ID   CNGA2_MOUSE             Reviewed;         664 AA.
AC   Q62398; Q80XH6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   04-NOV-2026, entry version 184.
DE   RecName: Full=Cyclic nucleotide-gated channel alpha-2;
DE            Short=CNG channel alpha-2;
DE            Short=CNG-2;
DE            Short=CNG2 {ECO:0000303|PubMed:11764791};
DE   AltName: Full=Olfactory cyclic nucleotide-gated channel subunit 1;
DE            Short=OCNC1 {ECO:0000303|PubMed:11764791};
GN   Name=Cnga2 {ECO:0000303|PubMed:11764791, ECO:0000312|MGI:MGI:108040};
GN   Synonyms=Cncg2, Cncg4;
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].
RC   TISSUE=Heart;
RX   PubMed=8841933; DOI=10.1006/jmcc.1996.0136;
RA   Ruiz M.L., London B., Nadal-Ginard B.;
RT   "Cloning and characterization of an olfactory cyclic nucleotide-gated
RT   channel expressed in mouse heart.";
RL   J. Mol. Cell. Cardiol. 28:1453-1461(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
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   [5]
RP   NOMENCLATURE.
RX   PubMed=11764791; DOI=10.1126/science.294.5549.2095;
RA   Bradley J., Frings S., Yau K.W., Reed R.;
RT   "Nomenclature for ion channel subunits.";
RL   Science 294:2095-2096(2001).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=34186026; DOI=10.1016/j.neuron.2021.05.032;
RA   Koike K., Yoo S.J., Bleymehl K., Omura M., Zapiec B., Pyrski M., Blum T.,
RA   Khan M., Bai Z., Leinders-Zufall T., Mombaerts P., Zufall F.;
RT   "Danger perception and stress response through an olfactory sensor for the
RT   bacterial metabolite hydrogen sulfide.";
RL   Neuron 109:2469-2484.e7(2021).
CC   -!- FUNCTION: Pore-forming subunit of the olfactory cyclic nucleotide-gated
CC       channel. Operates in the cilia of olfactory sensory neurons where
CC       chemical stimulation of the odorant is converted to an electrical
CC       signal. Mediates odorant-induced cAMP-dependent Ca(2+) influx
CC       triggering neuron depolarization (By similarity). The rise of
CC       intracellular Ca(2+) levels potentiates the olfactory response by
CC       activating Ca(2+)-dependent Cl(-) channels, but it also serves as a
CC       negative feedback signal to desensitize the channel for rapid
CC       adaptation to odorants. Conducts cAMP- and cGMP-gated ion currents,
CC       with permeability for monovalent and divalent cations (By similarity).
CC       Also expressed in a subpopulation of sensory neurons of the main
CC       olfactory epithelium (type B cells), where it mediates Ca(2+) influx in
CC       response to hydrogen sulfide, and is required for defensive behavioral
CC       responses to this stimulus (PubMed:34186026).
CC       {ECO:0000250|UniProtKB:Q00195, ECO:0000269|PubMed:34186026}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q00195};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q00195};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:Q00195};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NH4(+)(in) = NH4(+)(out); Xref=Rhea:RHEA:28747,
CC         ChEBI:CHEBI:28938; Evidence={ECO:0000250|UniProtKB:Q00194};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Rb(+)(in) = Rb(+)(out); Xref=Rhea:RHEA:78547,
CC         ChEBI:CHEBI:49847; Evidence={ECO:0000250|UniProtKB:Q00194};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Li(+)(in) = Li(+)(out); Xref=Rhea:RHEA:78551,
CC         ChEBI:CHEBI:49713; Evidence={ECO:0000250|UniProtKB:Q00194};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cs(+)(in) = Cs(+)(out); Xref=Rhea:RHEA:78555,
CC         ChEBI:CHEBI:49547; Evidence={ECO:0000250|UniProtKB:Q00194};
CC   -!- SUBUNIT: The olfactory cyclic nucleotide-gated channel is an
CC       heterotetramer composed of CNGA2, CNGA4 and CNGB1b subunits with 2:1:1
CC       stoichiometry. {ECO:0000250|UniProtKB:Q00195}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC       {ECO:0000269|PubMed:34186026}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain mediates trimerization of
CC       CNGA subunits. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutants fail to develop conditioned place
CC       aversion to hydrogen sulfide. {ECO:0000269|PubMed:34186026}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
CC       (TC 1.A.1.5) family. CNGA2 subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; U49391; AAC52712.1; -; Genomic_DNA.
DR   EMBL; AK132574; BAE21237.1; -; mRNA.
DR   EMBL; CH466624; EDL26564.1; -; Genomic_DNA.
DR   EMBL; BC048775; AAH48775.1; -; mRNA.
DR   RefSeq; NP_031750.3; NM_007724.4.
DR   RefSeq; XP_006527824.1; XM_006527761.1.
DR   AlphaFoldDB; Q62398; -.
DR   SMR; Q62398; -.
DR   FunCoup; Q62398; 1317.
DR   STRING; 10090.ENSMUSP00000006020; -.
DR   TCDB; 1.A.1.5.4; the voltage-gated ion channel (vic) superfamily.
DR   PhosphoSitePlus; Q62398; -.
DR   SwissPalm; Q62398; -.
DR   PaxDb; 10090-ENSMUSP00000006020; -.
DR   ProteomicsDB; 285507; -.
DR   Antibodypedia; 17043; 279 antibodies from 34 providers.
DR   DNASU; 12789; -.
DR   Ensembl; ENSMPUT00000011787; ENSMPUP00000011595; ENSMPUG00000011689.
DR   Ensembl; ENSMUST00000006020.8; ENSMUSP00000006020.8; ENSMUSG00000005864.8.
DR   GeneID; 12789; -.
DR   UCSC; uc009tkk.1; mouse.
DR   AGR; MGI:108040; -.
DR   CTD; 1260; -.
DR   MGI; MGI:108040; Cnga2.
DR   VEuPathDB; HostDB:ENSMUSG00000005864; -.
DR   eggNOG; KOG0500; Eukaryota.
DR   GeneTree; ENSGT00940000155374; -.
DR   HOGENOM; CLU_005746_12_0_1; -.
DR   InParanoid; Q62398; -.
DR   OMA; AALYNWC; -.
DR   OrthoDB; 421226at2759; -.
DR   PhylomeDB; Q62398; -.
DR   Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR   BioGRID-ORCS; 12789; 1 hit in 76 CRISPR screens.
DR   PRO; PR:Q62398; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q62398; protein.
DR   Bgee; ENSMUSG00000005864; Expressed in olfactory epithelium and 33 other cell types or tissues.
DR   ExpressionAtlas; Q62398; baseline and differential.
DR   GO; GO:0060170; C:ciliary membrane; IDA:ARUK-UCL.
DR   GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; ISO:GO_Central.
DR   GO; GO:0098804; C:non-motile cilium membrane; IDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:GO_Central.
DR   GO; GO:0030553; F:cGMP binding; ISO:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0005222; F:intracellularly cAMP-activated cation channel activity; ISO:GO_Central.
DR   GO; GO:0005223; F:intracellularly cGMP-activated cation channel activity; ISO:GO_Central.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IMP:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0051899; P:membrane depolarization; ISO:GO_Central.
DR   GO; GO:0098655; P:monoatomic cation transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR   GO; GO:1904880; P:response to hydrogen sulfide; IDA:UniProtKB.
DR   GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR   GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR   GO; GO:0006814; P:sodium ion transport; ISS:UniProtKB.
DR   CDD; cd00038; CAP_ED; 1.
DR   FunFam; 2.60.120.10:FF:000002; Cyclic nucleotide gated channel alpha 1a; 1.
DR   FunFam; 1.10.287.630:FF:000001; Cyclic nucleotide-gated channel alpha 3; 1.
DR   FunFam; 1.10.287.70:FF:000030; Cyclic nucleotide-gated channel alpha 3; 1.
DR   FunFam; 1.20.5.300:FF:000002; Cyclic nucleotide-gated channel alpha 3; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.5.300; -; 1.
DR   Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR032406; CLZ_dom.
DR   InterPro; IPR050866; CNG_cation_channel.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR   PANTHER; PTHR45638:SF3; CYCLIC NUCLEOTIDE-GATED OLFACTORY CHANNEL; 1.
DR   Pfam; PF16526; CLZ; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Calmodulin-binding; cAMP;
KW   cAMP-binding; Cell membrane; Cell projection; cGMP; cGMP-binding;
KW   Coiled coil; Ion channel; Ion transport; Ligand-gated ion channel;
KW   Membrane; Nucleotide-binding; Olfaction; Reference proteome;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..664
FT                   /note="Cyclic nucleotide-gated channel alpha-2"
FT                   /id="PRO_0000219313"
FT   TOPO_DOM        1..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        147..168
FT                   /note="Helical; Name=S1"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   TOPO_DOM        169..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        179..199
FT                   /note="Helical; Name=S2"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   TOPO_DOM        200..224
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        225..243
FT                   /note="Helical; Name=S3"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   TOPO_DOM        244..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        249..267
FT                   /note="Helical; Name=S4"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   TOPO_DOM        268..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        275..298
FT                   /note="Helical; Name=S5"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   TOPO_DOM        299..321
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        322..356
FT                   /note="Helical; Name=P-helix"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   TRANSMEM        357..381
FT                   /note="Helical; Name=S6"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   TOPO_DOM        382..664
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..380
FT                   /note="Ion conduction pathway"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   REGION          339..342
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   REGION          382..458
FT                   /note="C-linker"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   REGION          462..582
FT                   /note="Cyclic nucleotide-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   COILED          599..653
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   COMPBIAS        1..10
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         522
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   BINDING         525
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   BINDING         538
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   BINDING         538
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   BINDING         539
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   BINDING         539
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   SITE            366
FT                   /note="Central gate"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   SITE            370
FT                   /note="Central gate"
FT                   /evidence="ECO:0000250|UniProtKB:P29973"
FT   CONFLICT        110
FT                   /note="T -> P (in Ref. 1; AAC52712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="V -> F (in Ref. 1; AAC52712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        540..541
FT                   /note="AN -> GT (in Ref. 1; AAC52712)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   664 AA;  76193 MW;  34F8DF3B372C0D9C CRC64;
     MMTEKSNGVK SSPANNHNHH PPPSIKANGK DDHRAGSRPQ SVAADDDTSS ELQRLAEMDT
     PRRGRGGFRR IVRLVGIIRD WANKNFREEE PRPDSFLERF RGPELQTVTT HQGDGKGDKD
     GEGKGTKKKF ELFVLDPAGD WYYRWLFVIA MPVLYNWCLL VARACFSDLQ RNYFVVWLVL
     DYFSDTVYIA DLIIRLRTGF LEQGLLVKDP KKLRDNYIHT LQFKLDVASI IPTDLIYFAV
     GIHSPEVRFN RLLHFARMFE FFDRTETRTS YPNIFRISNL VLYILVIIHW NACIYYAISK
     SIGFGVDTWV YPNITDPEYG YLAREYIYCL YWSTLTLTTI GETPPPVKDE EYLFVIFDFL
     IGVLIFATIV GNVGSMISNM NATRAEFQAK IDAVKHYMQF RKVSKDMEAK VIKWFDYLWT
     NKKTVDEREV LKNLPAKLRA EIAINVHLST LKKVRIFQDC EAGLLVELVL KLRPQVFSPG
     DYICRKGDIG KEMYIIKEGK LAVVADDGVT QYALLSAGSC FGEISILNIK GSKMGNRRTA
     NIRSLGYSDL FCLSKDDLME AVTEYPDAKK VLEERGREIL MKEGLLDENE VAASMEVDVQ
     EKLEQLETNM ETLYTRFARL LAEYTGAQQK LKQRITVLET KMKQNHEDDY LSDGINTPEP
     AVAE
//