ID S26A3_HUMAN Reviewed; 764 AA. AC P40879; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 15-MAR-2017, entry version 163. DE RecName: Full=Chloride anion exchanger; DE AltName: Full=Down-regulated in adenoma; DE Short=Protein DRA; DE AltName: Full=Solute carrier family 26 member 3; GN Name=SLC26A3; Synonyms=DRA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Colon; RX PubMed=7683425; DOI=10.1073/pnas.90.9.4166; RA Schweinfest C.W., Henderson K.W., Suster S., Kondoh N., Papas T.S.; RT "Identification of a colon mucosa gene that is down-regulated in colon RT adenomas and adenocarcinomas."; RL Proc. Natl. Acad. Sci. U.S.A. 90:4166-4170(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP SIMILARITY TO SULFATE PERMEASES. RX PubMed=8140616; DOI=10.1016/0968-0004(94)90168-6; RA Sandal N.N., Marcker K.A.; RT "Similarities between a soybean nodulin, Neurospora crassa sulphate RT permease II and a putative human tumour suppressor."; RL Trends Biochem. Sci. 19:19-19(1994). RN [4] RP INTERACTION WITH PDZK1. RX PubMed=15766278; DOI=10.1021/bi048828b; RA Rossmann H., Jacob P., Baisch S., Hassoun R., Meier J., Natour D., RA Yahya K., Yun C., Biber J., Lackner K.J., Fiehn W., Gregor M., RA Seidler U., Lamprecht G.; RT "The CFTR associated protein CAP70 interacts with the apical Cl-/HCO3- RT exchanger DRA in rabbit small intestinal mucosa."; RL Biochemistry 44:4477-4487(2005). RN [5] RP GLYCOSYLATION AT ASN-153; ASN-161 AND ASN-165, AND SUBCELLULAR RP LOCATION. RX PubMed=22159084; DOI=10.1152/ajpcell.00165.2011; RA Hayashi H., Yamashita Y.; RT "Role of N-glycosylation in cell surface expression and protection RT against proteolysis of the intestinal anion exchanger SLC26A3."; RL Am. J. Physiol. 302:C781-C795(2012). RN [6] RP VARIANTS DIAR1 LEU-124 AND VAL-318 DEL, AND VARIANT TRP-307. RX PubMed=8896562; DOI=10.1038/ng1196-316; RA Hoeglund P., Haila S., Socha J., Tomaszewski L., Saarialho-Kere U., RA Karjalainen-Lindsberg M.-L., Airola K., Holmberg C., RA de la Chapelle A., Kere J.; RT "Mutations of the Down-regulated in adenoma (DRA) gene cause RT congenital chloride diarrhoea."; RL Nat. Genet. 14:316-319(1996). RN [7] RP VARIANTS DIAR1 SER-120; LEU-124; ARG-131 AND ARG-496. RX PubMed=9718329; DOI=10.1086/301998; RA Hoglund P., Auranen M., Socha J., Popinska K., Nazer H., Rajaram U., RA Al Sanie A., Al-Ghanim M., Holmberg C., de la Chapelle A., Kere J.; RT "Genetic background of congenital chloride diarrhea in high-incidence RT populations: Finland, Poland, and Saudi Arabia and Kuwait."; RL Am. J. Hum. Genet. 63:760-768(1998). RN [8] RP VARIANTS DIAR1 SER-120; ARG-131; VAL-318 DEL AND TYR-527 DEL. RX PubMed=9554749; RX DOI=10.1002/(SICI)1098-1004(1998)11:4<321::AID-HUMU10>3.0.CO;2-A; RA Hoeglund P., Haila S., Gustavson K.-H., Taipale M., Hannula K., RA Popinska K., Holmberg C., Socha J., de la Chapelle A., Kere J.; RT "Clustering of private mutations in the congenital chloride RT diarrhea/down-regulated in adenoma gene."; RL Hum. Mutat. 11:321-327(1998). RN [9] RP VARIANTS DIAR1 PRO-206 AND VAL-468. RX PubMed=11524734; DOI=10.1002/humu.1179; RA Hoeglund P., Sormaala M., Haila S., Socha J., Rajaram U., RA Scheurlen W., Sinaasappel M., de Jonge H., Holmberg C., Yoshikawa H., RA Kere J.; RT "Identification of seven novel mutations including the first two RT genomic rearrangements in SLC26A3 mutated in congenital chloride RT diarrhea."; RL Hum. Mutat. 18:233-242(2001). RN [10] RP VARIANTS DIAR1 CYS-520 AND ASN-652. RX PubMed=19861545; DOI=10.1073/pnas.0910672106; RA Choi M., Scholl U.I., Ji W., Liu T., Tikhonova I.R., Zumbo P., RA Nayir A., Bakkaloglu A., Ozen S., Sanjad S., Nelson-Williams C., RA Farhi A., Mane S., Lifton R.P.; RT "Genetic diagnosis by whole exome capture and massively parallel DNA RT sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 106:19096-19101(2009). RN [11] RP VARIANTS DIAR1 LEU-129; LEU-131; ILE-136; ASP-204; PRO-220; TYR-343; RP 344-PHE--VAL-349 DELINS ASP-ALA; ALA-379; PHE-398; ASN-521 AND RP ASN-544. RX PubMed=21394828; DOI=10.1002/humu.21498; RA Wedenoja S., Pekansaari E., Hoglund P., Makela S., Holmberg C., RA Kere J.; RT "Update on SLC26A3 mutations in congenital chloride diarrhea."; RL Hum. Mutat. 32:715-722(2011). RN [12] RP VARIANT DIAR1 PRO-220. RX PubMed=21150650; DOI=10.1097/MPG.0b013e3181f28d1a; RA Rodriguez-Herrera A., Navas-Lopez V.M., Redondo-Nevado J., RA Gutierrez G.; RT "Compound heterozygous mutations in the SLC26A3 gene in 2 Spanish RT siblings with congenital chloride diarrhea."; RL J. Pediatr. Gastroenterol. Nutr. 52:106-110(2011). RN [13] RP VARIANT DIAR1 SER-175. RX PubMed=22779076; DOI=10.3343/alm.2012.32.4.312; RA Lee E.S., Cho A.R., Ki C.S.; RT "Identification of SLC26A3 mutations in a Korean patient with RT congenital chloride diarrhea."; RL Ann. Lab. Med. 32:312-315(2012). RN [14] RP VARIANTS DIAR1 LEU-131 AND ASN-134. RX PubMed=23274434; DOI=10.1007/s00431-012-1905-3; RA Hong J., Seo J.K., Ko J.S., Cheong H.I., Choi J.H., Lee J.H., RA Seo J.W.; RT "Congenital chloride diarrhea in Korean children: novel mutations and RT genetic characteristics."; RL Eur. J. Pediatr. 172:545-550(2013). RN [15] RP VARIANTS DIAR1 SER-120; LEU-129; ARG-131; VAL-318 DEL; ILE-394; RP PRO-438; PRO-495; ARG-508; GLU-547; PRO-654 AND ILE-675 INS. RX PubMed=27657883; DOI=10.1097/MPG.0000000000001418; RA Amato F., Cardillo G., Liguori R., Scorza M., Comegna M., Elce A., RA Giordano S., Lucaccioni L., Lugli L., Cardile S., Romano C., RA Pezzella V., Castaldo G., Canani R.B.; RT "Twelve novel mutations in the SLC26A3 gene in 17 sporadic cases of RT congenital chloride diarrhea."; RL J. Pediatr. Gastroenterol. Nutr. 0:0-0(2016). CC -!- FUNCTION: Chloride/bicarbonate exchanger. Mediates the efficient CC absorption of chloride ions in the colon, participating in fluid CC homeostasis. Plays a role in the chloride and bicarbonate CC homeostasis during sperm epididymal maturation and capacitation. CC -!- SUBUNIT: Interacts with CFTR, SLC26A6 and SLC9A3R1 (By CC similarity). Interacts with PDZK1. {ECO:0000250, CC ECO:0000269|PubMed:15766278}. CC -!- INTERACTION: CC Q15599:SLC9A3R2; NbExp=5; IntAct=EBI-8542350, EBI-1149760; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:22159084}; Multi-pass membrane protein CC {ECO:0000269|PubMed:22159084}. Membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. Note=Localized in sperm membranes. CC Midpiece of sperm tail. Colocalizes with CFTR at the midpiece of CC sperm tail (By similarity). {ECO:0000250}. CC -!- DEVELOPMENTAL STAGE: Expression is significantly decreased in CC adenomas (polyps) and adenocarcinomas of the colon. CC -!- PTM: N-glycosylation is required for efficient cell surface CC expression, and protection from proteolytic degradation. CC {ECO:0000269|PubMed:22159084}. CC -!- DISEASE: Diarrhea 1, secretory chloride, congenital (DIAR1) CC [MIM:214700]: A disease characterized by voluminous watery stools CC containing an excess of chloride. The children with this disease CC are often premature. {ECO:0000269|PubMed:11524734, CC ECO:0000269|PubMed:19861545, ECO:0000269|PubMed:21150650, CC ECO:0000269|PubMed:21394828, ECO:0000269|PubMed:22779076, CC ECO:0000269|PubMed:23274434, ECO:0000269|PubMed:27657883, CC ECO:0000269|PubMed:8896562, ECO:0000269|PubMed:9554749, CC ECO:0000269|PubMed:9718329}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L02785; AAA58443.1; -; mRNA. DR EMBL; BC025671; AAH25671.1; -; mRNA. DR CCDS; CCDS5748.1; -. DR PIR; A47456; A47456. DR RefSeq; NP_000102.1; NM_000111.2. DR RefSeq; XP_011514169.1; XM_011515867.2. DR UniGene; Hs.1650; -. DR ProteinModelPortal; P40879; -. DR BioGrid; 108145; 1. DR IntAct; P40879; 2. DR MINT; MINT-1787198; -. DR STRING; 9606.ENSP00000345873; -. DR TCDB; 2.A.53.2.18; the sulfate permease (sulp) family. DR iPTMnet; P40879; -. DR PhosphoSitePlus; P40879; -. DR BioMuta; SLC26A3; -. DR DMDM; 729367; -. DR PaxDb; P40879; -. DR PeptideAtlas; P40879; -. DR PRIDE; P40879; -. DR DNASU; 1811; -. DR Ensembl; ENST00000340010; ENSP00000345873; ENSG00000091138. DR GeneID; 1811; -. DR KEGG; hsa:1811; -. DR UCSC; uc003ver.3; human. DR CTD; 1811; -. DR DisGeNET; 1811; -. DR GeneCards; SLC26A3; -. DR HGNC; HGNC:3018; SLC26A3. DR HPA; HPA036055; -. DR MalaCards; SLC26A3; -. DR MIM; 126650; gene. DR MIM; 214700; phenotype. DR neXtProt; NX_P40879; -. DR OpenTargets; ENSG00000091138; -. DR Orphanet; 53689; Congenital chloride diarrhea. DR PharmGKB; PA35044; -. DR eggNOG; KOG0236; Eukaryota. DR eggNOG; COG0659; LUCA. DR GeneTree; ENSGT00760000119026; -. DR HOGENOM; HOG000006546; -. DR HOVERGEN; HBG000639; -. DR InParanoid; P40879; -. DR KO; K14078; -. DR OMA; QETIGDC; -. DR OrthoDB; EOG091G07RT; -. DR PhylomeDB; P40879; -. DR TreeFam; TF313784; -. DR Reactome; R-HSA-427601; Multifunctional anion exchangers. DR GeneWiki; SLC26A3; -. DR GenomeRNAi; 1811; -. DR PRO; PR:P40879; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000091138; -. DR CleanEx; HS_SLC26A3; -. DR ExpressionAtlas; P40879; baseline and differential. DR Genevisible; P40879; HS. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB. DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central. DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0005452; F:inorganic anion exchanger activity; TAS:Reactome. DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc. DR GO; GO:0005215; F:transporter activity; TAS:ProtInc. DR GO; GO:0006820; P:anion transport; TAS:ProtInc. DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central. DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB. DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central. DR GO; GO:0007588; P:excretion; TAS:ProtInc. DR GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB. DR GO; GO:0006811; P:ion transport; TAS:Reactome. DR GO; GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB. DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central. DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central. DR GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB. DR Gene3D; 3.30.750.24; -; 2. DR InterPro; IPR018045; S04_transporter_CS. DR InterPro; IPR011547; SLC26A/SulP_dom. DR InterPro; IPR001902; SLC26A/SulP_fam. DR InterPro; IPR030321; SLC26A3. DR InterPro; IPR002645; STAS_dom. DR PANTHER; PTHR11814; PTHR11814; 1. DR PANTHER; PTHR11814:SF150; PTHR11814:SF150; 1. DR Pfam; PF01740; STAS; 1. DR Pfam; PF00916; Sulfate_transp; 1. DR SUPFAM; SSF52091; SSF52091; 2. DR TIGRFAMs; TIGR00815; sulP; 1. DR PROSITE; PS01130; SLC26A; 1. DR PROSITE; PS50801; STAS; 1. PE 1: Evidence at protein level; KW Antiport; Cell membrane; Chloride; Complete proteome; KW Disease mutation; Glycoprotein; Membrane; Polymorphism; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 764 Chloride anion exchanger. FT /FTId=PRO_0000080161. FT TOPO_DOM 1 76 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 77 97 Helical. {ECO:0000255}. FT TOPO_DOM 98 99 Extracellular. {ECO:0000305}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TOPO_DOM 121 124 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. FT TOPO_DOM 146 175 Extracellular. {ECO:0000305}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. FT TOPO_DOM 197 197 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 198 218 Helical. {ECO:0000255}. FT TOPO_DOM 219 257 Extracellular. {ECO:0000305}. FT TRANSMEM 258 278 Helical. {ECO:0000255}. FT TOPO_DOM 279 342 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 343 363 Helical. {ECO:0000255}. FT TOPO_DOM 364 374 Extracellular. {ECO:0000305}. FT TRANSMEM 375 395 Helical. {ECO:0000255}. FT TOPO_DOM 396 411 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 412 432 Helical. {ECO:0000255}. FT TOPO_DOM 433 469 Extracellular. {ECO:0000305}. FT TRANSMEM 470 490 Helical. {ECO:0000255}. FT TOPO_DOM 491 701 Cytoplasmic. {ECO:0000305}. FT DOMAIN 525 720 STAS. {ECO:0000255|PROSITE- FT ProRule:PRU00198}. FT CARBOHYD 153 153 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:22159084}. FT CARBOHYD 161 161 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:22159084}. FT CARBOHYD 165 165 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:22159084}. FT VARIANT 68 68 R -> Q (in dbSNP:rs10280704). FT /FTId=VAR_053660. FT VARIANT 120 120 G -> S (in DIAR1; dbSNP:rs386833479). FT {ECO:0000269|PubMed:27657883, FT ECO:0000269|PubMed:9554749, FT ECO:0000269|PubMed:9718329}. FT /FTId=VAR_007428. FT VARIANT 124 124 H -> L (in DIAR1; dbSNP:rs121913030). FT {ECO:0000269|PubMed:8896562, FT ECO:0000269|PubMed:9718329}. FT /FTId=VAR_007429. FT VARIANT 129 129 P -> L (in DIAR1; dbSNP:rs386833480). FT {ECO:0000269|PubMed:21394828, FT ECO:0000269|PubMed:27657883}. FT /FTId=VAR_066062. FT VARIANT 131 131 P -> L (in DIAR1; dbSNP:rs386833481). FT {ECO:0000269|PubMed:21394828, FT ECO:0000269|PubMed:23274434}. FT /FTId=VAR_066063. FT VARIANT 131 131 P -> R (in DIAR1; dbSNP:rs386833481). FT {ECO:0000269|PubMed:27657883, FT ECO:0000269|PubMed:9554749, FT ECO:0000269|PubMed:9718329}. FT /FTId=VAR_007430. FT VARIANT 134 134 S -> N (in DIAR1). FT {ECO:0000269|PubMed:23274434}. FT /FTId=VAR_077354. FT VARIANT 136 136 M -> I (in DIAR1; dbSNP:rs386833483). FT {ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066064. FT VARIANT 175 175 R -> S (in DIAR1; dbSNP:rs386833484). FT {ECO:0000269|PubMed:22779076}. FT /FTId=VAR_077355. FT VARIANT 204 204 Y -> D (in DIAR1; dbSNP:rs386833487). FT {ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066065. FT VARIANT 206 206 S -> P (in DIAR1; dbSNP:rs386833488). FT {ECO:0000269|PubMed:11524734}. FT /FTId=VAR_012777. FT VARIANT 220 220 H -> P (in DIAR1; dbSNP:rs386833489). FT {ECO:0000269|PubMed:21150650, FT ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066066. FT VARIANT 307 307 C -> W (in dbSNP:rs34407351). FT {ECO:0000269|PubMed:8896562}. FT /FTId=VAR_007431. FT VARIANT 318 318 Missing (in DIAR1; dbSNP:rs386833491). FT {ECO:0000269|PubMed:27657883, FT ECO:0000269|PubMed:8896562, FT ECO:0000269|PubMed:9554749}. FT /FTId=VAR_007432. FT VARIANT 343 343 C -> Y (in DIAR1; dbSNP:rs386833444). FT {ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066067. FT VARIANT 344 349 FGIAMV -> DA (in DIAR1). FT {ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066068. FT VARIANT 379 379 G -> A (in DIAR1; dbSNP:rs386833446). FT {ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066069. FT VARIANT 394 394 S -> I (in DIAR1). FT {ECO:0000269|PubMed:27657883}. FT /FTId=VAR_077356. FT VARIANT 398 398 S -> F (in DIAR1; dbSNP:rs143839547). FT {ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066070. FT VARIANT 438 438 S -> P (in DIAR1; dbSNP:rs763669046). FT {ECO:0000269|PubMed:27657883}. FT /FTId=VAR_077357. FT VARIANT 468 468 D -> V (in DIAR1; dbSNP:rs386833454). FT {ECO:0000269|PubMed:11524734}. FT /FTId=VAR_012778. FT VARIANT 495 495 Q -> P (in DIAR1). FT {ECO:0000269|PubMed:27657883}. FT /FTId=VAR_077358. FT VARIANT 496 496 L -> R (in DIAR1; dbSNP:rs386833457). FT {ECO:0000269|PubMed:9718329}. FT /FTId=VAR_066071. FT VARIANT 508 508 C -> R (in DIAR1). FT {ECO:0000269|PubMed:27657883}. FT /FTId=VAR_077359. FT VARIANT 520 520 Y -> C (in DIAR1; dbSNP:rs386833462). FT {ECO:0000269|PubMed:19861545}. FT /FTId=VAR_066072. FT VARIANT 521 521 K -> N (in DIAR1; dbSNP:rs386833463). FT {ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066073. FT VARIANT 527 527 Missing (in DIAR1). FT {ECO:0000269|PubMed:9554749}. FT /FTId=VAR_007433. FT VARIANT 544 544 I -> N (in DIAR1; dbSNP:rs386833467). FT {ECO:0000269|PubMed:21394828}. FT /FTId=VAR_066074. FT VARIANT 547 547 A -> E (in DIAR1). FT {ECO:0000269|PubMed:27657883}. FT /FTId=VAR_077360. FT VARIANT 554 554 R -> Q (in dbSNP:rs2301635). FT /FTId=VAR_053661. FT VARIANT 652 652 D -> N (in DIAR1; dbSNP:rs140426439). FT {ECO:0000269|PubMed:19861545}. FT /FTId=VAR_066075. FT VARIANT 654 654 S -> P (in DIAR1). FT {ECO:0000269|PubMed:27657883}. FT /FTId=VAR_077361. FT VARIANT 675 675 I -> II (in DIAR1; dbSNP:rs121913031). FT {ECO:0000269|PubMed:27657883}. FT /FTId=VAR_077362. FT VARIANT 753 753 N -> S (in dbSNP:rs35342296). FT /FTId=VAR_053662. SQ SEQUENCE 764 AA; 84505 MW; 694C5BC2D4121F6D CRC64; MIEPFGNQYI VARPVYSTNA FEENHKKTGR HHKTFLDHLK VCCSCSPQKA KRIVLSLFPI ASWLPAYRLK EWLLSDIVSG ISTGIVAVLQ GLAFALLVDI PPVYGLYASF FPAIIYLFFG TSRHISVGPF PILSMMVGLA VSGAVSKAVP DRNATTLGLP NNSNNSSLLD DERVRVAAAA SVTVLSGIIQ LAFGILRIGF VVIYLSESLI SGFTTAAAVH VLVSQLKFIF QLTVPSHTDP VSIFKVLYSV FSQIEKTNIA DLVTALIVLL VVSIVKEINQ RFKDKLPVPI PIEFIMTVIA AGVSYGCDFK NRFKVAVVGD MNPGFQPPIT PDVETFQNTV GDCFGIAMVA FAVAFSVASV YSLKYDYPLD GNQELIALGL GNIVCGVFRG FAGSTALSRS AVQESTGGKT QIAGLIGAII VLIVVLAIGF LLAPLQKSVL AALALGNLKG MLMQFAEIGR LWRKDKYDCL IWIMTFIFTI VLGLGLGLAA SVAFQLLTIV FRTQFPKCST LANIGRTNIY KNKKDYYDMY EPEGVKIFRC PSPIYFANIG FFRRKLIDAV GFSPLRILRK RNKALRKIRK LQKQGLLQVT PKGFICTVDT IKDSDEELDN NQIEVLDQPI NTTDLPFHID WNDDLPLNIE VPKISLHSLI LDFSAVSFLD VSSVRGLKSI LQEFIRIKVD VYIVGTDDDF IEKLNRYEFF DGEVKSSIFF LTIHDAVLHI LMKKDYSTSK FNPSQEKDGK IDFTINTNGG LRNRVYEVPV ETKF //