NPT2C_HUMAN
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 03-AUG-2022, entry version 147.
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 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 GlyGen; Q8N130; 4 sites.
DR iPTMnet; Q8N130; -.
DR PhosphoSitePlus; Q8N130; -.
DR BioMuta; SLC34A3; -.
DR DMDM; 313104149; -.
DR EPD; Q8N130; -.
DR MassIVE; Q8N130; -.
DR PaxDb; Q8N130; -.
DR PeptideAtlas; Q8N130; -.
DR PRIDE; Q8N130; -.
DR ProteomicsDB; 71531; -.
DR Antibodypedia; 18978; 128 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 CTD; 142680; -.
DR DisGeNET; 142680; -.
DR GeneCards; SLC34A3; -.
DR HGNC; HGNC:20305; SLC34A3.
DR HPA; ENSG00000198569; Tissue enhanced (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; HDAIPVM; -.
DR OrthoDB; 976094at2759; -.
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 BioGRID-ORCS; 142680; 14 hits in 1069 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 tissues.
DR ExpressionAtlas; Q8N130; baseline and differential.
DR Genevisible; Q8N130; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:cellular 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 InterPro; IPR029850; Na/Pi_transpt_2C.
DR PANTHER; PTHR10010; PTHR10010; 1.
DR PANTHER; PTHR10010:SF35; PTHR10010:SF35; 1.
DR Pfam; PF02690; Na_Pi_cotrans; 2.
DR TIGRFAMs; TIGR01013; 2a58; 1.
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
