NPT4_HUMAN
ID NPT4_HUMAN Reviewed; 420 AA.
AC O00476; B7WNJ5; B7Z511; Q8WWC7; Q9H533;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sodium-dependent phosphate transport protein 4;
DE AltName: Full=Na(+)/PI cotransporter 4;
DE AltName: Full=Sodium/phosphate cotransporter 4;
DE AltName: Full=Solute carrier family 17 member 3;
GN Name=SLC17A3; Synonyms=NPT4;
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), AND TISSUE SPECIFICITY.
RX PubMed=9149941; DOI=10.1101/gr.7.5.441;
RA Ruddy D.A., Kronmal G.S., Lee V.K., Mintier G.A., Quintana L.,
RA Domingo R. Jr., Meyer N.C., Irrinki A., McClelland E.E., Fullan A.,
RA Mapa F.A., Moore T., Thomas W., Loeb D.B., Harmon C., Tsuchihashi Z.,
RA Wolff R.K., Schatzman R.C., Feder J.N.;
RT "A 1.1-Mb transcript map of the hereditary hemochromatosis locus.";
RL Genome Res. 7:441-456(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-100.
RC TISSUE=Kidney;
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 [6]
RP SUBCELLULAR LOCATION, AND VARIANT ARG-201.
RX PubMed=15505377; DOI=10.1023/b:boli.0000045755.89308.2f;
RA Melis D., Havelaar A.C., Verbeek E., Smit G.P.A., Benedetti A.,
RA Mancini G.M.S., Verheijen F.;
RT "NPT4, a new microsomal phosphate transporter: mutation analysis in
RT glycogen storage disease type Ic.";
RL J. Inherit. Metab. Dis. 27:725-733(2004).
RN [7]
RP FUNCTION AS ORGANIC ANION TRANSPORTER (ISOFORM 2), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION (ISOFORM 2), POLYMORPHISM, INVOLVEMENT IN UAQTL4,
RP VARIANTS HIS-68 AND SER-226, AND CHARACTERIZATION OF VARIANTS HIS-68 AND
RP SER-226.
RX PubMed=20810651; DOI=10.1074/jbc.m110.121301;
RA Jutabha P., Anzai N., Kitamura K., Taniguchi A., Kaneko S., Yan K.,
RA Yamada H., Shimada H., Kimura T., Katada T., Fukutomi T., Tomita K.,
RA Urano W., Yamanaka H., Seki G., Fujita T., Moriyama Y., Yamada A.,
RA Uchida S., Wempe M.F., Endou H., Sakurai H.;
RT "Human sodium phosphate transporter 4 (hNPT4/SLC17A3) as a common renal
RT secretory pathway for drugs and urate.";
RL J. Biol. Chem. 285:35123-35132(2010).
CC -!- FUNCTION: [Isoform 2]: Voltage-driven, multispecific, organic anion
CC transporter able to transport para-aminohippurate (PAH), estrone
CC sulfate, estradiol-17-beta-glucuronide, bumetanide, and ochratoxin A.
CC Isoform 2 functions as urate efflux transporter on the apical side of
CC renal proximal tubule and is likely to act as an exit path for organic
CC anionic drugs as well as urate in vivo. May be involved in actively
CC transporting phosphate into cells via Na(+) cotransport.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15505377}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15505377}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:20810651}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20810651}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00476-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00476-2; Sequence=VSP_042888;
CC -!- TISSUE SPECIFICITY: Expressed in the liver and kidney. It is detected
CC in proximal tubules in renal cortex as well as some tubules and
CC glomeruli, with highest expression at the apical side of proximal
CC tubules (at protein level). {ECO:0000269|PubMed:20810651,
CC ECO:0000269|PubMed:9149941}.
CC -!- POLYMORPHISM: Genetic variations in SLC17A3 influence the variance in
CC serum uric acid concentrations and define the serum uric acid
CC concentration quantitative trait locus 4 (UAQTL4) [MIM:612671]. Excess
CC serum accumulation of uric acid can lead to the development of gout, a
CC common disorder characterized by tissue deposition of monosodium urate
CC crystals as a consequence of hyperuricemia.
CC {ECO:0000269|PubMed:20810651}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB53423.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U90545; AAB53423.1; ALT_INIT; mRNA.
DR EMBL; AK298271; BAH12747.1; -; mRNA.
DR EMBL; AL138726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55495.1; -; Genomic_DNA.
DR EMBL; BC017952; AAH17952.1; -; mRNA.
DR CCDS; CCDS4566.2; -. [O00476-1]
DR CCDS; CCDS47385.1; -. [O00476-2]
DR RefSeq; NP_001091956.1; NM_001098486.1. [O00476-2]
DR RefSeq; NP_006623.2; NM_006632.3. [O00476-1]
DR AlphaFoldDB; O00476; -.
DR SMR; O00476; -.
DR TCDB; 2.A.1.14.28; the major facilitator superfamily (mfs).
DR GlyGen; O00476; 4 sites.
DR iPTMnet; O00476; -.
DR PhosphoSitePlus; O00476; -.
DR BioMuta; SLC17A3; -.
DR MassIVE; O00476; -.
DR PaxDb; O00476; -.
DR PeptideAtlas; O00476; -.
DR PRIDE; O00476; -.
DR ProteomicsDB; 47921; -. [O00476-1]
DR ProteomicsDB; 47922; -. [O00476-2]
DR Antibodypedia; 10761; 74 antibodies from 15 providers.
DR DNASU; 10786; -.
DR Ensembl; ENST00000360657.7; ENSP00000353873.3; ENSG00000124564.17. [O00476-1]
DR Ensembl; ENST00000361703.10; ENSP00000355307.6; ENSG00000124564.17. [O00476-1]
DR Ensembl; ENST00000397060.8; ENSP00000380250.4; ENSG00000124564.17. [O00476-2]
DR GeneID; 10786; -.
DR KEGG; hsa:10786; -.
DR MANE-Select; ENST00000397060.8; ENSP00000380250.4; NM_001098486.2; NP_001091956.1. [O00476-2]
DR UCSC; uc003nfi.5; human. [O00476-1]
DR CTD; 10786; -.
DR DisGeNET; 10786; -.
DR GeneCards; SLC17A3; -.
DR HGNC; HGNC:10931; SLC17A3.
DR HPA; ENSG00000124564; Tissue enriched (kidney).
DR MalaCards; SLC17A3; -.
DR MIM; 611034; gene.
DR MIM; 612671; phenotype.
DR neXtProt; NX_O00476; -.
DR OpenTargets; ENSG00000124564; -.
DR PharmGKB; PA35822; -.
DR VEuPathDB; HostDB:ENSG00000124564; -.
DR eggNOG; KOG2532; Eukaryota.
DR GeneTree; ENSGT00940000162523; -.
DR HOGENOM; CLU_001265_5_0_1; -.
DR InParanoid; O00476; -.
DR OMA; CVAWGGW; -.
DR OrthoDB; 497052at2759; -.
DR PhylomeDB; O00476; -.
DR TreeFam; TF313535; -.
DR PathwayCommons; O00476; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 10786; 4 hits in 1063 CRISPR screens.
DR GenomeRNAi; 10786; -.
DR Pharos; O00476; Tbio.
DR PRO; PR:O00476; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O00476; protein.
DR Bgee; ENSG00000124564; Expressed in nephron tubule and 86 other tissues.
DR ExpressionAtlas; O00476; baseline and differential.
DR Genevisible; O00476; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015136; F:sialic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; ISS:UniProtKB.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015143; F:urate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:0015760; P:glucose-6-phosphate transport; TAS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0015711; P:organic anion transport; IDA:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; ISS:UniProtKB.
DR GO; GO:0015739; P:sialic acid transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; ISS:UniProtKB.
DR GO; GO:0046415; P:urate metabolic process; IMP:UniProtKB.
DR GO; GO:0015747; P:urate transport; IDA:UniProtKB.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR017373; Na-dep_P-transpt_4_prd.
DR Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF038072; Na(+)/PI_cotransporter4_prd; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW Ion transport; Membrane; Reference proteome; Sodium; Sodium transport;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..420
FT /note="Sodium-dependent phosphate transport protein 4"
FT /id="PRO_0000351138"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 101
FT /note="K -> KAPVYDWSPQIQGIIFGAVGYGGILTMAPSGYLAGRVGTKRVVGISL
FT FATSFLTLCIPLATDFGIVLLIVTRIVQGLSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042888"
FT VARIANT 68
FT /note="N -> H (found in a patient with gout; does not
FT affect isoform 2 localization at the cell membrane; results
FT in reduced urate efflux; dbSNP:rs387907257)"
FT /evidence="ECO:0000269|PubMed:20810651"
FT /id="VAR_068680"
FT VARIANT 100
FT /note="A -> T (in dbSNP:rs1165165)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024533"
FT VARIANT 201
FT /note="G -> R (in dbSNP:rs56027330)"
FT /evidence="ECO:0000269|PubMed:15505377"
FT /id="VAR_034700"
FT VARIANT 226
FT /note="F -> S (found in a patient with hyperuricemia;
FT decreased expression of isoform 2 at the cell membrane;
FT results in highly reduced urate efflux; dbSNP:rs387907256)"
FT /evidence="ECO:0000269|PubMed:20810651"
FT /id="VAR_068681"
FT VARIANT 300
FT /note="P -> L (in dbSNP:rs11966370)"
FT /id="VAR_046633"
FT CONFLICT 31
FT /note="V -> G (in Ref. 1; AAB53423)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="V -> F (in Ref. 1; AAB53423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46106 MW; BFDFCC7F4345F573 CRC64;
MATKTELSPT ARESKNAQDM QVDETLIPRK VPSLCSARYG IALVLHFCNF TTIAQNVIMN
ITMVAMVNST SPQSQLNDSS EVLPVDSFGG LSKAPKSLPA KSSILGGQFA IWEKWGPPQE
RSRLCSIALS GMLLGCFTAI LIGGFISETL GWPFVFYIFG GVGCVCCLLW FVVIYDDPVS
YPWISTSEKE YIISSLKQQV GSSKQPLPIK AMLRSLPIWS ICLGCFSHQW LVSTMVVYIP
TYISSVYHVN IRDNGLLSAL PFIVAWVIGM VGGYLADFLL TKKFRLITVR KIATILGSLP
SSALIVSLPY LNSGYITATA LLTLSCGLST LCQSGIYINV LDIAPRYSSF LMGASRGFSS
IAPVIVPTVS GFLLSQDPEF GWRNVFFLLF AVNLLGLLFY LIFGEADVQE WAKERKLTRL
