KCNA4_MOUSE
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 03-AUG-2022, entry version 168.
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 voltage-sensor and is
CC 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) (TC
CC 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; 4.
DR IntAct; Q61423; 3.
DR MINT; Q61423; -.
DR STRING; 10090.ENSMUSP00000037958; -.
DR GuidetoPHARMACOLOGY; 541; -.
DR GlyGen; Q61423; 1 site.
DR iPTMnet; Q61423; -.
DR PhosphoSitePlus; Q61423; -.
DR MaxQB; Q61423; -.
DR PaxDb; Q61423; -.
DR PeptideAtlas; Q61423; -.
DR PRIDE; Q61423; -.
DR ProteomicsDB; 263396; -.
DR ABCD; Q61423; 2 sequenced antibodies.
DR Antibodypedia; 3115; 196 antibodies from 32 providers.
DR DNASU; 16492; -.
DR Ensembl; ENSMUST00000037012; ENSMUSP00000037958; ENSMUSG00000042604.
DR GeneID; 16492; -.
DR KEGG; mmu:16492; -.
DR UCSC; uc008llu.2; mouse.
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; 695337at2759; -.
DR PhylomeDB; Q61423; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16492; 6 hits in 74 CRISPR screens.
DR PRO; PR:Q61423; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61423; protein.
DR Bgee; ENSMUSG00000042604; Expressed in caudate-putamen and 89 other tissues.
DR Genevisible; Q61423; MM.
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:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA: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:ion channel activity; ISO:MGI.
DR GO; GO:0005267; F:potassium channel activity; ISO:MGI.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
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 GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 1.20.5.600; -; 1.
DR Gene3D; 3.30.710.10; -; 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; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF07941; K_channel_TID; 1.
DR PRINTS; PR01511; KV14CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
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
