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   27-MAR-2024, entry version 187.
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,
GN   ECO:0000312|HGNC:HGNC:10975};
GN   Synonyms=KIAA0702 {ECO:0000303|PubMed:9734811}, NCKX1
GN   {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.
DR   RefSeq; XP_011520521.1; XM_011522219.1. [O60721-1]
DR   RefSeq; XP_011520522.1; XM_011522220.2.
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   GlyCosmos; O60721; 1 site, No reported glycans.
DR   GlyGen; O60721; 1 site.
DR   iPTMnet; O60721; -.
DR   PhosphoSitePlus; O60721; -.
DR   BioMuta; SLC24A1; -.
DR   MassIVE; O60721; -.
DR   MaxQB; O60721; -.
DR   PaxDb; 9606-ENSP00000261892; -.
DR   PeptideAtlas; O60721; -.
DR   ProteomicsDB; 49569; -. [O60721-1]
DR   ProteomicsDB; 49570; -. [O60721-2]
DR   ProteomicsDB; 61158; -.
DR   Antibodypedia; 26029; 147 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   AGR; HGNC:10975; -.
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; HNSTIRT; -.
DR   OrthoDB; 22570at2759; -.
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; 11 hits in 1152 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 145 other cell types or tissues.
DR   ExpressionAtlas; O60721; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
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:intracellular calcium ion homeostasis; IDA:ARUK-UCL.
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:0006811; P:monoatomic ion transport; TAS:Reactome.
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; NCX, central ion-binding region; 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   NCBIfam; TIGR00927; 2A1904; 1.
DR   NCBIfam; TIGR00367; calcium/sodium antiporter; 1.
DR   PANTHER; PTHR10846; SODIUM/POTASSIUM/CALCIUM EXCHANGER; 1.
DR   PANTHER; PTHR10846:SF36; SODIUM_POTASSIUM_CALCIUM EXCHANGER 1; 1.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   Genevisible; O60721; HS.
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
//