SEQ 165..185
FT /note="PCHLKGWQHRPTQHNAACKQG -> MAEHRSMDGRMEAATRGGSHL (in
FT isoform 1)"
FT /id="VSP_060002"
FT VARIANT 344
FT /note="R -> P (in dbSNP:rs11260579)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028209"
FT VARIANT 544
FT /note="E -> Q (in dbSNP:rs2228579)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028210"
FT VARIANT 636
FT /note="A -> T (in dbSNP:rs13306651)"
FT /id="VAR_028211"
FT VARIANT 696
FT /note="C -> Y (in dbSNP:rs1053844)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7499195"
FT /id="VAR_028212"
FT VARIANT 726
FT /note="G -> S (in dbSNP:rs6690013)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_028213"
FT VARIANT 770
FT /note="G -> R (in dbSNP:rs609805)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_028214"
FT CONFLICT 176
FT /note="T -> A (in Ref. 2; ABI64069)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="Q -> R (in Ref. 2; ABI64069)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="V -> A (in Ref. 2; ABI64069)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="H -> Y (in Ref. 4; BAC04105)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="F -> L (in Ref. 4; BAC04105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 802 AA; 87850 MW; 5CC845DA14F2E6B4 CRC64;
MRAVLSQKTT PLPRYLWPGH LSGPRRLTWS WCSDHRTPTC RELGSPHPTP CTGPARGWPR
RGGGPCGFTS AGHVLCGYPL CLLSGPIQGC GTGLGDSSMA FLSRTSPVAA ASFQSRQEAR
GSILLQSCQL PPQWLSTEAW TGEWKQPHGG ALTSRSPGPV APQRPCHLKG WQHRPTQHNA
ACKQGQAAAQ TPPRPGPPSA PPPPPKEGHQ EGLVELPASF RELLTFFCTN ATIHGAIRLV
CSRGNRLKTT SWGLLSLGAL VALCWQLGLL FERHWHRPVL MAVSVHSERK LLPLVTLCDG
NPRRPSPVLR HLELLDEFAR ENIDSLYNVN LSKGRAALSA TVPRHEPPFH LDREIRLQRL
SHSGSRVRVG FRLCNSTGGD CFYRGYTSGV AAVQDWYHFH YVDILALLPA AWEDSHGSQD
GHFVLSCSYD GLDCQARQFR TFHHPTYGSC YTVDGVWTAQ RPGITHGVGL VLRVEQQPHL
PLLSTLAGIR VMVHGRNHTP FLGHHSFSVR PGTEATISIR EDEVHRLGSP YGHCTAGGEG
VEVELLHNTS YTRQACLVSC FQQLMVETCS CGYYLHPLPA GAEYCSSARH PAWGHCFYRL
YQDLETHRLP CTSRCPRPCR ESAFKLSTGT SRWPSAKSAG WTLATLGEQG LPHQSHRQRS
SLAKINIVYQ ELNYRSVEEA PVYSVPQLLS AMGSLCSLWF GASVLSLLEL LELLLDASAL
TLVLGGRRLR RAWFSWPRAS PASGASSIKP EASQMPPPAG GTSDDPEPSG PHLPRVMLPG
VLAGVSAEES WAGPQPLETL DT
