ID   NPT2C_HUMAN             Reviewed;         599 AA.
AC   Q8N130; A2BFA1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Sodium-dependent phosphate transport protein 2C;
DE            Short=Sodium-phosphate transport protein 2C;
DE   AltName: Full=Na(+)-dependent phosphate cotransporter 2C;
DE   AltName: Full=Sodium/inorganic phosphate cotransporter IIC;
DE   AltName: Full=Sodium/phosphate cotransporter 2C;
DE            Short=Na(+)/Pi cotransporter 2C;
DE            Short=NaPi-2c;
DE   AltName: Full=Solute carrier family 34 member 3;
GN   Name=SLC34A3; Synonyms=NPT2C, NPTIIC;
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], FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND VARIANT VAL-513.
RC   TISSUE=Kidney;
RX   PubMed=11880379; DOI=10.1074/jbc.m200943200;
RA   Segawa H., Kaneko I., Takahashi A., Kuwahata M., Ito M., Ohkido I.,
RA   Tatsumi S., Miyamoto K.;
RT   "Growth-related renal type II Na/Pi cotransporter.";
RL   J. Biol. Chem. 277:19665-19672(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-513.
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=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   VARIANTS HHRH PHE-138; LEU-192; ARG-196 AND TRP-468, AND VARIANT VAL-513.
RX   PubMed=16358214; DOI=10.1086/499409;
RA   Bergwitz C., Roslin N.M., Tieder M., Loredo-Osti J.C., Bastepe M.,
RA   Abu-Zahra H., Frappier D., Burkett K., Carpenter T.O., Anderson D.,
RA   Garabedian M., Sermet I., Fujiwara T.M., Morgan K., Tenenhouse H.S.,
RA   Jueppner H.;
RT   "SLC34A3 mutations in patients with hereditary hypophosphatemic rickets
RT   with hypercalciuria predict a key role for the sodium-phosphate
RT   cotransporter NaPi-IIc in maintaining phosphate homeostasis.";
RL   Am. J. Hum. Genet. 78:179-192(2006).
RN   [5]
RP   VARIANTS HHRH LEU-192; LEU-353 AND GLU-413, AND VARIANTS HIS-67; ALA-180;
RP   ASN-237; SER-337 AND VAL-513.
RX   PubMed=16358215; DOI=10.1086/499410;
RA   Lorenz-Depiereux B., Benet-Pages A., Eckstein G., Tenenbaum-Rakover Y.,
RA   Wagenstaller J., Tiosano D., Gershoni-Baruch R., Albers N., Lichtner P.,
RA   Schnabel D., Hochberg Z., Strom T.M.;
RT   "Hereditary hypophosphatemic rickets with hypercalciuria is caused by
RT   mutations in the sodium-phosphate cotransporter gene SLC34A3.";
RL   Am. J. Hum. Genet. 78:193-201(2006).
CC   -!- FUNCTION: Involved in actively transporting phosphate into cells via
CC       Na(+) cotransport in the renal brush border membrane (PubMed:11880379).
CC       The cotransport has a Na(+):Pi stoichiometry of 2:1 and is
CC       electroneutral (By similarity). {ECO:0000250|UniProtKB:Q80SU6,
CC       ECO:0000269|PubMed:11880379}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Na(+)(out) + phosphate(out) = 2 Na(+)(in) + phosphate(in);
CC         Xref=Rhea:RHEA:71259, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000269|PubMed:11880379};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71260;
CC         Evidence={ECO:0000305|PubMed:11880379};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=79 uM for phosphate {ECO:0000269|PubMed:11880379};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:11880379};
CC   -!- INTERACTION:
CC       Q8N130; P58418: CLRN1; NbExp=3; IntAct=EBI-17769653, EBI-17274839;
CC       Q8N130; Q8TED1: GPX8; NbExp=3; IntAct=EBI-17769653, EBI-11721746;
CC       Q8N130; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-17769653, EBI-17684533;
CC       Q8N130; Q8WY98: TMEM234; NbExp=3; IntAct=EBI-17769653, EBI-8642211;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q8K4R8}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=ocalized at the brush border membrane in the
CC       kidney. {ECO:0000250|UniProtKB:Q8K4R8}.
CC   -!- TISSUE SPECIFICITY: Expressed only in the kidney.
CC       {ECO:0000269|PubMed:11880379}.
CC   -!- DISEASE: Hereditary hypophosphatemic rickets with hypercalciuria (HHRH)
CC       [MIM:241530]: Autosomal recessive form of hypophosphatemia
CC       characterized by reduced renal phosphate reabsorption and rickets.
CC       Increased serum levels of 1,25-dihydroxyvitamin D lead to increase in
CC       urinary calcium excretion. {ECO:0000269|PubMed:16358214,
CC       ECO:0000269|PubMed:16358215}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR   EMBL; AB055000; BAB83242.1; -; mRNA.
DR   EMBL; AK095999; BAC04667.1; -; mRNA.
DR   EMBL; BX255925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS7038.1; -.
DR   RefSeq; NP_001170787.1; NM_001177316.1.
DR   RefSeq; NP_001170788.1; NM_001177317.1.
DR   RefSeq; NP_543153.1; NM_080877.2.
DR   RefSeq; XP_016869781.1; XM_017014292.1.
DR   AlphaFoldDB; Q8N130; -.
DR   SMR; Q8N130; -.
DR   BioGRID; 126771; 7.
DR   IntAct; Q8N130; 5.
DR   STRING; 9606.ENSP00000442397; -.
DR   BindingDB; Q8N130; -.
DR   ChEMBL; CHEMBL4295900; -.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   DrugBank; DB14502; Sodium phosphate, dibasic.
DR   DrugBank; DB09449; Sodium phosphate, monobasic.
DR   DrugBank; DB14503; Sodium phosphate, monobasic, unspecified form.
DR   TCDB; 2.A.58.1.3; the phosphate:na(+) symporter (pnas) family.
DR   GlyCosmos; Q8N130; 4 sites, No reported glycans.
DR   GlyGen; Q8N130; 4 sites.
DR   iPTMnet; Q8N130; -.
DR   PhosphoSitePlus; Q8N130; -.
DR   BioMuta; SLC34A3; -.
DR   DMDM; 313104149; -.
DR   EPD; Q8N130; -.
DR   MassIVE; Q8N130; -.
DR   PaxDb; 9606-ENSP00000442397; -.
DR   PeptideAtlas; Q8N130; -.
DR   ProteomicsDB; 71531; -.
DR   Antibodypedia; 18978; 159 antibodies from 21 providers.
DR   DNASU; 142680; -.
DR   Ensembl; ENST00000361134.2; ENSP00000355353.2; ENSG00000198569.10.
DR   Ensembl; ENST00000538474.5; ENSP00000442397.1; ENSG00000198569.10.
DR   Ensembl; ENST00000673835.1; ENSP00000501114.1; ENSG00000198569.10.
DR   GeneID; 142680; -.
DR   KEGG; hsa:142680; -.
DR   MANE-Select; ENST00000673835.1; ENSP00000501114.1; NM_001177316.2; NP_001170787.2.
DR   UCSC; uc004cmf.1; human.
DR   AGR; HGNC:20305; -.
DR   CTD; 142680; -.
DR   DisGeNET; 142680; -.
DR   GeneCards; SLC34A3; -.
DR   HGNC; HGNC:20305; SLC34A3.
DR   HPA; ENSG00000198569; Group enriched (intestine, kidney).
DR   MalaCards; SLC34A3; -.
DR   MIM; 241530; phenotype.
DR   MIM; 609826; gene.
DR   neXtProt; NX_Q8N130; -.
DR   OpenTargets; ENSG00000198569; -.
DR   Orphanet; 157215; Hereditary hypophosphatemic rickets with hypercalciuria.
DR   PharmGKB; PA134930298; -.
DR   VEuPathDB; HostDB:ENSG00000198569; -.
DR   eggNOG; ENOG502QTG0; Eukaryota.
DR   GeneTree; ENSGT00950000183177; -.
DR   HOGENOM; CLU_025063_0_0_1; -.
DR   InParanoid; Q8N130; -.
DR   OMA; VHSIFNW; -.
DR   OrthoDB; 5404387at2759; -.
DR   PhylomeDB; Q8N130; -.
DR   TreeFam; TF313981; -.
DR   PathwayCommons; Q8N130; -.
DR   Reactome; R-HSA-427589; Type II Na+/Pi cotransporters.
DR   Reactome; R-HSA-5619097; Defective SLC34A3 causes Hereditary hypophosphatemic rickets with hypercalciuria (HHRH).
DR   SABIO-RK; Q8N130; -.
DR   SignaLink; Q8N130; -.
DR   SIGNOR; Q8N130; -.
DR   BioGRID-ORCS; 142680; 30 hits in 1145 CRISPR screens.
DR   GeneWiki; SLC34A3; -.
DR   GenomeRNAi; 142680; -.
DR   Pharos; Q8N130; Tbio.
DR   PRO; PR:Q8N130; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q8N130; Protein.
DR   Bgee; ENSG00000198569; Expressed in lower esophagus mucosa and 90 other cell types or tissues.
DR   ExpressionAtlas; Q8N130; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:HGNC-UCL.
DR   GO; GO:0005903; C:brush border; IBA:GO_Central.
DR   GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR   GO; GO:0030643; P:intracellular phosphate ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0006817; P:phosphate ion transport; IDA:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
DR   GO; GO:0044341; P:sodium-dependent phosphate transport; IBA:GO_Central.
DR   InterPro; IPR003841; Na/Pi_transpt.
DR   NCBIfam; TIGR01013; 2a58; 1.
DR   NCBIfam; NF037997; Na_Pi_symport; 1.
DR   PANTHER; PTHR10010:SF35; SODIUM-DEPENDENT PHOSPHATE TRANSPORT PROTEIN 2C; 1.
DR   PANTHER; PTHR10010; SOLUTE CARRIER FAMILY 34 SODIUM PHOSPHATE , MEMBER 2-RELATED; 1.
DR   Pfam; PF02690; Na_Pi_cotrans; 2.
DR   Genevisible; Q8N130; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Disease variant; Disulfide bond; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..599
FT                   /note="Sodium-dependent phosphate transport protein 2C"
FT                   /id="PRO_0000068617"
FT   TOPO_DOM        1..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical; Name=M3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..322
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical; Name=M4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        344..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical; Name=M5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..445
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..466
FT                   /note="Helical; Name=M6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        467..485
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..506
FT                   /note="Helical; Name=M7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..510
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        511..531
FT                   /note="Helical; Name=M8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        532..599
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K4R8"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        276..309
FT                   /evidence="ECO:0000250|UniProtKB:Q06496"
FT   VARIANT         67
FT                   /note="R -> H (in dbSNP:rs34372115)"
FT                   /evidence="ECO:0000269|PubMed:16358215"
FT                   /id="VAR_025706"
FT   VARIANT         138
FT                   /note="S -> F (in HHRH; dbSNP:rs141734934)"
FT                   /evidence="ECO:0000269|PubMed:16358214"
FT                   /id="VAR_025707"
FT   VARIANT         180
FT                   /note="G -> A (in dbSNP:rs35643193)"
FT                   /evidence="ECO:0000269|PubMed:16358215"
FT                   /id="VAR_025708"
FT   VARIANT         192
FT                   /note="S -> L (in HHRH; dbSNP:rs199690076)"
FT                   /evidence="ECO:0000269|PubMed:16358214,
FT                   ECO:0000269|PubMed:16358215"
FT                   /id="VAR_025709"
FT   VARIANT         196
FT                   /note="G -> R (in HHRH; dbSNP:rs121918237)"
FT                   /evidence="ECO:0000269|PubMed:16358214"
FT                   /id="VAR_025710"
FT   VARIANT         237
FT                   /note="D -> N (in dbSNP:rs145877051)"
FT                   /evidence="ECO:0000269|PubMed:16358215"
FT                   /id="VAR_025711"
FT   VARIANT         337
FT                   /note="G -> S (in dbSNP:rs35699762)"
FT                   /evidence="ECO:0000269|PubMed:16358215"
FT                   /id="VAR_025712"
FT   VARIANT         353
FT                   /note="R -> L (in HHRH; dbSNP:rs121918234)"
FT                   /evidence="ECO:0000269|PubMed:16358215"
FT                   /id="VAR_025713"
FT   VARIANT         413
FT                   /note="A -> E (in HHRH; dbSNP:rs121918235)"
FT                   /evidence="ECO:0000269|PubMed:16358215"
FT                   /id="VAR_025714"
FT   VARIANT         468
FT                   /note="R -> W (in HHRH; dbSNP:rs121918238)"
FT                   /evidence="ECO:0000269|PubMed:16358214"
FT                   /id="VAR_025715"
FT   VARIANT         513
FT                   /note="E -> V (in dbSNP:rs28542318)"
FT                   /evidence="ECO:0000269|PubMed:11880379,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:16358214,
FT                   ECO:0000269|PubMed:16358215"
FT                   /id="VAR_025716"
SQ   SEQUENCE   599 AA;  63550 MW;  3747DE33D0A53E95 CRC64;
     MPSSLPGSQV PHPTLDAVDL VEKTLRNEGT SSSAPVLEEG DTDPWTLPQL KDTSQPWKEL
     RVAGRLRRVA GSVLKACGLL GSLYFFICSL DVLSSAFQLL GSKVAGDIFK DNVVLSNPVA
     GLVIGVLVTA LVQSSSTSSS IVVSMVAAKL LTVRVSVPII MGVNVGTSIT STLVSMAQSG
     DRDEFQRAFS GSAVHGIFNW LTVLVLLPLE SATALLERLS ELALGAASLT PRAQAPDILK
     VLTKPLTHLI VQLDSDMIMS SATGNATNSS LIKHWCGTTG QPTQENSSCG AFGPCTEKNS
     TAPADRLPCR HLFAGTELTD LAVGCILLAG SLLVLCGCLV LIVKLLNSVL RGRVAQVVRT
     VINADFPFPL GWLGGYLAVL AGAGLTFALQ SSSVFTAAVV PLMGVGVISL DRAYPLLLGS
     NIGTTTTALL AALASPADRM LSALQVALIH FFFNLAGILL WYLVPALRLP IPLARHFGVV
     TARYRWVAGV YLLLGFLLLP LAAFGLSLAG GMELAAVGGP LVGLVLLVIL VTVLQRRRPA
     WLPVRLRSWA WLPVWLHSLE PWDRLVTRCC PCNVCSPPKA TTKEAYCYEN PEILASQQL
//