S12A7_MOUSE
ID S12A7_MOUSE Reviewed; 1083 AA.
AC Q9WVL3; Q3TB23; Q3TDX1; Q3UE50; Q6KAS8;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Solute carrier family 12 member 7;
DE AltName: Full=Electroneutral potassium-chloride cotransporter 4;
DE AltName: Full=K-Cl cotransporter 4;
GN Name=Slc12a7; Synonyms=Kcc4;
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] (ISOFORM 1).
RX PubMed=10347194; DOI=10.1074/jbc.274.23.16355;
RA Mount D.B., Mercado A., Song L., Xu J., George A.L. Jr., Delpire E.,
RA Gamba G.;
RT "Cloning and characterization of KCC3 and KCC4, new members of the cation-
RT chloride cotransporter gene family.";
RL J. Biol. Chem. 274:16355-16362(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1079 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP SUBUNIT.
RX PubMed=11551954; DOI=10.1074/jbc.m107155200;
RA Casula S., Shmukler B.E., Wilhelm S., Stuart-Tilley A.K., Su W.,
RA Chernova M.N., Brugnara C., Alper S.L.;
RT "A dominant negative mutant of the KCC1 K-Cl cotransporter: both N- and C-
RT terminal cytoplasmic domains are required for K-Cl cotransport activity.";
RL J. Biol. Chem. 276:41870-41878(2001).
RN [5]
RP FUNCTION, AND DISEASE.
RX PubMed=11976689; DOI=10.1038/416874a;
RA Boettger T., Huebner C.A., Maier H., Rust M.B., Beck F.X., Jentsch T.J.;
RT "Deafness and renal tubular acidosis in mice lacking the K-Cl co-
RT transporter Kcc4.";
RL Nature 416:874-878(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-33; THR-37 AND
RP SER-50, AND 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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-973 AND THR-980, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, 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 [11]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-312; ASN-331; ASN-344 AND
RP ASN-360.
RX PubMed=23376777; DOI=10.1016/j.bbamcr.2013.01.018;
RA Weng T.Y., Chiu W.T., Liu H.S., Cheng H.C., Shen M.R., Mount D.B.,
RA Chou C.Y.;
RT "Glycosylation regulates the function and membrane localization of KCC4.";
RL Biochim. Biophys. Acta 1833:1133-1146(2013).
CC -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport when
CC activated by cell swelling (By similarity). May mediate K(+) uptake
CC into Deiters' cells in the cochlea and contribute to K(+) recycling in
CC the inner ear. Important for the survival of cochlear outer and inner
CC hair cells and the maintenance of the organ of Corti. May be required
CC for basolateral Cl(-) extrusion in the kidney and contribute to renal
CC acidification. {ECO:0000250, ECO:0000269|PubMed:11976689}.
CC -!- ACTIVITY REGULATION: Inhibited by WNK3. {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC cotransporters. {ECO:0000305|PubMed:11551954}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23376777};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23376777}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WVL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVL3-2; Sequence=VSP_027770;
CC -!- TISSUE SPECIFICITY: Detected in proximal tubules in the kidney, in
CC particular in basolateral membranes of intercalated cells in the
CC cortical collecting duct.
CC -!- DEVELOPMENTAL STAGE: In 8 day old mice, before the onset of hearing,
CC detected in membranes of the stria vascularis and in most cells of the
CC organ of Corti. At P14, when the organ of Corti has matured, expression
CC is no longer detected in hair cells and the stria, but is restricted to
CC Deiters' cells that are supporting outer hair cells and to phalangeal
CC cells enveloping the inner hair cells.
CC -!- PTM: Glycosylation at Asn-331 and Asn-344 is required for proper
CC trafficking to the cell surface, and augments protein stability.
CC {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770,
CC ECO:0000269|PubMed:23376777}.
CC -!- DISEASE: Note=Defects in Slc12a7 are a cause of deafness due to the
CC progressive degeneration of outer and inner hair cells in the cochlea
CC and of neurons in the cochlear ganglion, leading to the loss of the
CC organ of Corti. {ECO:0000269|PubMed:11976689}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21379.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE42491.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF087436; AAD38328.1; -; mRNA.
DR EMBL; AK131129; BAD21379.1; ALT_INIT; mRNA.
DR EMBL; AK149750; BAE29061.1; -; mRNA.
DR EMBL; AK169950; BAE41477.1; -; mRNA.
DR EMBL; AK171498; BAE42491.1; ALT_FRAME; mRNA.
DR CCDS; CCDS26635.1; -. [Q9WVL3-1]
DR RefSeq; NP_035520.1; NM_011390.2. [Q9WVL3-1]
DR PDB; 6UKN; EM; 3.65 A; A=1-1083.
DR PDBsum; 6UKN; -.
DR AlphaFoldDB; Q9WVL3; -.
DR SMR; Q9WVL3; -.
DR BioGRID; 203280; 2.
DR STRING; 10090.ENSMUSP00000017900; -.
DR GlyGen; Q9WVL3; 4 sites.
DR iPTMnet; Q9WVL3; -.
DR PhosphoSitePlus; Q9WVL3; -.
DR EPD; Q9WVL3; -.
DR jPOST; Q9WVL3; -.
DR MaxQB; Q9WVL3; -.
DR PaxDb; Q9WVL3; -.
DR PeptideAtlas; Q9WVL3; -.
DR PRIDE; Q9WVL3; -.
DR ProteomicsDB; 255439; -. [Q9WVL3-1]
DR ProteomicsDB; 255440; -. [Q9WVL3-2]
DR Antibodypedia; 22300; 235 antibodies from 30 providers.
DR DNASU; 20499; -.
DR Ensembl; ENSMUST00000017900; ENSMUSP00000017900; ENSMUSG00000017756. [Q9WVL3-1]
DR GeneID; 20499; -.
DR KEGG; mmu:20499; -.
DR UCSC; uc007reb.1; mouse. [Q9WVL3-2]
DR UCSC; uc007rec.1; mouse. [Q9WVL3-1]
DR CTD; 10723; -.
DR MGI; MGI:1342283; Slc12a7.
DR VEuPathDB; HostDB:ENSMUSG00000017756; -.
DR eggNOG; KOG2082; Eukaryota.
DR GeneTree; ENSGT00940000157657; -.
DR HOGENOM; CLU_001883_1_2_1; -.
DR InParanoid; Q9WVL3; -.
DR OMA; ADNPFSW; -.
DR OrthoDB; 349744at2759; -.
DR PhylomeDB; Q9WVL3; -.
DR TreeFam; TF313657; -.
DR Reactome; R-MMU-426117; Cation-coupled Chloride cotransporters.
DR BioGRID-ORCS; 20499; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Slc12a7; mouse.
DR PRO; PR:Q9WVL3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9WVL3; protein.
DR Bgee; ENSMUSG00000017756; Expressed in vestibular membrane of cochlear duct and 217 other tissues.
DR ExpressionAtlas; Q9WVL3; baseline and differential.
DR Genevisible; Q9WVL3; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA: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:0140157; P:ammonium import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0006884; P:cell volume homeostasis; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR030354; KCC4.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF47; PTHR11827:SF47; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 2.
DR PRINTS; PR01081; KCLTRNSPORT.
DR TIGRFAMs; TIGR00930; 2a30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Chloride; Deafness;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1083
FT /note="Solute carrier family 12 member 7"
FT /id="PRO_0000178040"
FT TOPO_DOM 1..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..1083
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y666"
FT MOD_RES 973
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 980
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:23376777"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23376777"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:23376777"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:23376777"
FT VAR_SEQ 1010..1080
FT /note="DQSNVRRMHTAVKLNGVVLNKSQDAQLVLLNMPGPPKSRQGDENYMEFLEVL
FT TEGLNRVLLVRGGGREVIT -> LLHFMLFENRCWTKHTVIVPFPWSEFRVPVMKGLTG
FT ATETHL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027770"
FT CONFLICT 40
FT /note="T -> M (in Ref. 3; BAE41477)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="Y -> F (in Ref. 3; BAE41477)"
FT /evidence="ECO:0000305"
FT CONFLICT 951
FT /note="Q -> P (in Ref. 3; BAE29061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1083 AA; 119481 MW; E339D43F7D3B6BD7 CRC64;
MPTNFTVVPV EARADGAGDE AAERTEEPES PESVDQTSPT PGDGNPRENS PFINNVEVER
ESYFEGKNMA LFEEEMDSNP MVSSLLNKLA NYTNLSQGVV EHEEDEDSRR REVKAPRMGT
FIGVYLPCLQ NILGVILFLR LTWIVGAAGV MESFLIVAMC CTCTMLTAIS MSAIATNGVV
PAGGSYYMIS RSLGPEFGGA VGLCFYLGTT FAGAMYILGT IEIFLTYISP SAAIFQAETA
DGEAAALLNN MRVYGSCALA LMAVVVFVGV KYVNKLALVF LACVVLSILA IYAGVIKTAF
APPDIPVCLL GNRTLANRNF DTCAKMQVVS NGTVTTALWR LFCNGSSLGA TCDEYFAQNN
VTEIQGIPGV ASGVFLDNLW STYSDKGAFV EKKGVSSVPV SEESRPGGLP YVLTDIMTYF
TMLVGIYFPS VTGIMAGSNR SGDLKDAQKS IPTGTILAIV TTSFIYLSCI VLFGACIEGV
VLRDKFGEAL QGNLVIGMLA WPSPWVIVIG SFFSTCGAGL QSLTGAPRLL QAIARDGIIP
FLQVFGHGKA NGEPTWALLL TALICETGIL IASLDSVAPI LSMFFLMCYM FVNLACAVQT
LLRTPNWRPR FKFYHWTLSF LGMSLCLALM FICSWYYALF AMLIAGCIYK YIEYRGAEKE
WGDGIRGLSL NAARYALLRV EHGPPHTKNW RPQVLVMLNL DSEQCVKHPR LLSFTSQLKA
GKGLTIVGSV LEGTYLDKHV EAQRAEENIR SLMSAEKTKG FCQLVVSSNL RDGASHLIQS
AGLGGMKHNT VLMAWPEAWK EADNPFSWKN FVDTVRDTTA AHQALLVAKN IDLFPQNQER
FSDGNIDVWW IVHDGGMLML LPFLLRQHKV WRKCRMRIFT VAQVDDNSIQ MKKDLQMFLY
HLRISAEVEV VEMVENDISA FTYEKTLMME QRSQMLKQMQ LSKNEREREA QLIHDRNTAS
HTTATARTQA PPTPDKVQMT WTKEKLIAEK HRNKDTGPSG FKDLFSLKPD QSNVRRMHTA
VKLNGVVLNK SQDAQLVLLN MPGPPKSRQG DENYMEFLEV LTEGLNRVLL VRGGGREVIT
IYS
