KCND3_RAT
ID KCND3_RAT Reviewed; 655 AA.
AC Q62897; O08723; P70622; Q63286; Q99P42;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Potassium voltage-gated channel subfamily D member 3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv4.3;
GN Name=Kcnd3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8831489; DOI=10.1161/01.res.79.4.659;
RA Dixon J.E., Shi W., Wang H.-S., McDonald C., Yu H., Wymore R.S.,
RA Cohen I.S., McKinnon D.;
RT "Role of the Kv4.3 K+ channel in ventricular muscle. A molecular correlate
RT for the transient outward current.";
RL Circ. Res. 79:659-668(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8734615; DOI=10.1152/jn.1996.75.5.2174;
RA Serodio P., Vega-Saenz de Miera E., Rudy B.;
RT "Cloning of a novel component of A-type K+ channels operating at
RT subthreshold potentials with unique expression in heart and brain.";
RL J. Neurophysiol. 75:2174-2179(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=9001401; DOI=10.1016/s0014-5793(96)01388-9;
RA Tsaur M.-L., Chou C.-C., Shih Y.-H., Wang H.-L.;
RT "Cloning, expression and CNS distribution of Kv4.3, an A-type K+ channel
RT alpha subunit.";
RL FEBS Lett. 400:215-220(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Smooth muscle, and Vas deferens;
RX PubMed=9450548; DOI=10.1016/s0014-5793(97)01483-x;
RA Ohya S., Tanaka M., Oku T., Asai Y., Watanabe M., Giles W.R., Imaizumi Y.;
RT "Molecular cloning and tissue distribution of an alternatively spliced
RT variant of an A-type K+ channel alpha-subunit, Kv4.3 in the rat.";
RL FEBS Lett. 420:47-53(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX PubMed=11427525; DOI=10.1074/jbc.m101058200;
RA Song M., Helguera G., Eghbali M., Zhu N., Zarei M.M., Olcese R., Toro L.,
RA Stefani E.;
RT "Remodeling of Kv4.3 potassium channel gene expression under the control of
RT sex hormones.";
RL J. Biol. Chem. 276:31883-31890(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 455-606 (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RX PubMed=9314834; DOI=10.1161/01.res.81.4.533;
RA Takimoto K., Li D., Hershman K.M., Li P., Jackson E.K., Levitan E.S.;
RT "Decreased expression of Kv4.2 and novel Kv4.3 K+ channel subunit mRNAs in
RT ventricles of renovascular hypertensive rats.";
RL Circ. Res. 81:533-539(1997).
RN [7]
RP INTERACTION WITH KCNIP1; KCNIP2 AND KCNIP3.
RX PubMed=10676964; DOI=10.1038/35000592;
RA An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G.,
RA Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.;
RT "Modulation of A-type potassium channels by a family of calcium sensors.";
RL Nature 403:553-556(2000).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12006572; DOI=10.1074/jbc.m203651200;
RA Takimoto K., Yang E.-K., Conforti L.;
RT "Palmitoylation of KChIP splicing variants is required for efficient cell
RT surface expression of Kv4.3 channels.";
RL J. Biol. Chem. 277:26904-26911(2002).
RN [9]
RP INTERACTION WITH KCNIP4.
RX PubMed=11805342; DOI=10.1073/pnas.022509299;
RA Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D., Carroll K.I.,
RA Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E., Jurman M.E.,
RA Lawson D., Silos-Santiago I., Xie Y., Covarrubias M., Rhodes K.J.,
RA Distefano P.S., An W.F.;
RT "Elimination of fast inactivation in Kv4 A-type potassium channels by an
RT auxiliary subunit domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002).
RN [10]
RP PHOSPHORYLATION AT SER-569 BY CAMK2D.
RX PubMed=15456698; DOI=10.1152/ajpcell.00293.2004;
RA Sergeant G.P., Ohya S., Reihill J.A., Perrino B.A., Amberg G.C.,
RA Imaizumi Y., Horowitz B., Sanders K.M., Koh S.D.;
RT "Regulation of Kv4.3 currents by Ca2+/calmodulin-dependent protein kinase
RT II.";
RL Am. J. Physiol. 288:C304-C313(2005).
RN [11] {ECO:0000305}
RP INTERACTION WITH DLG1, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19213956; DOI=10.1161/circresaha.108.191007;
RA El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
RA Coulombe A., Jeromin A., Hatem S.N.;
RT "Kv4 potassium channels form a tripartite complex with the anchoring
RT protein SAP97 and CaMKII in cardiac myocytes.";
RL Circ. Res. 104:758-769(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 2-143 IN COMPLEX WITH KCNIP1.
RX PubMed=17057713; DOI=10.1038/nsmb1164;
RA Pioletti M., Findeisen F., Hura G.L., Minor D.L. Jr.;
RT "Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a
RT cross-shaped octamer.";
RL Nat. Struct. Mol. Biol. 13:987-995(2006).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly
CC inactivating A-type potassium channels. May contribute to I(To) current
CC in heart and I(Sa) current in neurons. Channel properties are modulated
CC by interactions with other alpha subunits and with regulatory subunits.
CC {ECO:0000269|PubMed:8734615, ECO:0000269|PubMed:8831489,
CC ECO:0000269|PubMed:9001401, ECO:0000269|PubMed:9450548}.
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCND1 and/or KCND2.
CC Interacts with DLG1. Associates with the regulatory subunits KCNIP1,
CC KCNIP2, KCNIP3 and KCNIP4. Interacts with KCNE1, KCNE2, SCN1B and
CC KCNAB1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q62897; Q9NZI2: KCNIP1; Xeno; NbExp=3; IntAct=EBI-7082853, EBI-2120635;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12006572,
CC ECO:0000269|PubMed:19213956}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:19213956};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000269|PubMed:19213956}. Note=Interaction with palmitoylated
CC KCNIP2 and KCNIP3 enhances cell surface expression.
CC {ECO:0000269|PubMed:12006572}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Kv4.3 long form;
CC IsoId=Q62897-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62897-2; Sequence=VSP_008831;
CC Name=3;
CC IsoId=Q62897-3; Sequence=VSP_008831, VSP_008832;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, in particular in the
CC retrosplenial cortex, medial habenula, anterior thalamus, hippocampus,
CC cerebellum and lateral geniculate and superior colliculus. Highly
CC expressed in heart atrium (at protein level) and throughout the
CC ventricle wall, in lung and vas deferens. {ECO:0000269|PubMed:19213956,
CC ECO:0000269|PubMed:8734615, ECO:0000269|PubMed:8831489,
CC ECO:0000269|PubMed:9001401, ECO:0000269|PubMed:9450548}.
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 -!- PTM: Regulated through phosphorylation at Ser-569 by CaMK2D.
CC {ECO:0000269|PubMed:15456698}.
CC -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
CC 1.A.1.2) subfamily. Kv4.3/KCND3 sub-subfamily. {ECO:0000305}.
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DR EMBL; U75448; AAB18337.1; -; mRNA.
DR EMBL; U42975; AAC52695.1; -; mRNA.
DR EMBL; L48619; AAA80459.1; -; mRNA.
DR EMBL; AB003587; BAA24525.1; -; mRNA.
DR EMBL; AF334791; AAK07651.1; -; mRNA.
DR EMBL; U92897; AAB53321.1; -; mRNA.
DR RefSeq; NP_001257891.1; NM_001270962.1.
DR RefSeq; NP_001257892.1; NM_001270963.1.
DR RefSeq; NP_113927.2; NM_031739.3. [Q62897-3]
DR PDB; 2I2R; X-ray; 3.35 A; A/B/C/D/I/J/K/L=2-143.
DR PDBsum; 2I2R; -.
DR AlphaFoldDB; Q62897; -.
DR SMR; Q62897; -.
DR BioGRID; 249307; 1.
DR CORUM; Q62897; -.
DR DIP; DIP-29245N; -.
DR IntAct; Q62897; 2.
DR MINT; Q62897; -.
DR STRING; 10116.ENSRNOP00000019997; -.
DR DrugCentral; Q62897; -.
DR GuidetoPHARMACOLOGY; 554; -.
DR iPTMnet; Q62897; -.
DR PhosphoSitePlus; Q62897; -.
DR PaxDb; Q62897; -.
DR PRIDE; Q62897; -.
DR ABCD; Q62897; 2 sequenced antibodies.
DR GeneID; 65195; -.
DR KEGG; rno:65195; -.
DR UCSC; RGD:68394; rat. [Q62897-1]
DR CTD; 3752; -.
DR RGD; 68394; Kcnd3.
DR eggNOG; KOG4390; Eukaryota.
DR InParanoid; Q62897; -.
DR OrthoDB; 469107at2759; -.
DR PhylomeDB; Q62897; -.
DR TreeFam; TF313103; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR Reactome; R-RNO-5576894; Phase 1 - inactivation of fast Na+ channels.
DR EvolutionaryTrace; Q62897; -.
DR PRO; PR:Q62897; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014686; Expressed in Ammon's horn and 14 other tissues.
DR ExpressionAtlas; Q62897; baseline and differential.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0034705; C:potassium channel complex; IDA:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IMP:RGD.
DR GO; GO:0005216; F:ion channel activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; IDA:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:CAFA.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:RGD.
DR GO; GO:0086009; P:membrane repolarization; ISO:RGD.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; IEA:GOC.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:CAFA.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; TAS:RGD.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0099625; P:ventricular cardiac muscle cell membrane repolarization; ISO:RGD.
DR Gene3D; 1.20.120.350; -; 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; IPR003975; K_chnl_volt-dep_Kv4.
DR InterPro; IPR004056; K_chnl_volt-dep_Kv4.3.
DR InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
DR InterPro; IPR021645; Shal-type_N.
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; PF11879; DUF3399; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11601; Shal-type; 1.
DR PRINTS; PR01518; KV43CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01497; SHALCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel; Zinc.
FT CHAIN 1..655
FT /note="Potassium voltage-gated channel subfamily D member
FT 3"
FT /id="PRO_0000054071"
FT TOPO_DOM 1..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 360..380
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..20
FT /note="Interaction with KCNIP2"
FT /evidence="ECO:0000250"
FT REGION 474..489
FT /note="Mediates dendritic targeting"
FT /evidence="ECO:0000250"
FT REGION 523..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 367..372
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 624..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0V1"
FT MOD_RES 569
FT /note="Phosphoserine; by CaMK2D"
FT /evidence="ECO:0000269|PubMed:15456698"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0V1"
FT VAR_SEQ 488..506
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:8734615,
FT ECO:0000303|PubMed:8831489, ECO:0000303|PubMed:9001401"
FT /id="VSP_008831"
FT VAR_SEQ 608..655
FT /note="SQITTAIISIPTPPALTPEGESRPPPASPGPNTNIPSITSNVVKVSVL ->
FT QDQEQPRGRVVTCKQEEIITLCI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9001401"
FT /id="VSP_008832"
FT CONFLICT 124
FT /note="L -> H (in Ref. 3; AAA80459)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="S -> T (in Ref. 2; AAC52695 and 5; AAK07651)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="S -> T (in Ref. 3; AAA80459)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="P -> A (in Ref. 2; AAC52695)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="V -> A (in Ref. 1; AAB18337 and 4; BAA24525)"
FT /evidence="ECO:0000305"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:2I2R"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:2I2R"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2I2R"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:2I2R"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:2I2R"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2I2R"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:2I2R"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:2I2R"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:2I2R"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:2I2R"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2I2R"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2I2R"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:2I2R"
SQ SEQUENCE 655 AA; 73513 MW; 26BC512BDE069C09 CRC64;
MAAGVAAWLP FARAAAIGWM PVANCPMPLA PADKNKRQDE LIVLNVSGRR FQTWRTTLER
YPDTLLGSTE KEFFFNEDTK EYFFDRDPEV FRCVLNFYRT GKLHYPRYEC ISAYDDELAF
YGILPEIIGD CCYEEYKDRK RENAERLMDD NESENNQESM PSLSFRQTMW RAFENPHTST
LALVFYYVTG FFIAVSVITN VVETVPCGTV PGSKELPCGE RYSVAFFCLD TACVMIFTVE
YLLRLFAAPS RYRFIRSVMS IIDVVAIMPY YIGLVMTNNE DVSGAFVTLR VFRVFRIFKF
SRHSQGLRIL GYTLKSCASE LGFLLFSLTM AIIIFATVMF YAEKGSSASK FTSIPASFWY
TIVTMTTLGY GDMVPKTIAG KIFGSICSLS GVLVIALPVP VIVSNFSRIY HQNQRADKRR
AQKKARLARI RVAKTGSSNA YLHSKRNGLL NEALELTGTP EEEHMGKTTS LIESQHHHLL
HCLEKTTGLS YLVDDPLLSV RTSTIKNHEF IDEQMFEQNC MESSMQNYPS TRSPSLSSHS
GLTTTCCSRR SKKTTHLPNS NLPATRLRSM QELSTIHIQG SEQPSLTTSR SSLNLKADDG
LRPNCKTSQI TTAIISIPTP PALTPEGESR PPPASPGPNT NIPSITSNVV KVSVL
