ID   KCNA4_MOUSE             Reviewed;         654 AA.
AC   Q61423; Q8CBF8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 4;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.4;
GN   Name=Kcna4;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=AKR/J;
RX   PubMed=8020965; DOI=10.1006/geno.1994.1153;
RA   Wymore R.S., Korenberg J.R., Kinoshita K.D., Aiyar J., Coyne C., Chen X.N.,
RA   Hustad C.M., Copeland N.G., Gutman G.A., Jenkins N.A., Chandy K.G.;
RT   "Genomic organization, nucleotide sequence, biophysical properties, and
RT   localization of the voltage-gated K+ channel gene KCNA4/Kv1.4 to mouse
RT   chromosome 2/human 11p14 and mapping of KCNC1/Kv3.1 to mouse 7/human
RT   11p14.3-p15.2 and KCNA1/Kv1.1 to human 12p13.";
RL   Genomics 20:191-202(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=27582084; DOI=10.1136/jmedgenet-2015-103637;
RA   Kaya N., Alsagob M., D'Adamo M.C., Al-Bakheet A., Hasan S., Muccioli M.,
RA   Almutairi F.B., Almass R., Aldosary M., Monies D., Mustafa O.M.,
RA   Alyounes B., Kenana R., Al-Zahrani J., Naim E., Binhumaid F.S., Qari A.,
RA   Almutairi F., Meyer B., Plageman T.F., Pessia M., Colak D., Al-Owain M.;
RT   "KCNA4 deficiency leads to a syndrome of abnormal striatum, congenital
RT   cataract and intellectual disability.";
RL   J. Med. Genet. 53:786-792(2016).
CC   -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC       potassium transport in excitable membranes. Forms tetrameric potassium-
CC       selective channels through which potassium ions pass in accordance with
CC       their electrochemical gradient. The channel alternates between opened
CC       and closed conformations in response to the voltage difference across
CC       the membrane (PubMed:8020965). Can form functional homotetrameric
CC       channels and heterotetrameric channels that contain variable
CC       proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family
CC       members as well; channel properties depend on the type of alpha
CC       subunits that are part of the channel (By similarity). Channel
CC       properties are modulated by cytoplasmic beta subunits that regulate the
CC       subcellular location of the alpha subunits and promote rapid
CC       inactivation. In vivo, membranes probably contain a mixture of
CC       heteromeric potassium channel complexes, making it difficult to assign
CC       currents observed in intact tissues to any particular potassium channel
CC       family member. Homotetrameric KCNA4 forms a potassium channel that
CC       opens in response to membrane depolarization, followed by rapid
CC       spontaneous channel closure (PubMed:8020965). Likewise, a
CC       heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid
CC       inactivation (By similarity). {ECO:0000250|UniProtKB:P15385,
CC       ECO:0000269|PubMed:8020965}.
CC   -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins
CC       (By similarity). Interacts with KCNAB1 and KCNAB2 (By similarity).
CC       Binds PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts
CC       with SIGMAR1 (By similarity). Detected in a complex with KCNA1 (By
CC       similarity). Interacts with KCNA2 (By similarity). Part of a complex
CC       containing KCNA1, KCNAB1 and LGI1 (By similarity). Interacts (via
CC       cytoplasmic N-terminal domain) with KCNRG (By similarity).
CC       {ECO:0000250|UniProtKB:P15385, ECO:0000250|UniProtKB:P22459}.
CC   -!- INTERACTION:
CC       Q61423; Q62108: Dlg4; NbExp=3; IntAct=EBI-2309633, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8020965};
CC       Multi-pass membrane protein {ECO:0000255}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:P15385}.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, lens and retina.
CC       {ECO:0000269|PubMed:27582084}.
CC   -!- DOMAIN: The N-terminus may be important in determining the rate of
CC       inactivation of the channel while the tail may play a role in
CC       modulation of channel activity and/or targeting of the channel to
CC       specific subcellular compartments. {ECO:0000250|UniProtKB:Q28527}.
CC   -!- DOMAIN: The transmembrane segment S4 functions as a voltage-sensor and
CC       is characterized by a series of positively charged amino acids at every
CC       third position. Channel opening and closing is effected by a
CC       conformation change that affects the position and orientation of the
CC       voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC       transmembrane electric field that is positive inside would push the
CC       positively charged S4 segment outwards, thereby opening the pore, while
CC       a field that is negative inside would pull the S4 segment inwards and
CC       close the pore. Changes in the position and orientation of S4 are then
CC       transmitted to the activation gate formed by the inner helix bundle via
CC       the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
CC       (TC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily. {ECO:0000305}.
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DR   EMBL; U03723; AAB60668.1; -; Genomic_DNA.
DR   EMBL; AK036112; BAC29309.1; -; mRNA.
DR   EMBL; BX293548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466519; EDL27774.1; -; Genomic_DNA.
DR   EMBL; BC109014; AAI09015.1; -; mRNA.
DR   CCDS; CCDS16505.1; -.
DR   PIR; S09045; S09045.
DR   RefSeq; NP_067250.2; NM_021275.4.
DR   RefSeq; XP_006498875.1; XM_006498812.2.
DR   AlphaFoldDB; Q61423; -.
DR   BMRB; Q61423; -.
DR   SMR; Q61423; -.
DR   BioGRID; 200879; 6.
DR   IntAct; Q61423; 3.
DR   MINT; Q61423; -.
DR   STRING; 10090.ENSMUSP00000037958; -.
DR   GuidetoPHARMACOLOGY; 541; -.
DR   GlyCosmos; Q61423; 1 site, No reported glycans.
DR   GlyGen; Q61423; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61423; -.
DR   PhosphoSitePlus; Q61423; -.
DR   MaxQB; Q61423; -.
DR   PaxDb; 10090-ENSMUSP00000037958; -.
DR   PeptideAtlas; Q61423; -.
DR   ProteomicsDB; 263396; -.
DR   ABCD; Q61423; 2 sequenced antibodies.
DR   Antibodypedia; 3115; 210 antibodies from 33 providers.
DR   DNASU; 16492; -.
DR   Ensembl; ENSMUST00000037012.3; ENSMUSP00000037958.3; ENSMUSG00000042604.6.
DR   GeneID; 16492; -.
DR   KEGG; mmu:16492; -.
DR   UCSC; uc008llu.2; mouse.
DR   AGR; MGI:96661; -.
DR   CTD; 3739; -.
DR   MGI; MGI:96661; Kcna4.
DR   VEuPathDB; HostDB:ENSMUSG00000042604; -.
DR   eggNOG; KOG1545; Eukaryota.
DR   GeneTree; ENSGT00940000162248; -.
DR   HOGENOM; CLU_011722_4_0_1; -.
DR   InParanoid; Q61423; -.
DR   OMA; GDECSYT; -.
DR   OrthoDB; 1478695at2759; -.
DR   PhylomeDB; Q61423; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 16492; 6 hits in 79 CRISPR screens.
DR   PRO; PR:Q61423; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q61423; Protein.
DR   Bgee; ENSMUSG00000042604; Expressed in caudate-putamen and 90 other cell types or tissues.
DR   GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0043194; C:axon initial segment; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR   GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:0005216; F:monoatomic ion channel activity; ISO:MGI.
DR   GO; GO:0022839; F:monoatomic ion-gated channel activity; IEA:UniProt.
DR   GO; GO:0005267; F:potassium channel activity; ISO:MGI.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0099508; F:voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.5.600; Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR020467; K_chnl_volt-dep_Kv1.4.
DR   InterPro; IPR012897; K_chnl_volt-dep_Kv1.4_TID.
DR   InterPro; IPR037065; K_chnl_volt-dep_Kv1.4_TID_sf.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537:SF284; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY A MEMBER 4; 1.
DR   PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF07941; K_channel_TID; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01511; KV14CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   Genevisible; Q61423; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Glycoprotein; Ion channel; Ion transport;
KW   Membrane; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..654
FT                   /note="Potassium voltage-gated channel subfamily A member
FT                   4"
FT                   /id="PRO_0000053982"
FT   TOPO_DOM        1..305
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        306..327
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        328..371
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        372..393
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        394..404
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        405..425
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        426..440
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        441..461
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        462..476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        477..498
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        499..512
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        513..524
FT                   /note="Helical; Name=Pore helix"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        525..532
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        533..539
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        540..568
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        569..654
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   REGION          24..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..476
FT                   /note="S4-S5 linker"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   REGION          630..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           525..530
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   MOTIF           652..654
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        80..99
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..140
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         600
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        160
FT                   /note="D -> E (in Ref. 1; AAB60668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="P -> T (in Ref. 1; AAB60668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        636
FT                   /note="E -> D (in Ref. 1; AAB60668)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   654 AA;  73470 MW;  9322A3DC9CBA2AC4 CRC64;
     MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA VEGTGGSGGG
     PHHHHQTRGA YSSHDPQGSR GSRRRRRQRT EKKKLHHRQS SFPHCSDLMP SGSEEKILRE
     LSEEEEDEEE EEEEEEEGRF YYSEEDHGDG CSYTDLLPQD DGGGGGYSSV RYSDCCERVV
     INVSGLRFET QMKTLAQFPE TLLGDPEKRT QYFDPLRNEY FFDRNRPSFD AILYYYQSGG
     RLKRPVNVPF DIFTEEVKFY QLGEEALLKF REDEGFVREE EDRALPENEF KKQIWLLFEY
     PESSSPARGI AIVSVLVILI SIVIFCLETL PEFRDDRDLI MALSAGGHSR LLNDTSAPHL
     ENSGHTIFND PFFIVETVCI VWFSFEFVVR CFACPSQALF FKNIMNIIDI VSILPYFITL
     GTDLAQQQGG GNGQQQQAMS FAILRIIRLV RVFRIFKLSR HSKGLQILGH TLRASMRELG
     LLIFFLFIGV ILFSSAVYFA EADEPTTHFQ SIPDAFWWAV VTMTTVGYGD MKPITVGGKI
     VGSLCAIAGV LTIALPVPVI VSNFNYFYHR ETENEEQTQL TQNAVSCPYL PSNLLKKFRS
     STSSSLGDKS EYLEMEEGVK ESLCGKEEKC QGKGDESETD KNNCSNAKAV ETDV
//