CUX2_HUMAN
ID CUX2_HUMAN Reviewed; 1486 AA.
AC O14529; A7E2Y4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Homeobox protein cut-like 2;
DE AltName: Full=Homeobox protein cux-2;
GN Name=CUX2; Synonyms=CUTL2, KIAA0293;
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 [LARGE SCALE MRNA], AND VARIANT LEU-1472.
RC TISSUE=Brain;
RX PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA Nomura N.;
RT "Construction and characterization of human brain cDNA libraries suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-1472.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP INVOLVEMENT IN DEE67, AND VARIANT DEE67 LYS-590.
RX PubMed=29630738; DOI=10.1002/ana.25222;
RA Chatron N., Moeller R.S., Champaigne N.L., Schneider A.L., Kuechler A.,
RA Labalme A., Simonet T., Baggett L., Bardel C., Kamsteeg E.J., Pfundt R.,
RA Romano C., Aronsson J., Alberti A., Vinci M., Miranda M.J., Lacroix A.,
RA Marjanovic D., des Portes V., Edery P., Wieczorek D., Gardella E.,
RA Scheffer I.E., Mefford H., Sanlaville D., Carvill G.L., Lesca G.;
RT "The epilepsy phenotypic spectrum associated with a recurrent CUX2
RT variant.";
RL Ann. Neurol. 83:926-934(2018).
RN [7]
RP INVOLVEMENT IN DEE67, AND VARIANT DEE67 LYS-590.
RX PubMed=29795476; DOI=10.1038/s41431-018-0184-5;
RA Barington M., Risom L., Ek J., Uldall P., Ostergaard E.;
RT "A recurrent de novo CUX2 missense variant associated with intellectual
RT disability, seizures, and autism spectrum disorder.";
RL Eur. J. Hum. Genet. 26:1388-1391(2018).
RN [8]
RP STRUCTURE BY NMR OF 544-631 AND 887-1125.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first, second and third CUT domains of human
RT homeobox protein CUX-2 (CUT-like 2).";
RL Submitted (OCT-2005) to the PDB data bank.
CC -!- FUNCTION: Transcription factor involved in the control of neuronal
CC proliferation and differentiation in the brain. Regulates dendrite
CC development and branching, dendritic spine formation, and
CC synaptogenesis in cortical layers II-III. Binds to DNA in a sequence-
CC specific manner. {ECO:0000250|UniProtKB:P70298}.
CC -!- INTERACTION:
CC O14529; Q93009: USP7; NbExp=2; IntAct=EBI-20889964, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000255|PROSITE-ProRule:PRU00374}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 67 (DEE67)
CC [MIM:618141]: 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. DEE67 is an autosomal dominant form characterized by
CC onset of seizures in infancy. Later onset of seizures in childhood may
CC occur in some patients. {ECO:0000269|PubMed:29630738,
CC ECO:0000269|PubMed:29795476}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA22962.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB006631; BAA22962.2; ALT_INIT; mRNA.
DR EMBL; AC005805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151245; AAI51246.1; -; mRNA.
DR CCDS; CCDS41837.1; -.
DR RefSeq; NP_056082.2; NM_015267.3.
DR PDB; 1WH6; NMR; -; A=887-974.
DR PDB; 1WH8; NMR; -; A=1028-1125.
DR PDB; 1X2L; NMR; -; A=544-631.
DR PDBsum; 1WH6; -.
DR PDBsum; 1WH8; -.
DR PDBsum; 1X2L; -.
DR AlphaFoldDB; O14529; -.
DR SMR; O14529; -.
DR BioGRID; 116907; 11.
DR IntAct; O14529; 2.
DR STRING; 9606.ENSP00000261726; -.
DR iPTMnet; O14529; -.
DR PhosphoSitePlus; O14529; -.
DR BioMuta; CUX2; -.
DR EPD; O14529; -.
DR jPOST; O14529; -.
DR MassIVE; O14529; -.
DR MaxQB; O14529; -.
DR PaxDb; O14529; -.
DR PeptideAtlas; O14529; -.
DR PRIDE; O14529; -.
DR Antibodypedia; 31073; 84 antibodies from 21 providers.
DR DNASU; 23316; -.
DR Ensembl; ENST00000261726.11; ENSP00000261726.6; ENSG00000111249.14.
DR GeneID; 23316; -.
DR KEGG; hsa:23316; -.
DR MANE-Select; ENST00000261726.11; ENSP00000261726.6; NM_015267.4; NP_056082.2.
DR UCSC; uc001tsa.4; human.
DR CTD; 23316; -.
DR DisGeNET; 23316; -.
DR GeneCards; CUX2; -.
DR HGNC; HGNC:19347; CUX2.
DR HPA; ENSG00000111249; Group enriched (brain, choroid plexus, liver, prostate).
DR MalaCards; CUX2; -.
DR MIM; 610648; gene.
DR MIM; 618141; phenotype.
DR neXtProt; NX_O14529; -.
DR OpenTargets; ENSG00000111249; -.
DR Orphanet; 2382; Lennox-Gastaut syndrome.
DR PharmGKB; PA162382977; -.
DR VEuPathDB; HostDB:ENSG00000111249; -.
DR eggNOG; KOG0963; Eukaryota.
DR eggNOG; KOG2252; Eukaryota.
DR GeneTree; ENSGT00940000160241; -.
DR HOGENOM; CLU_005104_1_0_1; -.
DR InParanoid; O14529; -.
DR OMA; QVDTAEI; -.
DR OrthoDB; 181575at2759; -.
DR PhylomeDB; O14529; -.
DR TreeFam; TF318206; -.
DR PathwayCommons; O14529; -.
DR SignaLink; O14529; -.
DR SIGNOR; O14529; -.
DR BioGRID-ORCS; 23316; 18 hits in 1091 CRISPR screens.
DR ChiTaRS; CUX2; human.
DR EvolutionaryTrace; O14529; -.
DR GenomeRNAi; 23316; -.
DR Pharos; O14529; Tbio.
DR PRO; PR:O14529; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O14529; protein.
DR Bgee; ENSG00000111249; Expressed in middle temporal gyrus and 109 other tissues.
DR ExpressionAtlas; O14529; baseline and differential.
DR Genevisible; O14529; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISS:CAFA.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:CAFA.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:CAFA.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:CAFA.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:CAFA.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:CAFA.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007614; P:short-term memory; ISS:CAFA.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 3.
DR InterPro; IPR003350; CUT_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR Pfam; PF02376; CUT; 3.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM01109; CUT; 3.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 3.
DR PROSITE; PS51042; CUT; 3.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disease variant; DNA-binding; Epilepsy;
KW Homeobox; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1486
FT /note="Homeobox protein cut-like 2"
FT /id="PRO_0000202396"
FT DNA_BIND 544..631
FT /note="CUT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 887..974
FT /note="CUT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 1038..1125
FT /note="CUT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 1168..1227
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 114..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 195..374
FT /evidence="ECO:0000255"
FT COILED 690..717
FT /evidence="ECO:0000255"
FT COMPBIAS 129..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 590
FT /note="E -> K (in DEE67; dbSNP:rs1565909334)"
FT /evidence="ECO:0000269|PubMed:29630738,
FT ECO:0000269|PubMed:29795476"
FT /id="VAR_081600"
FT VARIANT 1472
FT /note="V -> L (in dbSNP:rs6490073)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9179496"
FT /id="VAR_065096"
FT HELIX 555..568
FT /evidence="ECO:0007829|PDB:1X2L"
FT HELIX 573..579
FT /evidence="ECO:0007829|PDB:1X2L"
FT HELIX 585..593
FT /evidence="ECO:0007829|PDB:1X2L"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:1X2L"
FT HELIX 603..616
FT /evidence="ECO:0007829|PDB:1X2L"
FT HELIX 620..630
FT /evidence="ECO:0007829|PDB:1X2L"
FT HELIX 889..893
FT /evidence="ECO:0007829|PDB:1WH6"
FT HELIX 898..910
FT /evidence="ECO:0007829|PDB:1WH6"
FT TURN 911..913
FT /evidence="ECO:0007829|PDB:1WH6"
FT HELIX 916..922
FT /evidence="ECO:0007829|PDB:1WH6"
FT HELIX 928..936
FT /evidence="ECO:0007829|PDB:1WH6"
FT TURN 941..943
FT /evidence="ECO:0007829|PDB:1WH6"
FT HELIX 946..961
FT /evidence="ECO:0007829|PDB:1WH6"
FT HELIX 1037..1043
FT /evidence="ECO:0007829|PDB:1WH8"
FT HELIX 1049..1062
FT /evidence="ECO:0007829|PDB:1WH8"
FT HELIX 1067..1073
FT /evidence="ECO:0007829|PDB:1WH8"
FT HELIX 1079..1087
FT /evidence="ECO:0007829|PDB:1WH8"
FT TURN 1092..1094
FT /evidence="ECO:0007829|PDB:1WH8"
FT HELIX 1097..1111
FT /evidence="ECO:0007829|PDB:1WH8"
FT HELIX 1115..1123
FT /evidence="ECO:0007829|PDB:1WH8"
SQ SEQUENCE 1486 AA; 161677 MW; 71782EF5214D0262 CRC64;
MAANVGSMFQ YWKRFDLRRL QKELNSVASE LSARQEESEH SHKHLIELRR EFKKNVPEEI
REMVAPVLKS FQAEVVALSK RSQEAEAAFL SVYKQLIEAP DPVPVFEAAR SLDDRLQPPS
FDPSGQPRRD LHTSWKRNPE LLSPKEQREG TSPAGPTLTE GSRLPGIPGK ALLTETLLQR
NEAEKQKGLQ EVQITLAARL GEAEEKIKVL HSALKATQAE LLELRRKYDE EAASKADEVG
LIMTNLEKAN QRAEAAQREV ESLREQLASV NSSIRLACCS PQGPSGDKVN FTLCSGPRLE
AALASKDREI LRLLKDVQHL QSSLQELEEA SANQIADLER QLTAKSEAIE KLEEKLQAQS
DYEEIKTELS ILKAMKLASS TCSLPQGMAK PEDSLLIAKE AFFPTQKFLL EKPSLLASPE
EDPSEDDSIK DSLGTEQSYP SPQQLPPPPG PEDPLSPSPG QPLLGPSLGP DGTRTFSLSP
FPSLASGERL MMPPAAFKGE AGGLLVFPPA FYGAKPPTAP ATPAPGPEPL GGPEPADGGG
GGAAGPGAEE EQLDTAEIAF QVKEQLLKHN IGQRVFGHYV LGLSQGSVSE ILARPKPWRK
LTVKGKEPFI KMKQFLSDEQ NVLALRTIQV RQRGSITPRI RTPETGSDDA IKSILEQAKK
EIESQKGGEP KTSVAPLSIA NGTTPASTSE DAIKSILEQA RREMQAQQQA LLEMEVAPRG
RSVPPSPPER PSLATASQNG APALVKQEEG SGGPAQAPLP VLSPAAFVQS IIRKVKSEIG
DAGYFDHHWA SDRGLLSRPY ASVSPSLSSS SSSGYSGQPN GRAWPRGDEA PVPPEDEAAA
GAEDEPPRTG ELKAEGATAE AGARLPYYPA YVPRTLKPTV PPLTPEQYEL YMYREVDTLE
LTRQVKEKLA KNGICQRIFG EKVLGLSQGS VSDMLSRPKP WSKLTQKGRE PFIRMQLWLS
DQLGQAVGQQ PGASQASPTE PRSSPSPPPS PTEPEKSSQE PLSLSLESSK ENQQPEGRSS
SSLSGKMYSG SQAPGGIQEI VAMSPELDTY SITKRVKEVL TDNNLGQRLF GESILGLTQG
SVSDLLSRPK PWHKLSLKGR EPFVRMQLWL NDPHNVEKLR DMKKLEKKAY LKRRYGLIST
GSDSESPATR SECPSPCLQP QDLSLLQIKK PRVVLAPEEK EALRKAYQLE PYPSQQTIEL
LSFQLNLKTN TVINWFHNYR SRMRREMLVE GTQDEPDLDP SGGPGILPPG HSHPDPTPQS
PDSETEDQKP TVKELELQEG PEENSTPLTT QDKAQVRIKQ EQMEEDAEEE AGSQPQDSGE
LDKGQGPPKE EHPDPPGNDG LPKVAPGPLL PGGSTPDCPS LHPQQESEAG ERLHPDPLSF
KSASESSRCS LEVSLNSPSA ASSPGLMMSV SPVPSSSAPI SPSPPGAPPA KVPSASPTAD
MAGALHPSAK VNPNLQRRHE KMANLNNIIY RVERAANREE ALEWEF
