NCKX1_HUMAN
ID NCKX1_HUMAN Reviewed; 1099 AA.
AC O60721; O43485; O75184; Q17RM9;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Sodium/potassium/calcium exchanger 1;
DE AltName: Full=Na(+)/K(+)/Ca(2+)-exchange protein 1 {ECO:0000303|PubMed:9856482};
DE AltName: Full=Retinal rod Na-Ca+K exchanger {ECO:0000303|PubMed:9478004};
DE AltName: Full=Solute carrier family 24 member 1;
GN Name=SLC24A1 {ECO:0000303|PubMed:20850105, ECO:0000312|HGNC:HGNC:10975};
GN Synonyms=KIAA0702 {ECO:0000303|PubMed:9734811},
GN NCKX1 {ECO:0000303|PubMed:9856482};
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] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=9856482; DOI=10.1007/s004390050842;
RA Tucker J.E., Winkfein R.J., Murthy S.K., Friedman J.S., Walter M.A.,
RA Demetrick D.J., Schnetkamp P.P.M.;
RT "Chromosomal localization and genomic organization of the human retinal rod
RT Na-Ca+K exchanger.";
RL Hum. Genet. 103:411-414(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=9478004;
RA Tucker J.E., Winkfein R.J., Cooper C.B., Schnetkamp P.P.M.;
RT "cDNA cloning of the human retinal rod Na-Ca + K exchanger: comparison with
RT a revised bovine sequence.";
RL Invest. Ophthalmol. Vis. Sci. 39:435-440(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Heart, and 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1003 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [6]
RP FUNCTION OF THE N-TERMINUS IN TARGETING.
RX PubMed=10608890; DOI=10.1074/jbc.274.53.38177;
RA McKiernan C.J., Friedlander M.;
RT "The retinal rod Na(+)/Ca(2+),K(+) exchanger contains a noncleaved signal
RT sequence required for translocation of the N-terminus.";
RL J. Biol. Chem. 274:38177-38182(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-724, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN CSNB1D.
RX PubMed=20850105; DOI=10.1016/j.ajhg.2010.08.013;
RA Riazuddin S.A., Shahzadi A., Zeitz C., Ahmed Z.M., Ayyagari R.,
RA Chavali V.R., Ponferrada V.G., Audo I., Michiels C., Lancelot M.E.,
RA Nasir I.A., Zafar A.U., Khan S.N., Husnain T., Jiao X., MacDonald I.M.,
RA Riazuddin S., Sieving P.A., Katsanis N., Hejtmancik J.F.;
RT "A mutation in SLC24A1 implicated in autosomal-recessive congenital
RT stationary night blindness.";
RL Am. J. Hum. Genet. 87:523-531(2010).
RN [9]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=26631410; DOI=10.1016/j.ceca.2015.11.001;
RA Jalloul A.H., Szerencsei R.T., Schnetkamp P.P.;
RT "Cation dependencies and turnover rates of the human K(+)-dependent Na(+)-
RT Ca(2+) exchangers NCKX1, NCKX2, NCKX3 and NCKX4.";
RL Cell Calcium 59:1-11(2016).
CC -!- FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+)
CC and 1 K(+) in exchange for 4 Na(+) (PubMed:26631410). Critical
CC component of the visual transduction cascade, controlling the calcium
CC concentration of outer segments during light and darkness
CC (PubMed:20850105). Light causes a rapid lowering of cytosolic free
CC calcium in the outer segment of both retinal rod and cone
CC photoreceptors and the light-induced lowering of calcium is caused by
CC extrusion via this protein which plays a key role in the process of
CC light adaptation (PubMed:20850105). {ECO:0000269|PubMed:20850105,
CC ECO:0000269|PubMed:26631410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in)
CC + 4 Na(+)(out); Xref=Rhea:RHEA:69967, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:26631410};
CC -!- INTERACTION:
CC O60721; P16333: NCK1; NbExp=3; IntAct=EBI-1753504, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26631410};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O60721-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60721-2; Sequence=VSP_006160;
CC Name=3;
CC IsoId=O60721-3; Sequence=VSP_054491;
CC -!- TISSUE SPECIFICITY: Expressed in the retina, particularly in the inner
CC segment, outer and inner nuclear layers, and ganglion cell layer.
CC {ECO:0000269|PubMed:20850105}.
CC -!- PTM: The uncleaved signal sequence is required for efficient membrane
CC targeting and proper membrane integration.
CC {ECO:0000269|PubMed:10608890}.
CC -!- DISEASE: Night blindness, congenital stationary, 1D (CSNB1D)
CC [MIM:613830]: An autosomal recessive form of congenital stationary
CC night blindness, a non-progressive retinal disorder characterized by
CC impaired night vision. CSNB1D is characterized by a Riggs type of
CC electroretinogram (proportionally reduced a- and b-waves). Patients
CC have visual acuity within the normal range and no symptoms of myopia
CC and/or nystagmus. {ECO:0000269|PubMed:20850105}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC24A subfamily. {ECO:0000305}.
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DR EMBL; AF062921; AAC16732.1; -; mRNA.
DR EMBL; AF062922; AAC77912.1; -; mRNA.
DR EMBL; AF026132; AAB97832.1; -; mRNA.
DR EMBL; AC011939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117263; AAI17264.1; -; mRNA.
DR EMBL; BC143375; AAI43376.1; -; mRNA.
DR EMBL; AB014602; BAA31677.2; ALT_SEQ; mRNA.
DR CCDS; CCDS45284.1; -. [O60721-1]
DR CCDS; CCDS73742.1; -. [O60721-3]
DR CCDS; CCDS73743.1; -. [O60721-2]
DR RefSeq; NP_001287960.1; NM_001301031.1. [O60721-3]
DR RefSeq; NP_001287961.1; NM_001301032.1. [O60721-2]
DR RefSeq; NP_001287962.1; NM_001301033.1.
DR RefSeq; NP_004718.1; NM_004727.2. [O60721-1]
DR RefSeq; XP_005254835.1; XM_005254778.3. [O60721-1]
DR RefSeq; XP_011520521.1; XM_011522219.1. [O60721-1]
DR RefSeq; XP_011520522.1; XM_011522220.2. [O60721-2]
DR RefSeq; XP_011520523.1; XM_011522221.2. [O60721-3]
DR AlphaFoldDB; O60721; -.
DR BioGRID; 114624; 3.
DR IntAct; O60721; 5.
DR STRING; 9606.ENSP00000261892; -.
DR TCDB; 2.A.19.4.9; the ca(2+):cation antiporter (caca) family.
DR GlyGen; O60721; 1 site.
DR iPTMnet; O60721; -.
DR PhosphoSitePlus; O60721; -.
DR BioMuta; SLC24A1; -.
DR MassIVE; O60721; -.
DR MaxQB; O60721; -.
DR PaxDb; O60721; -.
DR PeptideAtlas; O60721; -.
DR PRIDE; O60721; -.
DR ProteomicsDB; 49569; -. [O60721-1]
DR ProteomicsDB; 49570; -. [O60721-2]
DR ProteomicsDB; 61158; -.
DR Antibodypedia; 26029; 133 antibodies from 23 providers.
DR DNASU; 9187; -.
DR Ensembl; ENST00000261892.11; ENSP00000261892.6; ENSG00000074621.14. [O60721-1]
DR Ensembl; ENST00000339868.10; ENSP00000341837.7; ENSG00000074621.14. [O60721-3]
DR Ensembl; ENST00000399033.8; ENSP00000381991.4; ENSG00000074621.14. [O60721-3]
DR Ensembl; ENST00000546330.1; ENSP00000439190.1; ENSG00000074621.14. [O60721-2]
DR GeneID; 9187; -.
DR KEGG; hsa:9187; -.
DR MANE-Select; ENST00000261892.11; ENSP00000261892.6; NM_004727.3; NP_004718.1.
DR UCSC; uc010ujf.2; human. [O60721-1]
DR CTD; 9187; -.
DR DisGeNET; 9187; -.
DR GeneCards; SLC24A1; -.
DR HGNC; HGNC:10975; SLC24A1.
DR HPA; ENSG00000074621; Tissue enriched (retina).
DR MalaCards; SLC24A1; -.
DR MIM; 603617; gene.
DR MIM; 613830; phenotype.
DR neXtProt; NX_O60721; -.
DR OpenTargets; ENSG00000074621; -.
DR Orphanet; 215; Congenital stationary night blindness.
DR PharmGKB; PA35851; -.
DR VEuPathDB; HostDB:ENSG00000074621; -.
DR eggNOG; KOG1307; Eukaryota.
DR GeneTree; ENSGT01030000234532; -.
DR InParanoid; O60721; -.
DR OMA; WPESRQK; -.
DR OrthoDB; 1168500at2759; -.
DR PhylomeDB; O60721; -.
DR TreeFam; TF318759; -.
DR PathwayCommons; O60721; -.
DR Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-HSA-425561; Sodium/Calcium exchangers.
DR Reactome; R-HSA-5619077; Defective SLC24A1 causes congenital stationary night blindness 1D (CSNB1D).
DR SignaLink; O60721; -.
DR SIGNOR; O60721; -.
DR BioGRID-ORCS; 9187; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; SLC24A1; human.
DR GenomeRNAi; 9187; -.
DR Pharos; O60721; Tbio.
DR PRO; PR:O60721; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O60721; protein.
DR Bgee; ENSG00000074621; Expressed in endothelial cell and 144 other tissues.
DR ExpressionAtlas; O60721; baseline and differential.
DR Genevisible; O60721; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0019867; C:outer membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0008273; F:calcium, potassium:sodium antiporter activity; IDA:ARUK-UCL.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0006816; P:calcium ion transport; NAS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:ARUK-UCL.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0060292; P:long-term synaptic depression; IBA:GO_Central.
DR GO; GO:0060291; P:long-term synaptic potentiation; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0009642; P:response to light intensity; NAS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0007601; P:visual perception; NAS:UniProtKB.
DR Gene3D; 1.20.1420.30; -; 2.
DR InterPro; IPR004481; K/Na/Ca-exchanger.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR InterPro; IPR004817; SLC24A1.
DR PANTHER; PTHR10846; PTHR10846; 2.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR TIGRFAMs; TIGR00927; 2A1904; 1.
DR TIGRFAMs; TIGR00367; TIGR00367; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Calcium; Calcium transport; Cell membrane;
KW Congenital stationary night blindness; Glycoprotein; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Sensory transduction;
KW Signal; Symport; Transmembrane; Transmembrane helix; Transport; Vision.
FT CHAIN 1..1099
FT /note="Sodium/potassium/calcium exchanger 1"
FT /id="PRO_0000223303"
FT SIGNAL 1..?
FT /note="Not cleaved"
FT /evidence="ECO:0000269|PubMed:10608890"
FT TOPO_DOM 1..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 908..928
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 929..935
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 957..971
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 993..1010
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1011..1031
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1032..1039
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1061..1068
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1069..1089
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1090..1099
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 494..534
FT /note="Alpha-1"
FT REPEAT 979..1010
FT /note="Alpha-2"
FT REGION 123..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..814
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..894
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 724
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 631..648
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9478004,
FT ECO:0000303|PubMed:9734811"
FT /id="VSP_006160"
FT VAR_SEQ 932..961
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054491"
FT VARIANT 37
FT /note="T -> S (in dbSNP:rs3743171)"
FT /id="VAR_050221"
FT VARIANT 311
FT /note="V -> L (in dbSNP:rs34363823)"
FT /id="VAR_050222"
FT VARIANT 313
FT /note="L -> V (in dbSNP:rs35571449)"
FT /id="VAR_050223"
FT CONFLICT 516
FT /note="V -> I (in Ref. 2; AAB97832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1099 AA; 121374 MW; 3911856BB088B5FD CRC64;
MGKLIRMGPQ ERWLLRTKRL HWSRLLFLLG MLIIGSTYQH LRRPRGLSSL WAAVSSHQPI
KLASRDLSSE EMMMMSSSPS KPSSEMGGKM LVPQASVGSD EATLSMTVEN IPSMPKRTAK
MIPTTTKNNY SPTAAGTERR KEDTPTSSRT LTYYTSTSSR QIVKKYTPTP RGEMKSYSPT
QVREKVKYTP SPRGRRVGTY VPSTFMTMET SHAITPRTTV KDSDITATYK ILETNSLKRI
MEETTPTTLK GMFDSTPTFL THEVEANVLT SPRSVMEKNN LFPPRRVESN SSAHPWGLVG
KSNPKTPQGT VLLHTPATSE GQVTISTMTG SSPAETKAFT AAWSLRNPSP RTSVSAIKTA
PAIVWRLAKK PSTAPSTSTT PTVRAKLTMQ VHHCVVVKPT PAMLTTPSPS LTTALLPEEL
SPSPSVLPPS LPDLHPKGEY PPDLFSVEER RQGWVVLHVF GMMYVFVALA IVCDEYFVPA
LGVITDKLQI SEDVAGATFM AAGGSAPELF TSLIGVFISH SNVGIGTIVG SAVFNILFVI
GTCSLFSREI LNLTWWPLFR DVSFYILDLI MLILFFLDSL IAWWESLLLL LAYAFYVFTM
KWNKHIEVWV KEQLSRRPVA KVMALEDLSK PGDGAIAVDE LQDNKKLKLP SLLTRGSSST
SLHNSTIRST IYQLMLHSLD PLREVRLAKE KEEESLNQGA RAQPQAKAES KPEEEEPAKL
PAVTVTPAPV PDIKGDQKEN PGGQEDVAEA ESTGEMPGEE GETAGEGETE EKSGGETQPE
GEGETETQGK GEECEDENEA EGKGDNEGED EGEIHAEDGE MKGNEGETES QELSAENHGE
AKNDEKGVED GGGSDGGDSE EEEEEEEEQE EEEEEEEQEE EEEEEEEEEE KGNEEPLSLD
WPETRQKQAI YLFLLPIVFP LWLTVPDVRR QESRKFFVFT FLGSIMWIAM FSYLMVWWAH
QVGETIGISE EIMGLTILAA GTSIPDLITS VIVARKGLGD MAVSSSVGSN IFDITVGLPV
PWLLFSLING LQPVPVSSNG LFCAIVLLFL MLLFVISSIA SCKWRMNKIL GFTMFLLYFV
FLIISVMLED RIISCPVSV
