KCNT2_HUMAN
ID KCNT2_HUMAN Reviewed; 1135 AA.
AC Q6UVM3; Q3SY59; Q5VTN1; Q6ZMT3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Potassium channel subfamily T member 2;
DE AltName: Full=Sequence like an intermediate conductance potassium channel subunit;
DE AltName: Full=Sodium and chloride-activated ATP-sensitive potassium channel Slo2.1;
GN Name=KCNT2; Synonyms=SLICK;
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), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14684870; DOI=10.1523/jneurosci.23-37-11681.2003;
RA Bhattacharjee A., Joiner W.J., Wu M., Yang Y., Sigworth F.J.,
RA Kaczmarek L.K.;
RT "Slick (Slo2.1), a rapidly-gating sodium-activated potassium channel
RT inhibited by ATP.";
RL J. Neurosci. 23:11681-11691(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adipose tissue;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
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]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=16687497; DOI=10.1523/jneurosci.3372-05.2006;
RA Santi C.M., Ferreira G., Yang B., Gazula V.R., Butler A., Wei A.,
RA Kaczmarek L.K., Salkoff L.;
RT "Opposite regulation of Slick and Slack K+ channels by neuromodulators.";
RL J. Neurosci. 26:5059-5068(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN DEE57, VARIANT DEE57
RP LEU-240, AND CHARACTERIZATION OF VARIANT DEE57 LEU-240.
RX PubMed=29069600; DOI=10.1016/j.celrep.2017.09.088;
RA Gururaj S., Palmer E.E., Sheehan G.D., Kandula T., Macintosh R., Ying K.,
RA Morris P., Tao J., Dias K.R., Zhu Y., Dinger M.E., Cowley M.J., Kirk E.P.,
RA Roscioli T., Sachdev R., Duffey M.E., Bye A., Bhattacharjee A.;
RT "A De Novo Mutation in the Sodium-Activated Potassium Channel KCNT2 Alters
RT Ion Selectivity and Causes Epileptic Encephalopathy.";
RL Cell Rep. 21:926-933(2017).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-33.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Outward rectifying potassium channel. Produces rapidly
CC activating outward rectifier K(+) currents. Activated by high
CC intracellular sodium and chloride levels (PubMed:14684870,
CC PubMed:16687497, PubMed:29069600). Channel activity is inhibited by ATP
CC and by inhalation anesthetics, such as isoflurane (PubMed:16687497) (By
CC similarity). Inhibited upon stimulation of G-protein coupled receptors,
CC such as CHRM1 and GRM1 (PubMed:16687497).
CC {ECO:0000250|UniProtKB:Q6UVM4, ECO:0000269|PubMed:14684870,
CC ECO:0000269|PubMed:16687497, ECO:0000269|PubMed:29069600}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29069600};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6UVM3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UVM3-2; Sequence=VSP_029855;
CC Name=3;
CC IsoId=Q6UVM3-3; Sequence=VSP_029854, VSP_029855, VSP_029856;
CC Name=4;
CC IsoId=Q6UVM3-4; Sequence=VSP_029852, VSP_029853, VSP_029855,
CC VSP_029856, VSP_029857;
CC -!- PTM: Phosphorylated by protein kinase C. Phosphorylation of the C-
CC terminal domain inhibits channel activity.
CC {ECO:0000269|PubMed:16687497}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 57 (DEE57)
CC [MIM:617771]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE57 is an autosomal dominant condition.
CC {ECO:0000269|PubMed:29069600}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. KCa4.2/KCNT2 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY359444; AAR06170.1; -; mRNA.
DR EMBL; AK131498; BAD18642.1; -; mRNA.
DR EMBL; BX647852; CAI46099.1; -; mRNA.
DR EMBL; AL138931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC103948; AAI03949.1; -; mRNA.
DR EMBL; BC103949; AAI03950.1; -; mRNA.
DR EMBL; BC103950; AAI03951.1; -; mRNA.
DR CCDS; CCDS1384.1; -. [Q6UVM3-1]
DR CCDS; CCDS72994.1; -. [Q6UVM3-3]
DR CCDS; CCDS72995.1; -. [Q6UVM3-2]
DR RefSeq; NP_001274748.1; NM_001287819.1. [Q6UVM3-2]
DR RefSeq; NP_001274749.1; NM_001287820.1. [Q6UVM3-3]
DR RefSeq; NP_940905.2; NM_198503.3. [Q6UVM3-1]
DR AlphaFoldDB; Q6UVM3; -.
DR SMR; Q6UVM3; -.
DR BioGRID; 131252; 32.
DR IntAct; Q6UVM3; 9.
DR STRING; 9606.ENSP00000294725; -.
DR BindingDB; Q6UVM3; -.
DR ChEMBL; CHEMBL4739693; -.
DR DrugCentral; Q6UVM3; -.
DR GuidetoPHARMACOLOGY; 386; -.
DR TCDB; 1.A.1.3.6; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q6UVM3; 1 site.
DR iPTMnet; Q6UVM3; -.
DR PhosphoSitePlus; Q6UVM3; -.
DR BioMuta; KCNT2; -.
DR DMDM; 74749370; -.
DR jPOST; Q6UVM3; -.
DR MassIVE; Q6UVM3; -.
DR PaxDb; Q6UVM3; -.
DR PeptideAtlas; Q6UVM3; -.
DR PRIDE; Q6UVM3; -.
DR ProteomicsDB; 67432; -. [Q6UVM3-1]
DR ProteomicsDB; 67433; -. [Q6UVM3-2]
DR ProteomicsDB; 67434; -. [Q6UVM3-3]
DR ProteomicsDB; 67435; -. [Q6UVM3-4]
DR Antibodypedia; 34469; 199 antibodies from 22 providers.
DR DNASU; 343450; -.
DR Ensembl; ENST00000294725.14; ENSP00000294725.8; ENSG00000162687.19. [Q6UVM3-1]
DR Ensembl; ENST00000367433.9; ENSP00000356403.5; ENSG00000162687.19. [Q6UVM3-2]
DR Ensembl; ENST00000609185.5; ENSP00000476657.1; ENSG00000162687.19. [Q6UVM3-3]
DR GeneID; 343450; -.
DR KEGG; hsa:343450; -.
DR MANE-Select; ENST00000294725.14; ENSP00000294725.8; NM_198503.5; NP_940905.2.
DR UCSC; uc001gtd.3; human. [Q6UVM3-1]
DR CTD; 343450; -.
DR DisGeNET; 343450; -.
DR GeneCards; KCNT2; -.
DR HGNC; HGNC:18866; KCNT2.
DR HPA; ENSG00000162687; Tissue enhanced (ovary).
DR MalaCards; KCNT2; -.
DR MIM; 610044; gene.
DR MIM; 617771; phenotype.
DR neXtProt; NX_Q6UVM3; -.
DR OpenTargets; ENSG00000162687; -.
DR PharmGKB; PA38726; -.
DR VEuPathDB; HostDB:ENSG00000162687; -.
DR eggNOG; KOG3193; Eukaryota.
DR GeneTree; ENSGT00940000158746; -.
DR HOGENOM; CLU_003370_0_0_1; -.
DR InParanoid; Q6UVM3; -.
DR OMA; QATYYVV; -.
DR OrthoDB; 858812at2759; -.
DR PhylomeDB; Q6UVM3; -.
DR TreeFam; TF314283; -.
DR PathwayCommons; Q6UVM3; -.
DR SignaLink; Q6UVM3; -.
DR BioGRID-ORCS; 343450; 9 hits in 1063 CRISPR screens.
DR ChiTaRS; KCNT2; human.
DR GeneWiki; KCNT2; -.
DR GenomeRNAi; 343450; -.
DR Pharos; Q6UVM3; Tchem.
DR PRO; PR:Q6UVM3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6UVM3; protein.
DR Bgee; ENSG00000162687; Expressed in parietal pleura and 143 other tissues.
DR ExpressionAtlas; Q6UVM3; baseline and differential.
DR Genevisible; Q6UVM3; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070089; F:chloride-activated potassium channel activity; IMP:UniProtKB.
DR GO; GO:0005228; F:intracellular sodium activated potassium channel activity; IBA:GO_Central.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IMP:UniProtKB.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Disease variant;
KW Epilepsy; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Nucleotide-binding; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1135
FT /note="Potassium channel subfamily T member 2"
FT /id="PRO_0000312503"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 229..249
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..1135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 422..543
FT /note="RCK N-terminal"
FT REGION 977..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1025..1032
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 129..153
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029852"
FT VAR_SEQ 468
FT /note="Q -> QCVCLCCR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029853"
FT VAR_SEQ 469..518
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_029854"
FT VAR_SEQ 760..783
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_029855"
FT VAR_SEQ 970
FT /note="E -> ESRKIASQ (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029856"
FT VAR_SEQ 1071..1135
FT /note="DEMNDHQSTLSYILINPSPDTRIELNDVVYLIRPDPLAYLPNSEPSRRNSIC
FT NVTGQDSREETQL -> GMLFKNYCIYGLVISCH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029857"
FT VARIANT 33
FT /note="V -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037527"
FT VARIANT 240
FT /note="F -> L (in DEE57; decreased protein abundance; loss
FT of chloride-activated potassium channel activity; loss of
FT potassium selectivity; dbSNP:rs1060499537)"
FT /evidence="ECO:0000269|PubMed:29069600"
FT /id="VAR_080867"
FT VARIANT 413
FT /note="C -> W (in dbSNP:rs12738104)"
FT /id="VAR_037528"
FT VARIANT 429
FT /note="K -> N (in dbSNP:rs12742082)"
FT /id="VAR_037529"
SQ SEQUENCE 1135 AA; 130501 MW; 4957C6DAB1E030CF CRC64;
MVDLESEVPP LPPRYRFRDL LLGDQGWQND DRVQVEFYMN ENTFKERLKL FFIKNQRSSL
RIRLFNFSLK LLSCLLYIIR VLLENPSQGN EWSHIFWVNR SLPLWGLQVS VALISLFETI
LLGYLSYKGN IWEQILRIPF ILEIINAVPF IISIFWPSLR NLFVPVFLNC WLAKHALENM
INDLHRAIQR TQSAMFNQVL ILISTLLCLI FTCICGIQHL ERIGKKLNLF DSLYFCIVTF
STVGFGDVTP ETWSSKLFVV AMICVALVVL PIQFEQLAYL WMERQKSGGN YSRHRAQTEK
HVVLCVSSLK IDLLMDFLNE FYAHPRLQDY YVVILCPTEM DVQVRRVLQI PMWSQRVIYL
QGSALKDQDL LRAKMDDAEA CFILSSRCEV DRTSSDHQTI LRAWAVKDFA PNCPLYVQIL
KPENKFHIKF ADHVVCEEEF KYAMLALNCI CPATSTLITL LVHTSRGQEG QQSPEQWQKM
YGRCSGNEVY HIVLEESTFF AEYEGKSFTY ASFHAHKKFG VCLIGVRRED NKNILLNPGP
RYIMNSTDIC FYINITKEEN SAFKNQDQQR KSNVSRSFYH GPSRLPVHSI IASMGTVAID
LQDTSCRSAS GPTLSLPTEG SKEIRRPSIA PVLEVADTSS IQTCDLLSDQ SEDETTPDEE
MSSNLEYAKG YPPYSPYIGS SPTFCHLLHE KVPFCCLRLD KSCQHNYYED AKAYGFKNKL
IIVAAETAGN GLYNFIVPLR AYYRPKKELN PIVLLLDNPP DMHFLDAICW FPMVYYMVGS
IDNLDDLLRC GVTFAANMVV VDKESTMSAE EDYMADAKTI VNVQTLFRLF SSLSIITELT
HPANMRFMQF RAKDCYSLAL SKLEKKERER GSNLAFMFRL PFAAGRVFSI SMLDTLLYQS
FVKDYMISIT RLLLGLDTTP GSGFLCSMKI TADDLWIRTY ARLYQKLCSS TGDVPIGIYR
TESQKLTTSE SQISISVEEW EDTKDSKEQG HHRSNHRNST SSDQSDHPLL RRKSMQWARR
LSRKGPKHSG KTAEKITQQR LNLYRRSERQ ELAELVKNRM KHLGLSTVGY DEMNDHQSTL
SYILINPSPD TRIELNDVVY LIRPDPLAYL PNSEPSRRNS ICNVTGQDSR EETQL
