ID KCNC4_HUMAN Reviewed; 635 AA.
AC Q03721; Q3MIM4; Q5TBI6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 27-MAR-2024, entry version 196.
DE RecName: Full=Potassium voltage-gated channel subfamily C member 4;
DE AltName: Full=KSHIIIC;
DE AltName: Full=Voltage-gated potassium channel subunit Kv3.4;
GN Name=KCNC4 {ECO:0000312|HGNC:HGNC:6236};
GN Synonyms=C1orf30 {ECO:0000312|HGNC:HGNC:6236};
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 2).
RC TISSUE=Brain;
RX PubMed=1381835; DOI=10.1098/rspb.1992.0036;
RA de Miera E.V.-S., Moreno H., Fruhling D., Kentros C., Rudy B.;
RT "Cloning of ShIII (Shaw-like) cDNAs encoding a novel high-voltage-
RT activating, TEA-sensitive, type-A K+ channel.";
RL Proc. R. Soc. B 248:9-18(1992).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 166-635 (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP PHOSPHORYLATION AT SER-15 AND SER-21, AND MUTAGENESIS OF SER-15 AND SER-21.
RX PubMed=7993631; DOI=10.1016/0896-6273(94)90425-1;
RA Covarrubias M., Wei A., Salkoff L., Vyas T.B.;
RT "Elimination of rapid potassium channel inactivation by phosphorylation of
RT the inactivation gate.";
RL Neuron 13:1403-1412(1994).
RN [5]
RP PHOSPHORYLATION AT SER-8 AND SER-9, AND MUTAGENESIS OF SER-8; SER-9; SER-15
RP AND SER-21.
RX PubMed=9649584; DOI=10.1085/jgp.112.1.71;
RA Beck E.J., Sorensen R.G., Slater S.J., Covarrubias M.;
RT "Interactions between multiple phosphorylation sites in the inactivation
RT particle of a K+ channel. Insights into the molecular mechanism of protein
RT kinase C action.";
RL J. Gen. Physiol. 112:71-84(1998).
RN [6]
RP STRUCTURE BY NMR OF 1-30.
RX PubMed=9000078; DOI=10.1038/385272a0;
RA Antz C., Geyer M., Fakler B., Schott M.K., Guy H.R., Frank R.,
RA Ruppersberg J.P., Kalbitzer H.R.;
RT "NMR structure of inactivation gates from mammalian voltage-dependent
RT potassium channels.";
RL Nature 385:272-275(1997).
RN [7]
RP STRUCTURE BY NMR OF 1-30.
RX PubMed=10048926; DOI=10.1038/5833;
RA Antz C., Bauer T., Kalbacher H., Frank R., Covarrubias M., Kalbitzer H.R.,
RA Ruppersberg J.P., Baukrowitz T., Fakler B.;
RT "Control of K+ channel gating by protein phosphorylation: structural
RT switches of the inactivation gate.";
RL Nat. Struct. Biol. 6:146-150(1999).
CC -!- FUNCTION: This protein mediates the voltage-dependent potassium ion
CC permeability of excitable membranes. Assuming opened or closed
CC conformations in response to the voltage difference across the
CC membrane, the protein forms a potassium-selective channel through which
CC potassium ions may pass in accordance with their electrochemical
CC gradient.
CC -!- SUBUNIT: Homotetramer (Probable). Heterotetramer of potassium channel
CC proteins (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- INTERACTION:
CC Q03721; P56817: BACE1; NbExp=3; IntAct=EBI-11334865, EBI-2433139;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q03721-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03721-2; Sequence=VSP_020581, VSP_020582;
CC Name=3;
CC IsoId=Q03721-3; Sequence=VSP_040033;
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position.
CC -!- DOMAIN: The tail may be important in modulation of channel activity
CC and/or targeting of the channel to specific subcellular compartments.
CC -!- PTM: Phosphorylation of serine residues in the inactivation gate
CC inhibits rapid channel closure. {ECO:0000269|PubMed:7993631,
CC ECO:0000269|PubMed:9649584}.
CC -!- MISCELLANEOUS: [Isoform 2]: Could be a cloning artifact. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Kv3.4/KCNC4 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M64676; AAA57263.1; -; mRNA.
DR EMBL; AL137790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019010; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC101769; AAI01770.1; -; mRNA.
DR CCDS; CCDS44193.1; -. [Q03721-3]
DR CCDS; CCDS821.1; -. [Q03721-1]
DR RefSeq; NP_001034663.1; NM_001039574.2. [Q03721-3]
DR RefSeq; NP_004969.2; NM_004978.4. [Q03721-1]
DR PDB; 1B4G; NMR; -; A=1-30.
DR PDB; 1B4I; NMR; -; A=1-30.
DR PDB; 1ZTN; NMR; -; A=1-30.
DR PDBsum; 1B4G; -.
DR PDBsum; 1B4I; -.
DR PDBsum; 1ZTN; -.
DR AlphaFoldDB; Q03721; -.
DR SMR; Q03721; -.
DR BioGRID; 109951; 37.
DR IntAct; Q03721; 29.
DR STRING; 9606.ENSP00000358802; -.
DR ChEMBL; CHEMBL2362996; -.
DR DrugBank; DB04522; Dexfosfoserine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q03721; -.
DR GlyCosmos; Q03721; 2 sites, No reported glycans.
DR GlyGen; Q03721; 2 sites.
DR iPTMnet; Q03721; -.
DR PhosphoSitePlus; Q03721; -.
DR BioMuta; KCNC4; -.
DR DMDM; 66774206; -.
DR MassIVE; Q03721; -.
DR PaxDb; 9606-ENSP00000358802; -.
DR PeptideAtlas; Q03721; -.
DR ProteomicsDB; 58220; -. [Q03721-1]
DR ProteomicsDB; 58221; -. [Q03721-2]
DR ProteomicsDB; 58222; -. [Q03721-3]
DR TopDownProteomics; Q03721-3; -. [Q03721-3]
DR ABCD; Q03721; 1 sequenced antibody.
DR Antibodypedia; 3094; 343 antibodies from 31 providers.
DR DNASU; 3749; -.
DR Ensembl; ENST00000369787.7; ENSP00000358802.3; ENSG00000116396.15. [Q03721-1]
DR Ensembl; ENST00000438661.3; ENSP00000393655.2; ENSG00000116396.15. [Q03721-3]
DR Ensembl; ENST00000469655.5; ENSP00000436656.1; ENSG00000116396.15. [Q03721-1]
DR GeneID; 3749; -.
DR KEGG; hsa:3749; -.
DR MANE-Select; ENST00000438661.3; ENSP00000393655.2; NM_001039574.3; NP_001034663.1. [Q03721-3]
DR UCSC; uc001dzg.4; human. [Q03721-1]
DR AGR; HGNC:6236; -.
DR CTD; 3749; -.
DR DisGeNET; 3749; -.
DR GeneCards; KCNC4; -.
DR HGNC; HGNC:6236; KCNC4.
DR HPA; ENSG00000116396; Tissue enhanced (brain).
DR MIM; 176265; gene.
DR neXtProt; NX_Q03721; -.
DR OpenTargets; ENSG00000116396; -.
DR PharmGKB; PA30028; -.
DR VEuPathDB; HostDB:ENSG00000116396; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000158860; -.
DR InParanoid; Q03721; -.
DR OMA; RIGANPT; -.
DR OrthoDB; 1478695at2759; -.
DR PhylomeDB; Q03721; -.
DR TreeFam; TF352511; -.
DR PathwayCommons; Q03721; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR SignaLink; Q03721; -.
DR SIGNOR; Q03721; -.
DR BioGRID-ORCS; 3749; 40 hits in 1158 CRISPR screens.
DR ChiTaRS; KCNC4; human.
DR EvolutionaryTrace; Q03721; -.
DR GeneWiki; KCNC4; -.
DR GenomeRNAi; 3749; -.
DR Pharos; Q03721; Tclin.
DR PRO; PR:Q03721; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q03721; Protein.
DR Bgee; ENSG00000116396; Expressed in right frontal lobe and 127 other cell types or tissues.
DR ExpressionAtlas; Q03721; baseline and differential.
DR Genevisible; Q03721; HS.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; TAS:ProtInc.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; TAS:ProtInc.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR CDD; cd18415; BTB_KCNC2_4; 1.
DR Gene3D; 1.10.287.70; -; 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; IPR003974; K_chnl_volt-dep_Kv3.
DR InterPro; IPR005405; K_chnl_volt-dep_Kv3.4.
DR InterPro; IPR021105; K_chnl_volt-dep_Kv3_ID.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537:SF126; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY C 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; PF11404; Potassium_chann; 1.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01583; KV34CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01498; SHAWCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..635
FT /note="Potassium voltage-gated channel subfamily C member
FT 4"
FT /id="PRO_0000054058"
FT TOPO_DOM 1..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..364
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Inactivation gate"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 436..441
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9649584"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9649584"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7993631"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7993631"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 539..582
FT /note="DSKQNGDANAVLSDEEGAGLTQPLASSPTPEERRALRRSTTRDR -> GEIR
FT GWEGKSLFPQWPREFPNGPQTLGFGMCFVWGFPKHKDVPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1381835,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020581"
FT VAR_SEQ 583..635
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1381835,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020582"
FT VAR_SEQ 607..635
FT /note="GTFVLRDLPLQHSPEAACPPTAGTLFLPH -> ETCQDALSSNYAQAEVLTL
FT S (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040033"
FT VARIANT 318
FT /note="D -> Y (in dbSNP:rs35167146)"
FT /id="VAR_034051"
FT VARIANT 516
FT /note="R -> Q (in dbSNP:rs59123361)"
FT /id="VAR_062185"
FT VARIANT 520
FT /note="C -> Y (in dbSNP:rs12411176)"
FT /id="VAR_027505"
FT MUTAGEN 8
FT /note="S->A: Decreased inhibition of channel closure by
FT PKC. Inhibition of channel closure is nearly abolished;
FT when associated with A-9."
FT /evidence="ECO:0000269|PubMed:9649584"
FT MUTAGEN 8
FT /note="S->D: Decreased rate of channel inactivation. Loss
FT of channel inactivation; when associated with D-9; D-15 and
FT D-21."
FT /evidence="ECO:0000269|PubMed:9649584"
FT MUTAGEN 9
FT /note="S->A: Strong decrease of inhibition of channel
FT closure by PKC. Inhibition of channel closure is nearly
FT abolished; when associated with A-8."
FT /evidence="ECO:0000269|PubMed:9649584"
FT MUTAGEN 9
FT /note="S->D: Decreased rate of channel inactivation. Loss
FT of channel inactivation; when associated with D-8; D-15 and
FT D-21."
FT /evidence="ECO:0000269|PubMed:9649584"
FT MUTAGEN 15
FT /note="S->A: Decreased inhibition of channel closure by
FT PKC."
FT /evidence="ECO:0000269|PubMed:7993631,
FT ECO:0000269|PubMed:9649584"
FT MUTAGEN 15
FT /note="S->D: Slightly decreased rate of channel
FT inactivation. Loss of channel inactivation; when associated
FT with D-8; D-9 and D-21."
FT /evidence="ECO:0000269|PubMed:7993631,
FT ECO:0000269|PubMed:9649584"
FT MUTAGEN 21
FT /note="S->A: Decreased inhibition of channel closure by
FT PKC."
FT /evidence="ECO:0000269|PubMed:7993631,
FT ECO:0000269|PubMed:9649584"
FT MUTAGEN 21
FT /note="S->D: Slightly decreased rate of channel
FT inactivation. Loss of channel inactivation; when associated
FT with D-8; D-9 and D-15."
FT /evidence="ECO:0000269|PubMed:7993631,
FT ECO:0000269|PubMed:9649584"
FT CONFLICT 86
FT /note="S -> T (in Ref. 1; AAA57263)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="F -> I (in Ref. 1; AAA57263)"
FT /evidence="ECO:0000305"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:1B4G"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1B4G"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1B4I"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:1ZTN"
SQ SEQUENCE 635 AA; 69767 MW; 8A36F0A16AD17722 CRC64;
MISSVCVSSY RGRKSGNKPP SKTCLKEEMA KGEASEKIII NVGGTRHETY RSTLRTLPGT
RLAWLADPDG GGRPETDGGG VGSSGSSGGG GCEFFFDRHP GVFAYVLNYY RTGKLHCPAD
VCGPLFEEEL TFWGIDETDV EPCCWMTYRQ HRDAEEALDI FESPDGGGSG AGPSDEAGDD
ERELALQRLG PHEGGAGHGA GSGGCRGWQP RMWALFEDPY SSRAARVVAF ASLFFILVSI
TTFCLETHEA FNIDRNVTEI LRVGNITSVH FRREVETEPI LTYIEGVCVL WFTLEFLVRI
VCCPDTLDFV KNLLNIIDFV AILPFYLEVG LSGLSSKAAR DVLGFLRVVR FVRILRIFKL
TRHFVGLRVL GHTLRASTNE FLLLIIFLAL GVLIFATMIY YAERIGARPS DPRGNDHTDF
KNIPIGFWWA VVTMTTLGYG DMYPKTWSGM LVGALCALAG VLTIAMPVPV IVNNFGMYYS
LAMAKQKLPK KRKKHVPRPA QLESPMYCKS EETSPRDSTC SDTSPPAREE GMIERKRADS
KQNGDANAVL SDEEGAGLTQ PLASSPTPEE RRALRRSTTR DRNKKAAACF LLSTGDYACA
DGSVRKGTFV LRDLPLQHSP EAACPPTAGT LFLPH
//
