CPLX1_HUMAN
ID CPLX1_HUMAN Reviewed; 134 AA.
AC O14810; A6NI80; B2R4R5; D3DVN3; F1T0G1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Complexin-1;
DE AltName: Full=Complexin I;
DE Short=CPX I;
DE AltName: Full=Synaphin-2;
GN Name=CPLX1;
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].
RC TISSUE=Brain;
RX PubMed=7553862; DOI=10.1016/0092-8674(95)90239-2;
RA McMahon H.T., Missler M., Li C., Suedhof T.C.;
RT "Complexins: cytosolic proteins that regulate SNAP receptor function.";
RL Cell 83:111-119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=24722188; DOI=10.1038/ncomms4650;
RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M.,
RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I.,
RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A.,
RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D.,
RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.;
RT "Protein interaction network of alternatively spliced isoforms from brain
RT links genetic risk factors for autism.";
RL Nat. Commun. 5:3650-3650(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=9853440; DOI=10.1016/s0140-6736(98)03341-8;
RA Harrison P.J., Eastwood S.L.;
RT "Preferential involvement of excitatory neurons in medial temporal lobe in
RT schizophrenia.";
RL Lancet 352:1669-1673(1998).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11483314; DOI=10.1016/s0306-4522(01)00141-5;
RA Eastwood S.L., Cotter D., Harrison P.J.;
RT "Cerebellar synaptic protein expression in schizophrenia.";
RL Neuroscience 105:219-229(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=15526345; DOI=10.1002/pmic.200400848;
RA Basso M., Giraudo S., Corpillo D., Bergamasco B., Lopiano L., Fasano M.;
RT "Proteome analysis of human substantia nigra in Parkinson's disease.";
RL Proteomics 4:3943-3952(2004).
RN [12]
RP INVOLVEMENT IN DEE63, AND VARIANT DEE63 108-GLU--LYS-134 DEL.
RX PubMed=26539891; DOI=10.1016/j.neuron.2015.09.048;
RA Karaca E., Harel T., Pehlivan D., Jhangiani S.N., Gambin T.,
RA Coban Akdemir Z., Gonzaga-Jauregui C., Erdin S., Bayram Y., Campbell I.M.,
RA Hunter J.V., Atik M.M., Van Esch H., Yuan B., Wiszniewski W., Isikay S.,
RA Yesil G., Yuregir O.O., Tug Bozdogan S., Aslan H., Aydin H., Tos T.,
RA Aksoy A., De Vivo D.C., Jain P., Geckinli B.B., Sezer O., Gul D.,
RA Durmaz B., Cogulu O., Ozkinay F., Topcu V., Candan S., Cebi A.H., Ikbal M.,
RA Yilmaz Gulec E., Gezdirici A., Koparir E., Ekici F., Coskun S., Cicek S.,
RA Karaer K., Koparir A., Duz M.B., Kirat E., Fenercioglu E., Ulucan H.,
RA Seven M., Guran T., Elcioglu N., Yildirim M.S., Aktas D., Alikasifoglu M.,
RA Ture M., Yakut T., Overton J.D., Yuksel A., Ozen M., Muzny D.M.,
RA Adams D.R., Boerwinkle E., Chung W.K., Gibbs R.A., Lupski J.R.;
RT "Genes that affect brain structure and function identified by rare variant
RT analyses of mendelian neurologic disease.";
RL Neuron 88:499-513(2015).
RN [13]
RP INVOLVEMENT IN DEE63, AND VARIANTS DEE63 105-CYS--LYS-134 DEL AND MET-128.
RX PubMed=28422131; DOI=10.1038/ejhg.2017.52;
RA Redler S., Strom T.M., Wieland T., Cremer K., Engels H., Distelmaier F.,
RA Schaper J., Kuechler A., Lemke J.R., Jeschke S., Schreyer N., Sticht H.,
RA Koch M., Luedecke H.J., Wieczorek D.;
RT "Variants in CPLX1 in two families with autosomal-recessive severe
RT infantile myoclonic epilepsy and ID.";
RL Eur. J. Hum. Genet. 25:889-893(2017).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 28-83 ALONE AND IN COMPLEX WITH
RP SNAP25; VAMP2 AND RAT STX1A, SUBUNIT, AND FUNCTION.
RX PubMed=21785414; DOI=10.1038/nsmb.2101;
RA Kummel D., Krishnakumar S.S., Radoff D.T., Li F., Giraudo C.G., Pincet F.,
RA Rothman J.E., Reinisch K.M.;
RT "Complexin cross-links prefusion SNAREs into a zigzag array.";
RL Nat. Struct. Mol. Biol. 18:927-933(2011).
CC -!- FUNCTION: Positively regulates a late step in exocytosis of various
CC cytoplasmic vesicles, such as synaptic vesicles and other secretory
CC vesicles (PubMed:21785414). Organizes the SNAREs into a cross-linked
CC zigzag topology that, when interposed between the vesicle and plasma
CC membranes, is incompatible with fusion, thereby preventing SNAREs from
CC releasing neurotransmitters until an action potential arrives at the
CC synapse (PubMed:21785414). Also involved in glucose-induced secretion
CC of insulin by pancreatic beta-cells. Essential for motor behavior.
CC {ECO:0000250|UniProtKB:P63040, ECO:0000269|PubMed:21785414}.
CC -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A. {ECO:0000269|PubMed:21785414}.
CC -!- INTERACTION:
CC O14810; P60880-2: SNAP25; NbExp=6; IntAct=EBI-2691813, EBI-12177361;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P63040}. Perikaryon
CC {ECO:0000250|UniProtKB:P63040}. Presynapse
CC {ECO:0000250|UniProtKB:P63040}. Note=Enriched at synaptic-releasing
CC sites in mature neurons. {ECO:0000250|UniProtKB:P63040}.
CC -!- TISSUE SPECIFICITY: Nervous system. In hippocampus and cerebellum,
CC expressed mainly by inhibitory neurons. Overexpressed in substantia
CC nigra from patients with Parkinson disease.
CC {ECO:0000269|PubMed:11483314, ECO:0000269|PubMed:15526345,
CC ECO:0000269|PubMed:9853440}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 63 (DEE63)
CC [MIM:617976]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE63 is an autosomal recessive disease with onset in
CC infancy. {ECO:0000269|PubMed:26539891, ECO:0000269|PubMed:28422131}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR EMBL; AF022383; AAB72108.1; -; mRNA.
DR EMBL; KJ534815; AHW56455.1; -; mRNA.
DR EMBL; BT007029; AAP35676.1; -; mRNA.
DR EMBL; AB593095; BAJ84035.1; -; mRNA.
DR EMBL; AK311921; BAG34862.1; -; mRNA.
DR EMBL; AC139887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82648.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82649.1; -; Genomic_DNA.
DR EMBL; BC002471; AAH02471.1; -; mRNA.
DR CCDS; CCDS46995.1; -.
DR RefSeq; NP_006642.1; NM_006651.3.
DR PDB; 3RK3; X-ray; 3.50 A; E=26-83.
DR PDB; 3RL0; X-ray; 3.80 A; g/h/i/j/k/l/m/n=26-83.
DR PDBsum; 3RK3; -.
DR PDBsum; 3RL0; -.
DR AlphaFoldDB; O14810; -.
DR SMR; O14810; -.
DR BioGRID; 116028; 40.
DR CORUM; O14810; -.
DR DIP; DIP-56109N; -.
DR IntAct; O14810; 12.
DR MINT; O14810; -.
DR STRING; 9606.ENSP00000305613; -.
DR iPTMnet; O14810; -.
DR PhosphoSitePlus; O14810; -.
DR BioMuta; CPLX1; -.
DR EPD; O14810; -.
DR MassIVE; O14810; -.
DR MaxQB; O14810; -.
DR PaxDb; O14810; -.
DR PeptideAtlas; O14810; -.
DR PRIDE; O14810; -.
DR ProteomicsDB; 48251; -.
DR Antibodypedia; 22160; 178 antibodies from 26 providers.
DR DNASU; 10815; -.
DR Ensembl; ENST00000304062.11; ENSP00000305613.6; ENSG00000168993.15.
DR GeneID; 10815; -.
DR KEGG; hsa:10815; -.
DR MANE-Select; ENST00000304062.11; ENSP00000305613.6; NM_006651.4; NP_006642.1.
DR UCSC; uc003gbi.4; human.
DR CTD; 10815; -.
DR DisGeNET; 10815; -.
DR GeneCards; CPLX1; -.
DR HGNC; HGNC:2309; CPLX1.
DR HPA; ENSG00000168993; Tissue enriched (brain).
DR MalaCards; CPLX1; -.
DR MIM; 605032; gene.
DR MIM; 617976; phenotype.
DR neXtProt; NX_O14810; -.
DR OpenTargets; ENSG00000168993; -.
DR Orphanet; 352582; Familial infantile myoclonic epilepsy.
DR Orphanet; 280; Wolf-Hirschhorn syndrome.
DR PharmGKB; PA26826; -.
DR VEuPathDB; HostDB:ENSG00000168993; -.
DR eggNOG; ENOG502S3I2; Eukaryota.
DR GeneTree; ENSGT00950000182938; -.
DR InParanoid; O14810; -.
DR OMA; TPIMDIF; -.
DR OrthoDB; 1556534at2759; -.
DR PhylomeDB; O14810; -.
DR TreeFam; TF315172; -.
DR PathwayCommons; O14810; -.
DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
DR SignaLink; O14810; -.
DR BioGRID-ORCS; 10815; 7 hits in 1060 CRISPR screens.
DR GeneWiki; CPLX1; -.
DR GenomeRNAi; 10815; -.
DR Pharos; O14810; Tbio.
DR PRO; PR:O14810; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O14810; protein.
DR Bgee; ENSG00000168993; Expressed in lateral nuclear group of thalamus and 122 other tissues.
DR ExpressionAtlas; O14810; baseline and differential.
DR Genevisible; O14810; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0070554; C:synaptobrevin 2-SNAP-25-syntaxin-3-complexin complex; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; TAS:ProtInc.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0017157; P:regulation of exocytosis; TAS:ParkinsonsUK-UCL.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IBA:GO_Central.
DR DisProt; DP02360; -.
DR InterPro; IPR008849; Synaphin.
DR PANTHER; PTHR16705; PTHR16705; 1.
DR Pfam; PF05835; Synaphin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; Disease variant;
KW Epilepsy; Exocytosis; Neurotransmitter transport; Reference proteome;
KW Synapse; Transport.
FT CHAIN 1..134
FT /note="Complexin-1"
FT /id="PRO_0000144870"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..70
FT /note="Interaction with the SNARE complex"
FT /evidence="ECO:0000250"
FT REGION 74..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..69
FT /evidence="ECO:0000255"
FT COMPBIAS 18..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 105..134
FT /note="Missing (in DEE63)"
FT /evidence="ECO:0000269|PubMed:28422131"
FT /id="VAR_080795"
FT VARIANT 108..134
FT /note="Missing (in DEE63)"
FT /evidence="ECO:0000269|PubMed:26539891"
FT /id="VAR_080796"
FT VARIANT 128
FT /note="L -> M (in DEE63; unknown pathological significance;
FT dbSNP:rs371709824)"
FT /evidence="ECO:0000269|PubMed:28422131"
FT /id="VAR_080797"
FT HELIX 29..70
FT /evidence="ECO:0007829|PDB:3RK3"
SQ SEQUENCE 134 AA; 15030 MW; A7A52F17F10D28A4 CRC64;
MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE
AVRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV
IKYLPGPLQD MLKK
