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Database: UniProt
Entry: S2611_HUMAN
LinkDB: S2611_HUMAN
Original site: S2611_HUMAN 
ID   S2611_HUMAN             Reviewed;         606 AA.
AC   Q86WA9; B2RCI7; Q86VX1; Q86YX7; Q8IV11; Q8N2I1; Q8NG03;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Sodium-independent sulfate anion transporter;
DE   AltName: Full=Solute carrier family 26 member 11;
GN   Name=SLC26A11 {ECO:0000312|HGNC:HGNC:14471};
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] {ECO:0000305, ECO:0000312|EMBL:CAD66450.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Endothelial cell {ECO:0000312|EMBL:CAD66450.1};
RX   PubMed=12626430; DOI=10.1096/fj.02-0787fje;
RA   Vincourt J.-B., Jullien D., Amalric F., Girard J.-P.;
RT   "Molecular and functional characterization of SLC26A11, a sodium-
RT   independent sulfate transporter from high endothelial venules.";
RL   FASEB J. 17:890-892(2003).
RN   [2] {ECO:0000312|EMBL:AAO26673.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mount D.B.;
RT   "Characterization of Homo sapiens SLC26A11, a putative anion exchanger.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [4] {ECO:0000312|EMBL:BAC11496.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thyroid {ECO:0000312|EMBL:BAC11496.1};
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [5] {ECO:0000312|EMBL:AAH47451.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain {ECO:0000312|EMBL:AAH35900.2}, and
RC   Hypothalamus {ECO:0000312|EMBL:AAH47451.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAM92902.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 307-599, AND TISSUE SPECIFICITY.
RX   PubMed=11087667; DOI=10.1006/geno.2000.6355;
RA   Lohi H., Kujala M., Kerkelae E., Saarialho-Kere U., Kestilae M., Kere J.;
RT   "Mapping of five new putative anion transporter genes in human and
RT   characterization of SLC26A6, a candidate gene for pancreatic anion
RT   exchanger.";
RL   Genomics 70:102-112(2000).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Placenta;
RX   PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA   Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA   Elsaesser H.-P., Mann M., Hasilik A.;
RT   "Integral and associated lysosomal membrane proteins.";
RL   Traffic 8:1676-1686(2007).
RN   [8]
RP   REVIEW, AND SUBCELLULAR LOCATION.
RX   PubMed=20957757; DOI=10.1002/pmic.201000196;
RA   Schroeder B.A., Wrocklage C., Hasilik A., Saftig P.;
RT   "The proteome of lysosomes.";
RL   Proteomics 10:4053-4076(2010).
RN   [9]
RP   VARIANT CYS-122.
RX   PubMed=22521418; DOI=10.1016/j.ajhg.2012.03.012;
RA   Jordan C.T., Cao L., Roberson E.D., Pierson K.C., Yang C.F., Joyce C.E.,
RA   Ryan C., Duan S., Helms C.A., Liu Y., Chen Y., McBride A.A., Hwu W.L.,
RA   Wu J.Y., Chen Y.T., Menter A., Goldbach-Mansky R., Lowes M.A.,
RA   Bowcock A.M.;
RT   "PSORS2 is due to mutations in CARD14.";
RL   Am. J. Hum. Genet. 90:784-795(2012).
CC   -!- FUNCTION: Sodium-independent anion exchanger mediating bicarbonate,
CC       chloride, sulfate and oxalate transport (By similarity). Exhibits
CC       sodium-independent sulfate anion transporter activity that may
CC       cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake into
CC       high endothelial venules endothelial cells (HEVEC) (PubMed:12626430).
CC       In the kidney, mediates chloride-bicarbonate exchange, facilitating V-
CC       ATPase-mediated acid secretion (By similarity). May function as a
CC       chloride channel, playing an important role in moderating chloride
CC       homeostasis and neuronal activity in the cerebellum (By similarity).
CC       {ECO:0000250|UniProtKB:G3C7W6, ECO:0000250|UniProtKB:Q80ZD3,
CC       ECO:0000269|PubMed:12626430}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) +
CC         hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:G3C7W6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + sulfate(in) = H(+)(out) + sulfate(out);
CC         Xref=Rhea:RHEA:28574, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189;
CC         Evidence={ECO:0000250|UniProtKB:G3C7W6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + oxalate(in) = chloride(in) + oxalate(out);
CC         Xref=Rhea:RHEA:72263, ChEBI:CHEBI:17996, ChEBI:CHEBI:30623;
CC         Evidence={ECO:0000250|UniProtKB:G3C7W6};
CC   -!- INTERACTION:
CC       Q86WA9; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-19115335, EBI-12188413;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12626430};
CC       Multi-pass membrane protein {ECO:0000255}. Lysosome membrane
CC       {ECO:0000269|PubMed:20957757}; Multi-pass membrane protein
CC       {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q80ZD3};
CC       Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q80ZD3}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Detected in all tissues tested with highest
CC       expression observed in brain, kidney, HEVEC and placenta and lowest in
CC       pancreas, skeletal muscle, liver, lung and heart.
CC       {ECO:0000269|PubMed:11087667, ECO:0000269|PubMed:12626430}.
CC   -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC       {ECO:0000255}.
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DR   EMBL; AJ544073; CAD66450.1; -; mRNA.
DR   EMBL; AF345195; AAO26673.1; -; mRNA.
DR   EMBL; AK315132; BAG37584.1; -; mRNA.
DR   EMBL; AK075248; BAC11496.1; -; mRNA.
DR   EMBL; BC035900; AAH35900.2; -; mRNA.
DR   EMBL; BC047451; AAH47451.1; -; mRNA.
DR   EMBL; AF331524; AAM92902.1; -; mRNA.
DR   CCDS; CCDS11771.2; -.
DR   RefSeq; NP_001159819.1; NM_001166347.1.
DR   RefSeq; NP_001159820.1; NM_001166348.1.
DR   RefSeq; NP_001159821.1; NM_001166349.1.
DR   RefSeq; NP_775897.3; NM_173626.3.
DR   AlphaFoldDB; Q86WA9; -.
DR   SMR; Q86WA9; -.
DR   BioGRID; 129771; 12.
DR   IntAct; Q86WA9; 3.
DR   MINT; Q86WA9; -.
DR   STRING; 9606.ENSP00000355384; -.
DR   TCDB; 2.A.53.1.10; the sulfate permease (sulp) family.
DR   iPTMnet; Q86WA9; -.
DR   PhosphoSitePlus; Q86WA9; -.
DR   SwissPalm; Q86WA9; -.
DR   BioMuta; SLC26A11; -.
DR   DMDM; 182705284; -.
DR   EPD; Q86WA9; -.
DR   jPOST; Q86WA9; -.
DR   MassIVE; Q86WA9; -.
DR   MaxQB; Q86WA9; -.
DR   PaxDb; 9606-ENSP00000355384; -.
DR   PeptideAtlas; Q86WA9; -.
DR   ProteomicsDB; 70139; -.
DR   Antibodypedia; 32732; 41 antibodies from 11 providers.
DR   DNASU; 284129; -.
DR   Ensembl; ENST00000361193.8; ENSP00000355384.3; ENSG00000181045.15.
DR   Ensembl; ENST00000411502.7; ENSP00000403998.3; ENSG00000181045.15.
DR   Ensembl; ENST00000546047.6; ENSP00000440724.2; ENSG00000181045.15.
DR   Ensembl; ENST00000572725.5; ENSP00000459470.1; ENSG00000181045.15.
DR   GeneID; 284129; -.
DR   KEGG; hsa:284129; -.
DR   MANE-Select; ENST00000361193.8; ENSP00000355384.3; NM_001166347.2; NP_001159819.1.
DR   UCSC; uc002jyb.3; human.
DR   AGR; HGNC:14471; -.
DR   CTD; 284129; -.
DR   DisGeNET; 284129; -.
DR   GeneCards; SLC26A11; -.
DR   HGNC; HGNC:14471; SLC26A11.
DR   HPA; ENSG00000181045; Low tissue specificity.
DR   MIM; 610117; gene.
DR   neXtProt; NX_Q86WA9; -.
DR   OpenTargets; ENSG00000181045; -.
DR   PharmGKB; PA37888; -.
DR   VEuPathDB; HostDB:ENSG00000181045; -.
DR   eggNOG; KOG0236; Eukaryota.
DR   GeneTree; ENSGT01070000253775; -.
DR   HOGENOM; CLU_003182_12_2_1; -.
DR   InParanoid; Q86WA9; -.
DR   OMA; VTNKFPI; -.
DR   OrthoDB; 1082533at2759; -.
DR   PhylomeDB; Q86WA9; -.
DR   TreeFam; TF323537; -.
DR   PathwayCommons; Q86WA9; -.
DR   Reactome; R-HSA-427601; Multifunctional anion exchangers.
DR   SignaLink; Q86WA9; -.
DR   BioGRID-ORCS; 284129; 11 hits in 1134 CRISPR screens.
DR   ChiTaRS; SLC26A11; human.
DR   GenomeRNAi; 284129; -.
DR   Pharos; Q86WA9; Tdark.
DR   PRO; PR:Q86WA9; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q86WA9; Protein.
DR   Bgee; ENSG00000181045; Expressed in pancreatic ductal cell and 173 other cell types or tissues.
DR   ExpressionAtlas; Q86WA9; baseline and differential.
DR   Genevisible; Q86WA9; HS.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; ISS:UniProtKB.
DR   GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IDA:UniProtKB.
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:0006811; P:monoatomic ion transport; TAS:Reactome.
DR   GO; GO:0019532; P:oxalate transport; ISS:UniProtKB.
DR   GO; GO:0008272; P:sulfate transport; IDA:UniProtKB.
DR   CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR018045; S04_transporter_CS.
DR   InterPro; IPR011547; SLC26A/SulP_dom.
DR   InterPro; IPR001902; SLC26A/SulP_fam.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR11814:SF55; SODIUM-INDEPENDENT SULFATE ANION TRANSPORTER; 1.
DR   PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS01130; SLC26A; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
KW   Anion exchange; Cell membrane; Ion transport; Lysosome; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..606
FT                   /note="Sodium-independent sulfate anion transporter"
FT                   /id="PRO_0000320686"
FT   TOPO_DOM        1..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..100
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..119
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..147
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..197
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..307
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..341
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..374
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        396..398
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..606
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          470..584
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   VARIANT         122
FT                   /note="Y -> C (in dbSNP:rs765188926)"
FT                   /evidence="ECO:0000269|PubMed:22521418"
FT                   /id="VAR_068239"
FT   CONFLICT        14
FT                   /note="S -> Y (in Ref. 1; CAD66450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="L -> M (in Ref. 1; CAD66450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="V -> M (in Ref. 6; AAM92902)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="F -> S (in Ref. 2; AAO26673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332
FT                   /note="N -> D (in Ref. 1; CAD66450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        415
FT                   /note="V -> A (in Ref. 2; AAO26673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="Y -> H (in Ref. 2; AAO26673)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        579
FT                   /note="H -> R (in Ref. 4; BAC11496)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        583
FT                   /note="E -> K (in Ref. 5; AAH35900)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   606 AA;  65299 MW;  A0D974B49F16450D CRC64;
     MPSSVTALGQ ARSSGPGMAP SACCCSPAAL QRRLPILAWL PSYSLQWLKM DFVAGLSVGL
     TAIPQALAYA EVAGLPPQYG LYSAFMGCFV YFFLGTSRDV TLGPTAIMSL LVSFYTFHEP
     AYAVLLAFLS GCIQLAMGVL RLGFLLDFIS YPVIKGFTSA AAVTIGFGQI KNLLGLQNIP
     RPFFLQVYHT FLRIAETRVG DAVLGLVCML LLLVLKLMRD HVPPVHPEMP PGVRLSRGLV
     WAATTARNAL VVSFAALVAY SFEVTGYQPF ILTGETAEGL PPVRIPPFSV TTANGTISFT
     EMVQDMGAGL AVVPLMGLLE SIAVAKAFAS QNNYRIDANQ ELLAIGLTNM LGSLVSSYPV
     TGSFGRTAVN AQSGVCTPAG GLVTGVLVLL SLDYLTSLFY YIPKSALAAV IIMAVAPLFD
     TKIFRTLWRV KRLDLLPLCV TFLLCFWEVQ YGILAGALVS LLMLLHSAAR PETKVSEGPV
     LVLQPASGLS FPAMEALREE ILSRALEVSP PRCLVLECTH VCSIDYTVVL GLGELLQDFQ
     KQGVALAFVG LQVPVLRVLL SADLKGFQYF STLEEAEKHL RQEPGTQPYN IREDSILDQK
     VALLKA
//
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