S12A2_MOUSE
ID S12A2_MOUSE Reviewed; 1205 AA.
AC P55012; E9PYU3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Solute carrier family 12 member 2;
DE AltName: Full=Basolateral Na-K-Cl symporter;
DE AltName: Full=Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2;
GN Name=Slc12a2; Synonyms=Nkcc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7929272; DOI=10.1016/s0021-9258(18)47302-4;
RA Delpire E., Rauchman M.I., Beier D.R., Hebert S.C., Gullans S.R.;
RT "Molecular cloning and chromosome localization of a putative basolateral
RT Na(+)-K(+)-2Cl-cotransporter from mouse inner medullary collecting duct
RT (mIMCD-3) cells.";
RL J. Biol. Chem. 269:25677-25683(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-259 AND SER-933, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937 AND SER-987, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP MUTAGENESIS OF ALA-320; ASN-369; ALA-372; ARG-403; 885-TRP--SER-1205 AND
RP GLU-973, AND FUNCTION.
RX PubMed=32658972; DOI=10.1093/brain/awaa176;
RA McNeill A., Iovino E., Mansard L., Vache C., Baux D., Bedoukian E., Cox H.,
RA Dean J., Goudie D., Kumar A., Newbury-Ecob R., Fallerini C., Renieri A.,
RA Lopergolo D., Mari F., Blanchet C., Willems M., Roux A.F., Pippucci T.,
RA Delpire E.;
RT "SLC12A2 variants cause a neurodevelopmental disorder or cochleovestibular
RT defect.";
RL Brain 143:2380-2387(2020).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=32294086; DOI=10.1371/journal.pgen.1008643;
RA Mutai H., Wasano K., Momozawa Y., Kamatani Y., Miya F., Masuda S.,
RA Morimoto N., Nara K., Takahashi S., Tsunoda T., Homma K., Kubo M.,
RA Matsunaga T.;
RT "Variants encoding a restricted carboxy-terminal domain of SLC12A2 cause
RT hereditary hearing loss in humans.";
RL PLoS Genet. 16:e1008643-e1008643(2020).
CC -!- FUNCTION: Cation-chloride cotransporter which mediates the
CC electroneutral transport of chloride, potassium and/or sodium ions
CC across the membrane (PubMed:32658972). Plays a vital role in the
CC regulation of ionic balance and cell volume.
CC {ECO:0000250|UniProtKB:P55011, ECO:0000269|PubMed:32658972}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P55011}.
CC -!- INTERACTION:
CC P55012; P47811: Mapk14; NbExp=2; IntAct=EBI-621078, EBI-298727;
CC P55012; Q9Z1W9: Stk39; NbExp=3; IntAct=EBI-621078, EBI-444764;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:A0A0G2KTI4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression found in the
CC cochlea, cochlear lateral wall, and the choroid plexus
CC (PubMed:32294086). Lower expression found in the cerebellum and the
CC cortex (PubMed:32294086). {ECO:0000269|PubMed:32294086}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
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DR EMBL; U13174; AAC77832.1; -; mRNA.
DR EMBL; AC127678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A55015; A55015.
DR RefSeq; NP_033220.2; NM_009194.3.
DR AlphaFoldDB; P55012; -.
DR SMR; P55012; -.
DR BioGRID; 203277; 8.
DR ELM; P55012; -.
DR IntAct; P55012; 4.
DR MINT; P55012; -.
DR STRING; 10090.ENSMUSP00000111023; -.
DR GlyGen; P55012; 2 sites.
DR iPTMnet; P55012; -.
DR PhosphoSitePlus; P55012; -.
DR SwissPalm; P55012; -.
DR EPD; P55012; -.
DR jPOST; P55012; -.
DR MaxQB; P55012; -.
DR PaxDb; P55012; -.
DR PeptideAtlas; P55012; -.
DR PRIDE; P55012; -.
DR ProteomicsDB; 253337; -.
DR DNASU; 20496; -.
DR GeneID; 20496; -.
DR KEGG; mmu:20496; -.
DR CTD; 6558; -.
DR MGI; MGI:101924; Slc12a2.
DR eggNOG; KOG2083; Eukaryota.
DR InParanoid; P55012; -.
DR OrthoDB; 254933at2759; -.
DR Reactome; R-MMU-426117; Cation-coupled Chloride cotransporters.
DR BioGRID-ORCS; 20496; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Slc12a2; mouse.
DR PRO; PR:P55012; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P55012; protein.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0042995; C:cell projection; IDA:ARUK-UCL.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015377; F:cation:chloride symporter activity; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0008511; F:sodium:potassium:chloride symporter activity; ISO:MGI.
DR GO; GO:0072488; P:ammonium transmembrane transport; ISO:MGI.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0006884; P:cell volume homeostasis; IMP:ARUK-UCL.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IMP:ARUK-UCL.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:ARUK-UCL.
DR GO; GO:1990869; P:cellular response to chemokine; IMP:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0035865; P:cellular response to potassium ion; IMP:ARUK-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:ARUK-UCL.
DR GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:MGI.
DR GO; GO:0006972; P:hyperosmotic response; ISO:MGI.
DR GO; GO:0098658; P:inorganic anion import across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0098659; P:inorganic cation import across plasma membrane; ISO:MGI.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0061044; P:negative regulation of vascular wound healing; IMP:ARUK-UCL.
DR GO; GO:1904450; P:positive regulation of aspartate secretion; IMP:ARUK-UCL.
DR GO; GO:0045795; P:positive regulation of cell volume; ISO:MGI.
DR GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:1904464; P:regulation of matrix metallopeptidase secretion; IMP:ARUK-UCL.
DR GO; GO:0150003; P:regulation of spontaneous synaptic transmission; IMP:ARUK-UCL.
DR GO; GO:0055078; P:sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR GO; GO:0010818; P:T cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0070634; P:transepithelial ammonium transport; ISO:MGI.
DR GO; GO:0030321; P:transepithelial chloride transport; ISO:MGI.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR013612; AA_permease_N.
DR InterPro; IPR002444; NKCC1.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR002443; SLC12A1/SLC12A2.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF58; PTHR11827:SF58; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF08403; AA_permease_N; 1.
DR Pfam; PF03522; SLC12; 1.
DR PRINTS; PR01207; NAKCLTRNSPRT.
DR PRINTS; PR01208; NAKCLTRSPRT1.
DR TIGRFAMs; TIGR00930; 2a30; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Chloride; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1205
FT /note="Solute carrier family 12 member 2"
FT /id="PRO_0000178024"
FT TOPO_DOM 1..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 280..306
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT INTRAMEM 280..292
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT INTRAMEM 293..300
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT INTRAMEM 301..306
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 307..314
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 315..336
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 337..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 355..390
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 391..399
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 400..417
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 418..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 423..447
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 448..479
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 480..500
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT INTRAMEM 480..491
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT INTRAMEM 492..493
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT INTRAMEM 494..500
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 501..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 508..535
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 536..592
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 593..625
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 626..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 647..661
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 662..663
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 664..690
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 691..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 705..723
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 724
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TRANSMEM 725..744
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT TOPO_DOM 745..1205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55014"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55016"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55016"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 556..561
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT DISULFID 570..575
FT /evidence="ECO:0000250|UniProtKB:P55011"
FT MUTAGEN 320
FT /note="A->V: Reduced potassium ion transmembrane
FT transport."
FT /evidence="ECO:0000269|PubMed:32658972"
FT MUTAGEN 369
FT /note="N->I: Reduced potassium ion transmembrane
FT transport."
FT /evidence="ECO:0000269|PubMed:32658972"
FT MUTAGEN 372
FT /note="A->L: Reduced potassium ion transmembrane
FT transport."
FT /evidence="ECO:0000269|PubMed:32658972"
FT MUTAGEN 403
FT /note="R->Q: Reduced potassium ion transmembrane
FT transport."
FT /evidence="ECO:0000269|PubMed:32658972"
FT MUTAGEN 885..1205
FT /note="Missing: Reduced potassium ion transmembrane
FT transport."
FT /evidence="ECO:0000269|PubMed:32658972"
FT MUTAGEN 973
FT /note="E->K: Reduced potassium ion transmembrane
FT transport."
FT /evidence="ECO:0000269|PubMed:32658972"
FT CONFLICT 7
FT /note="R -> G (in Ref. 1; AAC77832)"
FT /evidence="ECO:0000305"
FT CONFLICT 1097
FT /note="F -> Y (in Ref. 1; AAC77832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1205 AA; 131034 MW; 4DE24CC8070D42F2 CRC64;
MEPGPARPRL APAARPGWGR AAGCRRRGGP ARHGRASGQE DATTAGRQAG GGVRGEGTPA
AGDGLGRPLG PTPSQSRFQV DPVSENAGRA AAAAAAAAAA AAAAGAAGKE TPAAGKAGGE
SGVAKGSEEA KGRFRVNFVD PAASSSADDS LSDAAGVGGD GPNVSFQNGG DTVLSEGSSL
HSGGGSGHHQ QYYYDTHTNT YYLRTFGHNT MDAVPRIDHY RHTAAQLGEK LLRPSLAELH
DELEKEPFED GFANGEESTP TRDAVVAYTA ESKGVVKFGW IKGVLVRCML NIWGVMLFIR
LSWIVGQAGI GLSVVVIAMA TVVTTITGLS TSAIATNGFV RGGGAYYLIS RSLGPEFGGA
IGLIFAFANA VAVAMYVVGF AETVVELLKE HSILMIDEIN DIRIIGAITV VILLGISVAG
MEWEAKAQIV LLVILLLAIA DFVIGTFISL ESKKPKGFFG YKSEIFNENF GPDFREEETF
FSVFAIFFPA ATGILAGANI SGDLADPQSA IPKGTLLAIL ITTVVYIGIA VSVGSCVVRD
ATGNVNDTIT TELTNCTSAA CKLNFDFSYC ESNTCSYGLM NNFQVMSMVS GFAPLISAGI
FSATLSSALA SLVSAPKIFQ ALCKDNIYPA FQMFAKGYGK NNEPLRGYIL TFLIALGFIL
IAELNVIAPI ISNFFLASYA LINFSVFHAS LAKSPGWRPA FKYYNMWISL IGAILCCIVM
FVINWWAALL TYVIVLGLYI YVTYKKPDVN WGSSTQALTY LSALQHSIRL SGVEDHVKNF
RPQCLVMTGS PNSRPALLHL VHDFTKNVGL MICGHVHMGP RRQAMKEMSI DQARYQRWLI
KNKMKAFYAP VHADDLREGA QYLMQAAGLG RMKPNTLVLG FKKDWLQADM RDVDMYINLF
HDAFDIQFGV VVIRLKEGLD ISHLQGQEEL LSSQEKSPGT KDVVVNVDYS KKSDQDTCKS
SGEKSITQKD EEEDGKTPTQ PLLKKESKGP IVPLNVADQK LLEASTQFQK KQGKNTIDVW
WLFDDGGLTL LIPYLLTTKK KWKDCKIRVF IGGKINRIDH DRRAMATLLS KFRIDFSDIM
VLGDINTKPK KENIIAFDDM IEPYRLHEDD KEQDIADKMK EDEPWRITDN ELELYKTKTY
RQIRLNELLK EHSSTANIIV MSLPVARKGA VSSALYMAWL EALSKDLPPV LLVRGNHQSV
LTFYS
