ID   SL9A6_MOUSE             Reviewed;         702 AA.
AC   A1L3P4; Q8BTG0;
DT   22-FEB-2023, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Sodium/hydrogen exchanger 6;
DE   AltName: Full=Na(+)/H(+) exchanger 6;
DE            Short=NHE-6;
DE   AltName: Full=Sodium/hydrogen exchanger;
DE   AltName: Full=Solute carrier family 9 member 6;
GN   Name=Slc9a6; Synonyms=Nhe6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   SUBCELLULAR LOCATION, FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=17005858; DOI=10.1523/jneurosci.2990-06.2006;
RA   Hill J.K., Brett C.L., Chyou A., Kallay L.M., Sakaguchi M., Rao R.,
RA   Gillespie P.G.;
RT   "Vestibular hair bundles control pH with (Na+, K+)/H+ exchangers NHE6 and
RT   NHE9.";
RL   J. Neurosci. 26:9944-9955(2006).
RN   [7]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=21413028; DOI=10.1002/jcp.22501;
RA   Liu L., Schlesinger P.H., Slack N.M., Friedman P.A., Blair H.C.;
RT   "High capacity Na+/H+ exchange activity in mineralizing osteoblasts.";
RL   J. Cell. Physiol. 226:1702-1712(2011).
RN   [8]
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=23303939; DOI=10.1523/jneurosci.2583-12.2013;
RA   Deane E.C., Ilie A.E., Sizdahkhani S., Das Gupta M., Orlowski J.,
RA   McKinney R.A.;
RT   "Enhanced recruitment of endosomal Na+/H+ exchanger NHE6 into dendritic
RT   spines of hippocampal pyramidal neurons during NMDA receptor-dependent
RT   long-term potentiation.";
RL   J. Neurosci. 33:595-610(2013).
RN   [9]
RP   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=24035762; DOI=10.1016/j.neuron.2013.07.043;
RA   Ouyang Q., Lizarraga S.B., Schmidt M., Yang U., Gong J., Ellisor D.,
RA   Kauer J.A., Morrow E.M.;
RT   "Christianson syndrome protein NHE6 modulates TrkB endosomal signaling
RT   required for neuronal circuit development.";
RL   Neuron 80:97-112(2013).
RN   [10]
RP   MUTAGENESIS OF ALA-11.
RX   PubMed=31676550; DOI=10.1523/eneuro.0046-19.2019;
RA   Ouyang Q., Joesch-Cohen L., Mishra S., Riaz H.A., Schmidt M., Morrow E.M.;
RT   "Functional Assessment In Vivo of the Mouse Homolog of the Human Ala-9-Ser
RT   NHE6 Variant.";
RL   ENeuro 6:0-0(2019).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=34526390; DOI=10.1523/jneurosci.1244-20.2021;
RA   Pescosolido M.F., Ouyang Q., Liu J.S., Morrow E.M.;
RT   "Loss of Christianson Syndrome Na+/H+ Exchanger 6 (NHE6) Causes Abnormal
RT   Endosome Maturation and Trafficking Underlying Lysosome Dysfunction in
RT   Neurons.";
RL   J. Neurosci. 41:9235-9256(2021).
CC   -!- FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the
CC       electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+)
CC       or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity
CC       generated by vacuolar (V)-ATPase, thereby limiting luminal
CC       acidification. Responsible for alkalizing and maintaining the endosomal
CC       pH, and consequently in, e.g., endosome maturation and trafficking of
CC       recycling endosomal cargo (PubMed:17005858, PubMed:21413028,
CC       PubMed:24035762, PubMed:34526390). Plays a critical role during
CC       neurodevelopment by regulating synaptic development and plasticity
CC       (PubMed:21413028, PubMed:34526390). Implicated in the maintenance of
CC       cell polarity in a manner that is dependent on its ability to modulate
CC       intravesicular pH (By similarity). Regulates intracelular pH in some
CC       specialized cells, osteoclasts and stereocilia where this transporter
CC       localizes to the plasma membrane (PubMed:17005858, PubMed:21413028).
CC       {ECO:0000250|UniProtKB:Q92581, ECO:0000269|PubMed:17005858,
CC       ECO:0000269|PubMed:21413028, ECO:0000269|PubMed:24035762,
CC       ECO:0000269|PubMed:34526390}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out);
CC         Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000305|PubMed:21413028};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC         Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000269|PubMed:17005858};
CC   -!- SUBUNIT: Homodimer. Interacts with RACK1; regulates the distribution of
CC       SLC9A6 between endosomes and the plasma membrane.
CC       {ECO:0000250|UniProtKB:Q92581}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q92581};
CC       Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane
CC       {ECO:0000269|PubMed:23303939, ECO:0000269|PubMed:24035762}; Multi-pass
CC       membrane protein {ECO:0000255}. Early endosome membrane
CC       {ECO:0000269|PubMed:23303939, ECO:0000269|PubMed:24035762}; Multi-pass
CC       membrane protein {ECO:0000255}. Late endosome membrane
CC       {ECO:0000269|PubMed:24035762}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17005858}; Multi-pass
CC       membrane protein {ECO:0000255}. Note=Present predominantly in the
CC       recycling compartments including early and recycling endosomes, but
CC       undergoes plasma membrane localization during vesicular recycling,
CC       which is enhanced upon certain stimuli, such as hypoxia.
CC       {ECO:0000250|UniProtKB:Q92581}.
CC   -!- DEVELOPMENTAL STAGE: Developmentally regulated in area CA1 of the
CC       hippocamus, peaking at around postnatal day 50 and declining
CC       thereafter. {ECO:0000269|PubMed:23303939}.
CC   -!- PTM: Ubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q92581}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92581}.
CC   -!- DISRUPTION PHENOTYPE: The SLC9A6 null mice show a 10-20% increased
CC       mortality after birth, yet the surviving mice do not display any
CC       obvious difference. Behavioral tests reveal a modest motor
CC       hyperactivity associated with coordination deficits and limited ataxia.
CC       Neurons from these deficient mice exhibit endosomal hyperacidification,
CC       as well as impoverished neuronal arborization and attendant circuit
CC       dysfunction. {ECO:0000269|PubMed:24035762}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC       transporter (TC 2.A.36) family. {ECO:0000305}.
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DR   EMBL; AK032326; BAC27816.1; -; mRNA.
DR   EMBL; AC124584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL672085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC130221; AAI30222.1; -; mRNA.
DR   CCDS; CCDS40979.1; -.
DR   RefSeq; NP_766368.2; NM_172780.3.
DR   AlphaFoldDB; A1L3P4; -.
DR   SMR; A1L3P4; -.
DR   STRING; 10090.ENSMUSP00000076922; -.
DR   iPTMnet; A1L3P4; -.
DR   PhosphoSitePlus; A1L3P4; -.
DR   SwissPalm; A1L3P4; -.
DR   MaxQB; A1L3P4; -.
DR   PaxDb; 10090-ENSMUSP00000076922; -.
DR   PeptideAtlas; A1L3P4; -.
DR   PRIDE; A1L3P4; -.
DR   ProteomicsDB; 333294; -.
DR   Antibodypedia; 30408; 190 antibodies from 26 providers.
DR   DNASU; 236794; -.
DR   Ensembl; ENSMUST00000077741.12; ENSMUSP00000076922.6; ENSMUSG00000060681.16.
DR   GeneID; 236794; -.
DR   KEGG; mmu:236794; -.
DR   UCSC; uc009tgk.2; mouse.
DR   AGR; MGI:2443511; -.
DR   CTD; 10479; -.
DR   MGI; MGI:2443511; Slc9a6.
DR   VEuPathDB; HostDB:ENSMUSG00000060681; -.
DR   eggNOG; KOG1965; Eukaryota.
DR   GeneTree; ENSGT00940000153460; -.
DR   InParanoid; A1L3P4; -.
DR   OMA; LPNCCGP; -.
DR   OrthoDB; 1065060at2759; -.
DR   TreeFam; TF318755; -.
DR   Reactome; R-MMU-425986; Sodium/Proton exchangers.
DR   BioGRID-ORCS; 236794; 0 hits in 78 CRISPR screens.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; A1L3P4; Protein.
DR   Bgee; ENSMUSG00000060681; Expressed in superior cervical ganglion and 218 other cell types or tissues.
DR   ExpressionAtlas; A1L3P4; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; IDA:MGI.
DR   GO; GO:0044308; C:axonal spine; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005770; C:late endosome; IDA:MGI.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0015386; F:potassium:proton antiporter activity; IDA:UniProtKB.
DR   GO; GO:0015385; F:sodium:proton antiporter activity; IDA:UniProtKB.
DR   GO; GO:0048675; P:axon extension; ISO:MGI.
DR   GO; GO:0031547; P:brain-derived neurotrophic factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0097484; P:dendrite extension; ISO:MGI.
DR   GO; GO:0060996; P:dendritic spine development; IMP:MGI.
DR   GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:1902600; P:proton transmembrane transport; IMP:MGI.
DR   GO; GO:0051453; P:regulation of intracellular pH; IDA:UniProtKB.
DR   GO; GO:0051386; P:regulation of neurotrophin TRK receptor signaling pathway; IMP:MGI.
DR   GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR   GO; GO:0098719; P:sodium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   Gene3D; 6.10.140.1330; -; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR004709; NaH_exchanger.
DR   InterPro; IPR002090; NHE-6/7/9.
DR   NCBIfam; TIGR00840; b_cpa1; 1.
DR   PANTHER; PTHR10110; SODIUM/HYDROGEN EXCHANGER; 1.
DR   PANTHER; PTHR10110:SF94; SODIUM_HYDROGEN EXCHANGER 6; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   PRINTS; PR01084; NAHEXCHNGR.
DR   PRINTS; PR01088; NAHEXCHNGR6.
PE   1: Evidence at protein level;
KW   Cell membrane; Endosome; Ion transport; Membrane; Reference proteome;
KW   Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..702
FT                   /note="Sodium/hydrogen exchanger 6"
FT                   /id="PRO_0000457379"
FT   TRANSMEM        72..92
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..345
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        437..457
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        480..500
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        516..536
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         11
FT                   /note="A->S: Mice have normal brain size at 6 months of age
FT                   and do not show cerebellar degeneration or defective
FT                   neuronal arborization. Neurons from male mice also do not
FT                   demonstrate an abnormality in intraendosomal pH compared
FT                   with controls."
FT                   /evidence="ECO:0000269|PubMed:31676550"
FT   CONFLICT        695
FT                   /note="D -> G (in Ref. 1; BAC27816)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   702 AA;  77953 MW;  243F0126533B5547 CRC64;
     MAGARRGWRL APVRRGVCGP RARPLMRPLW LLFAVSFFGW TGALDGSGGT TRAMDEEIVS
     EKQAEESHRQ DSANLLIFIL LLTLTILTIW LFKHRRARFL HETGLAMIYG LLVGLVLRYG
     IHVPSDVNNV TLSCEVQSSP TTLLVNVSGK FYEYTLKGEI SSHELNNVQD NEMLRKVTFD
     PEVFFNILLP PIIFYAGYSL KRRHFFRNLG SILAYAFLGT AISCFVIGSI MYGCVTLMKV
     TGQLAGDFYF TDCLLFGAIV SATDPVTVLA IFHELQVDVE LYALLFGESV LNDAVAIVLS
     SSIVAYQPAG DNSHTFDVTA MFKSIGIFLG IFSGSFAMGA ATGVVTALVT KFTKLREFQL
     LETGLFFLMS WSTFLLAEAW GFTGVVAVLF CGITQAHYTY NNLSTESQHR TKQLFELLNF
     LAENFIFSYM GLTLFTFQNH VFNPTFVVGA FIAIFLGRAA NIYPLSLLLN LGRRSKIGSN
     FQHMMMFAGL RGAMAFALAI RDTATYARQM MFSTTLLIVF FTVWVFGGGT TAMLSCLHIR
     VGVDSDQEHL GVPDNERRTT KAESAWLFRM WYNFDHNYLK PLLTHSGPPL TTTLPACCGP
     IARCLTSPQA YENQEQLKDD DSDLILNDGD ISLTYGDSTV NTESATASAP RRFMGNSSED
     ALDRELTFGD HELVIRGTRL VLPMDDSEPA LNSLDDTRHS PA
//