KCNH1_RAT
ID KCNH1_RAT Reviewed; 962 AA.
AC Q63472;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 1;
DE AltName: Full=Ether-a-go-go potassium channel 1;
DE Short=EAG channel 1;
DE Short=EAG1;
DE Short=r-eag {ECO:0000303|PubMed:9400421};
DE AltName: Full=Voltage-gated potassium channel subunit Kv10.1;
GN Name=Kcnh1; Synonyms=Eag {ECO:0000303|PubMed:7925287};
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Cerebellum;
RX PubMed=7925287; DOI=10.1002/j.1460-2075.1994.tb06767.x;
RA Ludwig J., Terlau H., Wunder F., Brueggemann A., Pardo L.A., Marquardt A.,
RA Stuehmer W., Pongs O.;
RT "Functional expression of a rat homologue of the voltage gated ether a go-
RT go potassium channel reveals differences in selectivity and activation
RT kinetics between the Drosophila channel and its mammalian counterpart.";
RL EMBO J. 13:4451-4458(1994).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN CAD, AND SUBUNIT.
RX PubMed=9400421; DOI=10.1093/emboj/16.21.6337;
RA Ludwig J., Owen D., Pongs O.;
RT "Carboxy-terminal domain mediates assembly of the voltage-gated rat ether-
RT a-go-go potassium channel.";
RL EMBO J. 16:6337-6345(1997).
RN [3]
RP INTERACTION WITH ALG10B.
RC STRAIN=Wistar; TISSUE=Cerebellum;
RX PubMed=9722534; DOI=10.1074/jbc.273.36.23080;
RA Hoshi N., Takahashi H., Shahidullah M., Yokoyama S., Higashida H.;
RT "KCR1, a membrane protein that facilitates functional expression of non-
RT inactivating K+ currents associates with rat EAG voltage-dependent K+
RT channels.";
RL J. Biol. Chem. 273:23080-23085(1998).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10718922; DOI=10.1046/j.1365-2826.2000.00447.x;
RA Wulfsen I., Hauber H.-P., Schiemann D., Bauer C.K., Schwarz J.R.;
RT "Expression of mRNA for voltage-dependent and inward-rectifying K channels
RT in GH3/B6 cells and rat pituitary.";
RL J. Neuroendocrinol. 12:263-272(2000).
RN [5]
RP INTERACTION WITH RABEP1.
RX PubMed=22841712; DOI=10.1016/j.febslet.2012.07.055;
RA Ninkovic M., Mitkovski M., Kohl T., Stuhmer W., Pardo L.A.;
RT "Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion
RT channel trafficking.";
RL FEBS Lett. 586:3077-3084(2012).
RN [6]
RP INTERACTION WITH CTTN.
RX PubMed=23144454; DOI=10.1074/jbc.m112.372540;
RA Herrmann S., Ninkovic M., Kohl T., Lorinczi E., Pardo L.A.;
RT "Cortactin controls surface expression of the voltage-gated potassium
RT channel K(V)10.1.";
RL J. Biol. Chem. 287:44151-44163(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24495567; DOI=10.1186/1471-2202-15-23;
RA Chuang C.C., Jow G.M., Lin H.M., Weng Y.H., Hu J.H., Peng Y.J., Chiu Y.C.,
RA Chiu M.M., Jeng C.J.;
RT "The punctate localization of rat Eag1 K+ channels is conferred by the
RT proximal post-CNBHD region.";
RL BMC Neurosci. 15:23-23(2014).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25556795; DOI=10.1113/jphysiol.2014.281600;
RA Mortensen L.S., Schmidt H., Farsi Z., Barrantes-Freer A., Rubio M.E.,
RA Ufartes R., Eilers J., Sakaba T., Stuehmer W., Pardo L.A.;
RT "KV 10.1 opposes activity-dependent increase in Ca2+ influx into the
RT presynaptic terminal of the parallel fibre-Purkinje cell synapse.";
RL J. Physiol. (Lond.) 593:181-196(2015).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.78 ANGSTROMS) OF 1-962 IN COMPLEX WITH
RP CALM, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND GLYCOSYLATION AT ASN-388.
RX PubMed=27516594; DOI=10.1126/science.aaf8070;
RA Whicher J.R., MacKinnon R.;
RT "Structure of the voltage-gated K(+) channel Eag1 reveals an alternative
RT voltage sensing mechanism.";
RL Science 353:664-669(2016).
CC -!- FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed
CC rectifier potassium channel (PubMed:7925287, PubMed:9400421,
CC PubMed:24495567, PubMed:27516594). Channel properties are modulated by
CC subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the
CC regulation of cell proliferation and differentiation, in particular
CC adipogenic and osteogenic differentiation in bone marrow-derived
CC mesenchymal stem cells (MSCs) (By similarity).
CC {ECO:0000250|UniProtKB:O95259, ECO:0000269|PubMed:24495567,
CC ECO:0000269|PubMed:27516594, ECO:0000269|PubMed:7925287,
CC ECO:0000269|PubMed:9400421}.
CC -!- ACTIVITY REGULATION: Channel activity is inhibited by interaction with
CC Ca(2+)-bound calmodulin (PubMed:27516594). Interaction of a single
CC pore-forming alpha subunit with a calmodulin chain is sufficient to
CC promote channel closure. Channel activity is not regulated by cyclic
CC nucleotides. Channel activity is inhibited by binding intracellular
CC phosphatidylinositol-3,5-bisphosphate and phosphatidylinositol-4,5-
CC bisphosphate (PIP2), but is not inhibited by phosphatidylinositol 4-
CC phosphate (By similarity). {ECO:0000250|UniProtKB:O95259,
CC ECO:0000250|UniProtKB:Q60603, ECO:0000269|PubMed:27516594}.
CC -!- SUBUNIT: The potassium channel is composed of a homo- or
CC heterotetrameric complex of pore-forming alpha subunits that can
CC associate with modulating beta subunits (PubMed:9400421,
CC PubMed:27516594). Heteromultimer with KCNH5/EAG2 (By similarity).
CC Interacts with ALG10B (PubMed:9722534). Interacts with RABEP1
CC (PubMed:22841712). Interacts (via C-terminus) with CTTN
CC (PubMed:23144454). Interacts (via cytoplasmic region) with Ca(2+)-bound
CC calmodulin (PubMed:27516594). {ECO:0000250|UniProtKB:O95259,
CC ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:23144454,
CC ECO:0000269|PubMed:27516594, ECO:0000269|PubMed:9400421,
CC ECO:0000269|PubMed:9722534}.
CC -!- INTERACTION:
CC Q63472; O35550: Rabep1; NbExp=2; IntAct=EBI-7991592, EBI-7991542;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24495567,
CC ECO:0000269|PubMed:27516594, ECO:0000269|PubMed:7925287,
CC ECO:0000269|PubMed:9400421}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27516594}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite
CC {ECO:0000269|PubMed:24495567}. Cell projection, axon
CC {ECO:0000269|PubMed:24495567}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:25556795}. Perikaryon
CC {ECO:0000269|PubMed:24495567}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:24495567}. Early endosome membrane
CC {ECO:0000250|UniProtKB:O95259}. Note=Perinuclear KCNH1 is located to
CC NPC-free islands. {ECO:0000250|UniProtKB:O95259}.
CC -!- TISSUE SPECIFICITY: Detected in cerebellum, at parallel fiber synapses
CC on Purkinje cell spines (PubMed:25556795). Detected in hippocampus
CC neurons (at protein level) (PubMed:24495567). Detected in brain, but
CC not in the other tissues tested; expression is highest in granular
CC cells of the dentate gyrus, in hippocampus CA3 pyramidal cells, and in
CC cerebellar granule cells (PubMed:7925287). Detected in pituitary
CC (PubMed:10718922). {ECO:0000269|PubMed:10718922,
CC ECO:0000269|PubMed:24495567, ECO:0000269|PubMed:25556795,
CC ECO:0000269|PubMed:7925287}.
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. {ECO:0000269|PubMed:9400421}.
CC -!- DOMAIN: The C-terminal region interacts with the cyclic nucleotide-
CC binding domain and contributes to regulate channel gating.
CC {ECO:0000250|UniProtKB:Q60603}.
CC -!- DOMAIN: The PAS and PAC domain interact with the cyclic nucleotide-
CC binding domain and contribute to the regulation of channel gating.
CC Calmodulin binding clamps together the PAS and PAC domain with the
CC cyclic nucleotide-binding domain from a neighboring subunit and causes
CC a conformation change that leads to channel closure.
CC {ECO:0000269|PubMed:27516594}.
CC -!- DOMAIN: The cyclic nucleotide-binding domain lacks residues that are
CC essential for nucleotide-binding and cannot bind cyclic nucleotides.
CC Instead, residues from the C-terminal domain (the so-called intrinsic
CC ligand) bind in the cavity that would be expected to bind cyclic
CC nucleotides. Interaction with the C-terminal region hinders interaction
CC with CALM and reduces the affinity for CALM.
CC {ECO:0000250|UniProtKB:Q60603}.
CC -!- PTM: Channel activity is regulated via tyrosine
CC phosphorylation/dephosphorylation by SRC and PTPN6.
CC {ECO:0000250|UniProtKB:O95259}.
CC -!- SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC
CC 1.A.1.20) subfamily. Kv10.1/KCNH1 sub-subfamily. {ECO:0000305}.
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DR EMBL; Z34264; CAA84018.1; -; mRNA.
DR PIR; I53197; I53197.
DR RefSeq; NP_113930.1; NM_031742.1.
DR RefSeq; XP_006250553.1; XM_006250491.3.
DR PDB; 5K7L; EM; 3.78 A; A=1-962.
DR PDB; 6PBX; EM; 4.00 A; A/C/E/G=14-962.
DR PDB; 6PBY; EM; 3.67 A; A/C/E/G=14-962.
DR PDBsum; 5K7L; -.
DR PDBsum; 6PBX; -.
DR PDBsum; 6PBY; -.
DR AlphaFoldDB; Q63472; -.
DR SMR; Q63472; -.
DR BioGRID; 249310; 1.
DR IntAct; Q63472; 2.
DR MINT; Q63472; -.
DR ChEMBL; CHEMBL4295858; -.
DR GuidetoPHARMACOLOGY; 570; -.
DR TCDB; 1.A.1.20.4; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q63472; 2 sites.
DR iPTMnet; Q63472; -.
DR PhosphoSitePlus; Q63472; -.
DR PaxDb; Q63472; -.
DR PRIDE; Q63472; -.
DR GeneID; 65198; -.
DR KEGG; rno:65198; -.
DR CTD; 3756; -.
DR RGD; 68398; Kcnh1.
DR VEuPathDB; HostDB:ENSRNOG00000003841; -.
DR HOGENOM; CLU_005746_3_1_1; -.
DR InParanoid; Q63472; -.
DR PhylomeDB; Q63472; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:Q63472; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003841; Expressed in frontal cortex and 10 other tissues.
DR ExpressionAtlas; Q63472; baseline and differential.
DR Genevisible; Q63472; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030673; C:axolemma; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; IPI:RGD.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0001964; P:startle response; IMP:RGD.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR030170; EAG1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003949; K_chnl_volt-dep_EAG.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR10217:SF530; PTHR10217:SF530; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PRINTS; PR01464; EAGCHANNEL.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Cell membrane; Cell projection; Endosome;
KW Glycoprotein; Ion channel; Ion transport; Lipid-binding; Membrane; Nucleus;
KW Phosphoprotein; Postsynaptic cell membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..962
FT /note="Potassium voltage-gated channel subfamily H member
FT 1"
FT /id="PRO_0000053996"
FT TOPO_DOM 1..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TRANSMEM 221..241
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TOPO_DOM 242..248
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TRANSMEM 249..269
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TOPO_DOM 270..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TRANSMEM 291..309
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TOPO_DOM 310..318
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TRANSMEM 319..341
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TOPO_DOM 342..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TRANSMEM 351..372
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TOPO_DOM 373..421
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27516594"
FT INTRAMEM 422..443
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TOPO_DOM 444..450
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TRANSMEM 451..471
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000269|PubMed:27516594"
FT TOPO_DOM 472..962
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27516594"
FT DOMAIN 14..94
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT REGION 151..162
FT /note="Required for phosphatidylinositol bisphosphate
FT binding"
FT /evidence="ECO:0000250|UniProtKB:O95259"
FT REGION 646..743
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q60603"
FT REGION 672..674
FT /note="Interaction with cyclic nucleotide-binding pocket"
FT /evidence="ECO:0000250|UniProtKB:Q60603"
FT REGION 830..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..937
FT /note="CAD (involved in subunit assembly)"
FT /evidence="ECO:0000269|PubMed:9400421"
FT REGION 933..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 436..441
FT /note="Selectivity filter"
FT /evidence="ECO:0000269|PubMed:27516594"
FT COMPBIAS 830..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60603"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60603"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60603"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:27516594"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 962 AA; 108291 MW; 69DF4CE2DC435608 CRC64;
MTMAGGRRGL VAPQNTFLEN IVRRSNDTNF VLGNAQIVDW PIVYSNDGFC KLSGYHRAEV
MQKSSACSFM YGELTDKDTV EKVRQTFENY EMNSFEILMY KKNRTPVWFF VKIAPIRNEQ
DKVVLFLCTF SDITAFKQPI EDDSCKGWGK FARLTRALTS SRGVLQQLAP SVQKGENVHK
HSRLAEVLQL GSDILPQYKQ EAPKTPPHII LHYCVFKTTW DWIILILTFY TAILVPYNVS
FKTRQNNVAW LVVDSIVDVI FLVDIVLNFH TTFVGPAGEV ISDPKLIRMN YLKTWFVIDL
LSCLPYDVIN AFENVDEGIS SLFSSLKVVR LLRLGRVARK LDHYIEYGAA VLVLLVCVFG
LAAHWMACIW YSIGDYEIFD EDTKTIRNNS WLYQLALDIG TPYQFNGSGS GKWEGGPSKN
SVYISSLYFT MTSLTSVGFG NIAPSTDIEK IFAVAIMMIG SLLYATIFGN VTTIFQQMYA
NTNRYHEMLN SVRDFLKLYQ VPKGLSERVM DYIVSTWSMS RGIDTEKVLQ ICPKDMRADI
CVHLNRKVFK EHPAFRLASD GCLRALAMEF QTVHCAPGDL IYHAGESVDS LCFVVSGSLE
VIQDDEVVAI LGKGDVFGDV FWKEATLAQS CANVRALTYC DLHVIKRDAL QKVLEFYTAF
SHSFSRNLIL TYNLRKRIVF RKISDVKREE EERMKRKNEA PLILPPDHPV RRLFQRFRQQ
KEARLAAERG GRDLDDLDVE KGNALTDHTS ANHSLVKASV VTVRESPATP VSFQAASTST
VSDHAKLHAP GSECLGPKAG GGDPAKRKGW ARFKDACGKG EDWNKVSKAE SMETLPERTK
ASGEATLKKT DSCDSGITKS DLRLDNVGEA RSPQDRSPIL AEVKHSFYPI PEQTLQATVL
EVKHELKEDI KALNAKMTSI EKQLSEILRI LMSRGSSQSP QDTCEVSRPQ SPESDRDIFG
AS
