NPAS4_HUMAN
ID NPAS4_HUMAN Reviewed; 802 AA.
AC Q8IUM7; B7ZL81; Q8N8S5; Q8N9Q9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Neuronal PAS domain-containing protein 4 {ECO:0000305};
DE Short=Neuronal PAS4 {ECO:0000305};
DE AltName: Full=Class E basic helix-loop-helix protein 79 {ECO:0000305};
DE Short=bHLHe79 {ECO:0000305};
DE AltName: Full=HLH-PAS transcription factor NXF {ECO:0000303|PubMed:14701734};
DE AltName: Full=PAS domain-containing protein 10 {ECO:0000305};
GN Name=NPAS4 {ECO:0000312|HGNC:HGNC:18983};
GN Synonyms=BHLHE79 {ECO:0000312|HGNC:HGNC:18983},
GN NXF {ECO:0000303|PubMed:14701734}, PASD10 {ECO:0000312|HGNC:HGNC:18983};
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] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=14701734; DOI=10.1128/mcb.24.2.608-616.2004;
RA Ooe N., Saito K., Mikami N., Nakatuka I., Kaneko H.;
RT "Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals
RT a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton
RT modulator drebrin gene expression.";
RL Mol. Cell. Biol. 24:608-616(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 VARIANTS SER-147; CYS-208; LYS-257; ARG-293; ARG-296; LEU-317; ALA-344;
RP ILE-359; SER-472; LYS-500; MET-587; ASP-702; TYR-750 AND ILE-777,
RP CHARACTERIZATION OF VARIANTS SER-147; CYS-208; LYS-257; ARG-293; ARG-296;
RP LEU-317; ALA-344; ILE-359; SER-472; LYS-500; MET-587; ASP-702; TYR-750 AND
RP ILE-777, AND SUBUNIT.
RX PubMed=24465693; DOI=10.1371/journal.pone.0085768;
RA Bersten D.C., Bruning J.B., Peet D.J., Whitelaw M.L.;
RT "Human variants in the neuronal basic helix-loop-helix/Per-Arnt-Sim
RT (bHLH/PAS) transcription factor complex NPAS4/ARNT2 disrupt function.";
RL PLoS ONE 9:E85768-E85768(2014).
CC -!- FUNCTION: Transcription factor expressed in neurons of the brain that
CC regulates the excitatory-inhibitory balance within neural circuits and
CC is required for contextual memory in the hippocampus (By similarity).
CC Plays a key role in the structural and functional plasticity of neurons
CC (By similarity). Acts as an early-response transcription factor in both
CC excitatory and inhibitory neurons, where it induces distinct but
CC overlapping sets of late-response genes in these two types of neurons,
CC allowing the synapses that form on inhibitory and excitatory neurons to
CC be modified by neuronal activity in a manner specific to their function
CC within a circuit, thereby facilitating appropriate circuit responses to
CC sensory experience (By similarity). In excitatory neurons, activates
CC transcription of BDNF, which in turn controls the number of GABA-
CC releasing synapses that form on excitatory neurons, thereby promoting
CC an increased number of inhibitory synapses on excitatory neurons (By
CC similarity). In inhibitory neurons, regulates a distinct set of target
CC genes that serve to increase excitatory input onto somatostatin
CC neurons, probably resulting in enhanced feedback inhibition within
CC cortical circuits (By similarity). The excitatory and inhibitory
CC balance in neurons affects a number of processes, such as short-term
CC and long-term memory, acquisition of experience, fear memory, response
CC to stress and social behavior (By similarity). Acts as a regulator of
CC dendritic spine development in olfactory bulb granule cells in a
CC sensory-experience-dependent manner by regulating expression of MDM2
CC (By similarity). Efficient DNA binding requires dimerization with
CC another bHLH protein, such as ARNT, ARNT2 or BMAL1 (PubMed:14701734).
CC Can activate the CME (CNS midline enhancer) element (PubMed:14701734).
CC {ECO:0000250|UniProtKB:Q8BGD7, ECO:0000269|PubMed:14701734}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein (PubMed:14701734, PubMed:24465693). Heterodimer; forms a
CC heterodimer with ARNT, ARNT2 or BMAL1 (PubMed:14701734,
CC PubMed:24465693). {ECO:0000269|PubMed:14701734,
CC ECO:0000269|PubMed:24465693}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BGD7,
CC ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IUM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IUM7-3; Sequence=VSP_056596, VSP_056597;
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:14701734}.
CC -!- PTM: Ubiquitinated, leading to degradation by the proteosome.
CC {ECO:0000250|UniProtKB:Q8BGD7}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04271.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB049469; BAC19830.1; -; mRNA.
DR EMBL; AK094025; BAC04271.1; ALT_FRAME; mRNA.
DR EMBL; AK096253; BAC04738.1; -; mRNA.
DR EMBL; AP001107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC105001; AAI05002.1; -; mRNA.
DR EMBL; BC105003; AAI05004.1; -; mRNA.
DR EMBL; BC143630; AAI43631.1; -; mRNA.
DR CCDS; CCDS8138.1; -. [Q8IUM7-1]
DR RefSeq; NP_001305733.1; NM_001318804.1.
DR RefSeq; NP_849195.2; NM_178864.3. [Q8IUM7-1]
DR RefSeq; XP_016873028.1; XM_017017539.1. [Q8IUM7-3]
DR AlphaFoldDB; Q8IUM7; -.
DR SMR; Q8IUM7; -.
DR BioGRID; 129335; 5.
DR IntAct; Q8IUM7; 1.
DR STRING; 9606.ENSP00000311196; -.
DR PhosphoSitePlus; Q8IUM7; -.
DR BioMuta; NPAS4; -.
DR DMDM; 74714317; -.
DR PaxDb; Q8IUM7; -.
DR PeptideAtlas; Q8IUM7; -.
DR PRIDE; Q8IUM7; -.
DR ProteomicsDB; 70585; -. [Q8IUM7-1]
DR ProteomicsDB; 7213; -.
DR Antibodypedia; 30154; 209 antibodies from 31 providers.
DR DNASU; 266743; -.
DR Ensembl; ENST00000311034.7; ENSP00000311196.2; ENSG00000174576.10. [Q8IUM7-1]
DR Ensembl; ENST00000525148.1; ENSP00000433135.1; ENSG00000174576.10. [Q8IUM7-3]
DR Ensembl; ENST00000639555.1; ENSP00000492526.1; ENSG00000174576.10. [Q8IUM7-3]
DR GeneID; 266743; -.
DR KEGG; hsa:266743; -.
DR MANE-Select; ENST00000311034.7; ENSP00000311196.2; NM_178864.4; NP_849195.2.
DR UCSC; uc001ohx.2; human. [Q8IUM7-1]
DR CTD; 266743; -.
DR DisGeNET; 266743; -.
DR GeneCards; NPAS4; -.
DR HGNC; HGNC:18983; NPAS4.
DR HPA; ENSG00000174576; Tissue enriched (brain).
DR MIM; 608554; gene.
DR neXtProt; NX_Q8IUM7; -.
DR OpenTargets; ENSG00000174576; -.
DR PharmGKB; PA142671254; -.
DR VEuPathDB; HostDB:ENSG00000174576; -.
DR eggNOG; ENOG502QRXX; Eukaryota.
DR GeneTree; ENSGT00530000064165; -.
DR HOGENOM; CLU_013890_0_0_1; -.
DR InParanoid; Q8IUM7; -.
DR OMA; KTYFTQE; -.
DR OrthoDB; 219290at2759; -.
DR PhylomeDB; Q8IUM7; -.
DR TreeFam; TF319684; -.
DR PathwayCommons; Q8IUM7; -.
DR SignaLink; Q8IUM7; -.
DR BioGRID-ORCS; 266743; 26 hits in 1094 CRISPR screens.
DR ChiTaRS; NPAS4; human.
DR GenomeRNAi; 266743; -.
DR Pharos; Q8IUM7; Tbio.
DR PRO; PR:Q8IUM7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8IUM7; protein.
DR Bgee; ENSG00000174576; Expressed in pituitary gland and 87 other tissues.
DR Genevisible; Q8IUM7; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071386; P:cellular response to corticosterone stimulus; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007614; P:short-term memory; ISS:UniProtKB.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR CDD; cd00130; PAS; 2.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Differentiation; DNA-binding;
KW Neurogenesis; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..802
FT /note="Neuronal PAS domain-containing protein 4"
FT /id="PRO_0000248222"
FT DOMAIN 1..53
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 70..144
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 203..273
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 278..317
FT /note="PAC"
FT REGION 1..13
FT /note="Basic motif; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 14..53
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 466..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..38
FT /evidence="ECO:0000255"
FT COILED 624..648
FT /evidence="ECO:0000255"
FT COMPBIAS 529..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 234
FT /note="V -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056596"
FT VAR_SEQ 235..802
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056597"
FT VARIANT 147
FT /note="F -> S (decreased transcription factor activity due
FT to impaired interaction with ARNT2; dbSNP:rs79072452)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076845"
FT VARIANT 208
FT /note="G -> C (does not affect the transcription factor
FT activity; dbSNP:rs905768)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076846"
FT VARIANT 257
FT /note="E -> K (decreased transcription factor activity;
FT dbSNP:rs375915619)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076847"
FT VARIANT 293
FT /note="W -> R (does not affect the transcription factor
FT activity; dbSNP:rs200310338)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076848"
FT VARIANT 296
FT /note="C -> R (likely benign variant; does not affect the
FT transcription factor activity)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076849"
FT VARIANT 317
FT /note="M -> L (does not affect the transcription factor
FT activity; dbSNP:rs76159120)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076850"
FT VARIANT 344
FT /note="P -> A (does not affect the transcription factor
FT activity; dbSNP:rs140299985)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076851"
FT VARIANT 359
FT /note="T -> I (does not affect the transcription factor
FT activity; dbSNP:rs145746289)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076852"
FT VARIANT 472
FT /note="P -> S (does not affect the transcription factor
FT activity; dbSNP:rs150700317)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076853"
FT VARIANT 500
FT /note="Q -> K (does not affect the transcription factor
FT activity; dbSNP:rs71457718)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076854"
FT VARIANT 587
FT /note="T -> M (does not affect the transcription factor
FT activity; dbSNP:rs142965018)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076855"
FT VARIANT 702
FT /note="N -> D (does not affect the transcription factor
FT activity; dbSNP:rs147463475)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076856"
FT VARIANT 750
FT /note="D -> Y (does not affect the transcription factor
FT activity; dbSNP:rs139929410)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076857"
FT VARIANT 777
FT /note="T -> I (does not affect the transcription factor
FT activity; dbSNP:rs111848728)"
FT /evidence="ECO:0000269|PubMed:24465693"
FT /id="VAR_076858"
FT CONFLICT 72
FT /note="Q -> R (in Ref. 2; BAC04738)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="E -> K (in Ref. 2; BAC04738)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="L -> H (in Ref. 2; BAC04738)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="D -> G (in Ref. 2; BAC04271)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="G -> E (in Ref. 2; BAC04271)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="E -> K (in Ref. 2; BAC04271)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="T -> A (in Ref. 2; BAC04271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 802 AA; 87117 MW; 0F5CB6486D0813F0 CRC64;
MYRSTKGASK ARRDQINAEI RNLKELLPLA EADKVRLSYL HIMSLACIYT RKGVFFAGGT
PLAGPTGLLS AQELEDIVAA LPGFLLVFTA EGKLLYLSES VSEHLGHSMV DLVAQGDSIY
DIIDPADHLT VRQQLTLPSA LDTDRLFRCR FNTSKSLRRQ SAGNKLVLIR GRFHAHPPGA
YWAGNPVFTA FCAPLEPRPR PGPGPGPGPA SLFLAMFQSR HAKDLALLDI SESVLIYLGF
ERSELLCKSW YGLLHPEDLA HASAQHYRLL AESGDIQAEM VVRLQAKTGG WAWIYCLLYS
EGPEGPITAN NYPISDMEAW SLRQQLNSED TQAAYVLGTP TMLPSFPENI LSQEECSSTN
PLFTAALGAP RSTSFPSAPE LSVVSASEEL PRPSKELDFS YLTFPSGPEP SLQAELSKDL
VCTPPYTPHQ PGGCAFLFSL HEPFQTHLPT PSSTLQEQLT PSTATFSDQL TPSSATFPDP
LTSPLQGQLT ETSVRSYEDQ LTPCTSTFPD QLLPSTATFP EPLGSPAHEQ LTPPSTAFQA
HLDSPSQTFP EQLSPNPTKT YFAQEGCSFL YEKLPPSPSS PGNGDCTLLA LAQLRGPLSV
DVPLVPEGLL TPEASPVKQS FFHYSEKEQN EIDRLIQQIS QLAQGMDRPF SAEAGTGGLE
PLGGLEPLDS NLSLSGAGPP VLSLDLKPWK CQELDFLADP DNMFLEETPV EDIFMDLSTP
DPSEEWGSGD PEAEGPGGAP SPCNNLSPED HSFLEDLATY ETAFETGVSA FPYDGFTDEL
HQLQSQVQDS FHEDGSGGEP TF
