VGLU3_HUMAN
ID VGLU3_HUMAN Reviewed; 589 AA.
AC Q8NDX2; B3KXZ6; B7ZKV4; Q17RQ8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Vesicular glutamate transporter 3 {ECO:0000303|PubMed:12151341};
DE Short=VGluT3 {ECO:0000303|PubMed:12151341};
DE AltName: Full=Solute carrier family 17 member 8;
GN Name=SLC17A8 {ECO:0000312|HGNC:HGNC:20151}; Synonyms=VGLUT3;
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), FUNCTION, TRANSPORTER ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12151341; DOI=10.1093/embo-reports/kvf159;
RA Takamori S., Malherbe P., Broger C., Jahn R.;
RT "Molecular cloning and functional characterization of human vesicular
RT glutamate transporter 3.";
RL EMBO Rep. 3:798-803(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart, and Lung;
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 [5]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=33440152; DOI=10.1016/j.celrep.2020.108623;
RA Cheret C., Ganzella M., Preobraschenski J., Jahn R., Ahnert-Hilger G.;
RT "Vesicular Glutamate Transporters (SLCA17 A6, 7, 8) Control Synaptic
RT Phosphate Levels.";
RL Cell Rep. 34:108623-108623(2021).
RN [6]
RP VARIANT DFNA25 VAL-211.
RX PubMed=18674745; DOI=10.1016/j.ajhg.2008.07.008;
RA Ruel J., Emery S., Nouvian R., Bersot T., Amilhon B., Van Rybroek J.M.,
RA Rebillard G., Lenoir M., Eybalin M., Delprat B., Sivakumaran T.A.,
RA Giros B., El Mestikawy S., Moser T., Smith R.J.H., Lesperance M.M.,
RA Puel J.-L.;
RT "Impairment of SLC17A8 encoding vesicular glutamate transporter-3, VGLUT3,
RT underlies nonsyndromic deafness DFNA25 and inner hair cell dysfunction in
RT null mice.";
RL Am. J. Hum. Genet. 83:278-292(2008).
CC -!- FUNCTION: Multifunctional transporter that transports L-glutamate as
CC well as multiple ions such as chloride, sodium and phosphate
CC (PubMed:33440152, PubMed:12151341). At the synaptic vesicle membrane,
CC mainly functions as an uniporter that mediates the uptake of L-
CC glutamate into synaptic vesicles at presynaptic nerve terminals of
CC excitatory neural cells (PubMed:12151341). The L-glutamate uniporter
CC activity is electrogenic and is driven by the proton electrochemical
CC gradient, mainly by the electrical gradient established by the vacuolar
CC H(+)-ATPase across the synaptic vesicle membrane (PubMed:12151341). In
CC addition, functions as a chloride channel that allows a chloride
CC permeation through the synaptic vesicle membrane that affects the
CC proton electrochemical gradient and promotes synaptic vesicles
CC acidification (By similarity). At the plasma membrane, following
CC exocytosis, functions as a symporter of Na(+) and phosphate from the
CC extracellular space to the cytoplasm allowing synaptic phosphate
CC homeostasis regulation (Probable). The symporter activity is
CC electrogenic (PubMed:33440152). Moreover, operates synergistically with
CC SLC18A3/VACHT under a constant H(+) gradient, thereby allowing striatal
CC vesicular acetylcholine uptake (By similarity).
CC {ECO:0000250|UniProtKB:Q7TSF2, ECO:0000269|PubMed:12151341,
CC ECO:0000305|PubMed:33440152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:12151341};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000305|PubMed:33440152};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q7TSF2};
CC -!- ACTIVITY REGULATION: The L-glutamate uniporter activity exhibits a
CC biphasic dependence on chloride concentration. Chloride channel
CC activity is allosterically activated by lumenal H(+) and Cl(-) leading
CC to synaptic vesicles acidification. The glutamate transport activity is
CC allosterically activated by lumenal H(+) and Cl(-), preventing non-
CC vesicular L-glutamate release. {ECO:0000250|UniProtKB:Q7TSF2}.
CC -!- INTERACTION:
CC Q8NDX2-2; P78329: CYP4F2; NbExp=3; IntAct=EBI-17249797, EBI-1752413;
CC Q8NDX2-2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-17249797, EBI-10171534;
CC Q8NDX2-2; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-17249797, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q7TSF2}. Cell membrane
CC {ECO:0000305|PubMed:33440152}; Multi-pass membrane protein
CC {ECO:0000305}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q7TSF2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NDX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDX2-2; Sequence=VSP_033265;
CC -!- TISSUE SPECIFICITY: Expressed in amygdala, cerebellum, hippocampus,
CC medulla, spinal cord and thalamus. {ECO:0000269|PubMed:12151341}.
CC -!- DISEASE: Deafness, autosomal dominant, 25 (DFNA25) [MIM:605583]: A form
CC of non-syndromic sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. DFNA25 expression is variable in terms of onset and rate
CC of progression, with an age-dependent penetrance resembling an early-
CC onset presbycusis, or senile deafness, a progressive bilateral loss of
CC hearing that occurs in the aged. {ECO:0000269|PubMed:18674745}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. VGLUT subfamily. {ECO:0000305}.
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DR EMBL; AJ459241; CAD30553.1; -; mRNA.
DR EMBL; AK128319; BAG54658.1; -; mRNA.
DR EMBL; CH471054; EAW97637.1; -; Genomic_DNA.
DR EMBL; BC117229; AAI17230.1; -; mRNA.
DR EMBL; BC143396; AAI43397.1; -; mRNA.
DR CCDS; CCDS44957.1; -. [Q8NDX2-2]
DR CCDS; CCDS9077.1; -. [Q8NDX2-1]
DR RefSeq; NP_001138760.1; NM_001145288.1. [Q8NDX2-2]
DR RefSeq; NP_647480.1; NM_139319.2. [Q8NDX2-1]
DR AlphaFoldDB; Q8NDX2; -.
DR SMR; Q8NDX2; -.
DR BioGRID; 128880; 11.
DR IntAct; Q8NDX2; 4.
DR STRING; 9606.ENSP00000316909; -.
DR TCDB; 2.A.1.14.32; the major facilitator superfamily (mfs).
DR GlyGen; Q8NDX2; 1 site.
DR BioMuta; SLC17A8; -.
DR DMDM; 74723817; -.
DR EPD; Q8NDX2; -.
DR MassIVE; Q8NDX2; -.
DR PaxDb; Q8NDX2; -.
DR PeptideAtlas; Q8NDX2; -.
DR PRIDE; Q8NDX2; -.
DR Antibodypedia; 57947; 85 antibodies from 13 providers.
DR DNASU; 246213; -.
DR Ensembl; ENST00000323346.10; ENSP00000316909.4; ENSG00000179520.11. [Q8NDX2-1]
DR Ensembl; ENST00000392989.3; ENSP00000376715.3; ENSG00000179520.11. [Q8NDX2-2]
DR GeneID; 246213; -.
DR KEGG; hsa:246213; -.
DR MANE-Select; ENST00000323346.10; ENSP00000316909.4; NM_139319.3; NP_647480.1.
DR UCSC; uc009ztx.4; human. [Q8NDX2-1]
DR CTD; 246213; -.
DR DisGeNET; 246213; -.
DR GeneCards; SLC17A8; -.
DR GeneReviews; SLC17A8; -.
DR HGNC; HGNC:20151; SLC17A8.
DR HPA; ENSG00000179520; Group enriched (brain, intestine).
DR MalaCards; SLC17A8; -.
DR MIM; 605583; phenotype.
DR MIM; 607557; gene.
DR neXtProt; NX_Q8NDX2; -.
DR OpenTargets; ENSG00000179520; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA223010; -.
DR VEuPathDB; HostDB:ENSG00000179520; -.
DR eggNOG; KOG2532; Eukaryota.
DR GeneTree; ENSGT00940000158187; -.
DR HOGENOM; CLU_001265_5_0_1; -.
DR InParanoid; Q8NDX2; -.
DR OMA; RRTTWGM; -.
DR OrthoDB; 497052at2759; -.
DR PhylomeDB; Q8NDX2; -.
DR TreeFam; TF313535; -.
DR PathwayCommons; Q8NDX2; -.
DR Reactome; R-HSA-428643; Organic anion transporters.
DR Reactome; R-HSA-5619076; Defective SLC17A8 causes autosomal dominant deafness 25 (DFNA25).
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR SignaLink; Q8NDX2; -.
DR BioGRID-ORCS; 246213; 7 hits in 1070 CRISPR screens.
DR ChiTaRS; SLC17A8; human.
DR GeneWiki; SLC17A8; -.
DR GenomeRNAi; 246213; -.
DR Pharos; Q8NDX2; Tbio.
DR PRO; PR:Q8NDX2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NDX2; protein.
DR Bgee; ENSG00000179520; Expressed in small intestine Peyer's patch and 62 other tissues.
DR Genevisible; Q8NDX2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0097441; C:basal dendrite; IEA:Ensembl.
DR GO; GO:0060076; C:excitatory synapse; IBA:GO_Central.
DR GO; GO:0097451; C:glial limiting end-foot; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:1990030; C:pericellular basket; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0030672; C:synaptic vesicle membrane; TAS:Reactome.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0051938; P:L-glutamate import; ISS:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0003407; P:neural retina development; IEA:Ensembl.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IDA:SynGO.
DR GO; GO:0055062; P:phosphate ion homeostasis; IDA:UniProtKB.
DR GO; GO:0051951; P:positive regulation of glutamate uptake involved in transmission of nerve impulse; ISS:UniProtKB.
DR GO; GO:0051631; P:regulation of acetylcholine uptake; ISS:UniProtKB.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IC:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Chloride; Chloride channel;
KW Cytoplasmic vesicle; Deafness; Disease variant; Glycoprotein; Hearing;
KW Ion channel; Ion transport; Membrane; Neurotransmitter transport;
KW Non-syndromic deafness; Phosphate transport; Reference proteome; Sodium;
KW Sodium transport; Symport; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..589
FT /note="Vesicular glutamate transporter 3"
FT /id="PRO_0000331614"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..130
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..182
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..249
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..353
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..413
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..481
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 302..351
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033265"
FT VARIANT 8
FT /note="T -> I (in dbSNP:rs45610843)"
FT /id="VAR_042905"
FT VARIANT 211
FT /note="A -> V (in DFNA25; dbSNP:rs121918339)"
FT /evidence="ECO:0000269|PubMed:18674745"
FT /id="VAR_054130"
FT VARIANT 220
FT /note="A -> T (in dbSNP:rs11568530)"
FT /id="VAR_054131"
FT VARIANT 246
FT /note="G -> E (in dbSNP:rs11568543)"
FT /id="VAR_054132"
SQ SEQUENCE 589 AA; 64991 MW; E74DDC91495F8775 CRC64;
MPFKAFDTFK EKILKPGKEG VKNAVGDSLG ILQRKIDGTT EEEDNIELNE EGRPVQTSRP
SPPLCDCHCC GLPKRYIIAI MSGLGFCISF GIRCNLGVAI VEMVNNSTVY VDGKPEIQTA
QFNWDPETVG LIHGSFFWGY IMTQIPGGFI SNKFAANRVF GAAIFLTSTL NMFIPSAARV
HYGCVMCVRI LQGLVEGVTY PACHGMWSKW APPLERSRLA TTSFCGSYAG AVVAMPLAGV
LVQYIGWSSV FYIYGMFGII WYMFWLLQAY ECPAAHPTIS NEEKTYIETS IGEGANVVSL
SKFSTPWKRF FTSLPVYAII VANFCRSWTF YLLLISQPAY FEEVFGFAIS KVGLLSAVPH
MVMTIVVPIG GQLADYLRSR QILTTTAVRK IMNCGGFGME ATLLLVVGFS HTKGVAISFL
VLAVGFSGFA ISGFNVNHLD IAPRYASILM GISNGVGTLS GMVCPLIVGA MTRHKTREEW
QNVFLIAALV HYSGVIFYGV FASGEKQEWA DPENLSEEKC GIIDQDELAE EIELNHESFA
SPKKKMSYGA TSQNCEVQKK EWKGQRGATL DEEELTSYQN EERNFSTIS
