ID   SET1_CAEEL              Reviewed;        1507 AA.
AC   Q18221; Q95QU6; Q95QU7;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Histone-lysine N-methyltransferase set-2;
DE            EC=2.1.1.354 {ECO:0000250|UniProtKB:P38827};
DE   AltName: Full=SET domain-containing protein 2;
GN   Name=set-2; ORFNames=C26E6.9;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=11729150; DOI=10.1093/genetics/159.3.1019;
RA   Xu L., Strome S.;
RT   "Depletion of a novel SET-domain protein enhances the sterility of mes-3
RT   and mes-4 mutants of Caenorhabditis elegans.";
RL   Genetics 159:1019-1029(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=12242227; DOI=10.1093/genetics/162.1.113;
RA   Colaiacovo M.P., Stanfield G.M., Reddy K.C., Reinke V., Kim S.K.,
RA   Villeneuve A.M.;
RT   "A targeted RNAi screen for genes involved in chromosome morphogenesis and
RT   nuclear organization in the Caenorhabditis elegans germline.";
RL   Genetics 162:113-128(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=12724425; DOI=10.1128/mcb.23.10.3681-3691.2003;
RA   Jedrusik M.A., Schulze E.;
RT   "Telomeric position effect variegation in Saccharomyces cerevisiae by
RT   Caenorhabditis elegans linker histones suggests a mechanistic connection
RT   between germ line and telomeric silencing.";
RL   Mol. Cell. Biol. 23:3681-3691(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=17967446; DOI=10.1016/j.ydbio.2007.09.035;
RA   Simonet T., Dulermo R., Schott S., Palladino F.;
RT   "Antagonistic functions of SET-2/SET1 and HPL/HP1 proteins in C. elegans
RT   development.";
RL   Dev. Biol. 312:367-383(2007).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=20555324; DOI=10.1038/nature09195;
RA   Greer E.L., Maures T.J., Hauswirth A.G., Green E.M., Leeman D.S.,
RA   Maro G.S., Han S., Banko M.R., Gozani O., Brunet A.;
RT   "Members of the H3K4 trimethylation complex regulate lifespan in a
RT   germline-dependent manner in C. elegans.";
RL   Nature 466:383-387(2010).
RN   [7]
RP   FUNCTION.
RX   PubMed=22012258; DOI=10.1038/nature10572;
RA   Greer E.L., Maures T.J., Ucar D., Hauswirth A.G., Mancini E., Lim J.P.,
RA   Benayoun B.A., Shi Y., Brunet A.;
RT   "Transgenerational epigenetic inheritance of longevity in Caenorhabditis
RT   elegans.";
RL   Nature 479:365-371(2011).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH WDR-5.1.
RX   PubMed=21527717; DOI=10.1073/pnas.1019290108;
RA   Xiao Y., Bedet C., Robert V.J., Simonet T., Dunkelbarger S.,
RA   Rakotomalala C., Soete G., Korswagen H.C., Strome S., Palladino F.;
RT   "Caenorhabditis elegans chromatin-associated proteins SET-2 and ASH-2 are
RT   differentially required for histone H3 Lys 4 methylation in embryos and
RT   adult germ cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:8305-8310(2011).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25124442; DOI=10.1126/science.1255885;
RA   Zuryn S., Ahier A., Portoso M., White E.R., Morin M.C., Margueron R.,
RA   Jarriault S.;
RT   "Sequential histone-modifying activities determine the robustness of
RT   transdifferentiation.";
RL   Science 345:826-829(2014).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28379943; DOI=10.1038/nature21686;
RA   Han S., Schroeder E.A., Silva-Garcia C.G., Hebestreit K., Mair W.B.,
RA   Brunet A.;
RT   "Mono-unsaturated fatty acids link H3K4me3 modifiers to C. elegans
RT   lifespan.";
RL   Nature 544:185-190(2017).
RN   [11] {ECO:0000305}
RP   IDENTIFICATION IN THE SET2 COMPLEX.
RX   PubMed=31602465; DOI=10.1093/nar/gkz880;
RA   Beurton F., Stempor P., Caron M., Appert A., Dong Y., Chen R.A., Cluet D.,
RA   Coute Y., Herbette M., Huang N., Polveche H., Spichty M., Bedet C.,
RA   Ahringer J., Palladino F.;
RT   "Physical and functional interaction between SET1/COMPASS complex component
RT   CFP-1 and a Sin3S HDAC complex in C. elegans.";
RL   Nucleic Acids Res. 47:11164-11180(2019).
CC   -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC       specifically mono-, di- and trimethylates histone H3 to form
CC       H3K4me1/2/3 (PubMed:21527717, PubMed:20555324). Binds RNAs which might
CC       negatively affect its histone methyltransferase activity (By
CC       similarity). COMPASS recognizes ubiquitinated H2B on one face of the
CC       nucleosome which stimulates the methylation of H3 on the opposing face
CC       (By similarity). H3 'Lys-4' methylation represents a specific tag for
CC       epigenetic transcriptional activation (PubMed:21527717). Implicated in
CC       the epigenetic inheritance of lifespan over several generations
CC       (PubMed:22012258). Acts in the germline to limit the longevity of the
CC       soma, probably by regulating a lipid metabolism pathway that signals
CC       from the germline to the intestine, thereby preventing accumulation of
CC       mono-unsaturated fatty acids (PubMed:20555324, PubMed:28379943).
CC       Methylation in the germline is required for germline development and
CC       fertility, possibly by ensuring genome stability (PubMed:21527717,
CC       PubMed:12242227). May act redundantly with mes-3 and mes-4 proteins in
CC       the development of a fertile germline (PubMed:11729150). Required for
CC       RNAi (PubMed:17967446). Functions as an antagonist of hpl-1 and hpl-2
CC       activity in growth and somatic gonad development (PubMed:17967446).
CC       Cooperates with jmjd-3.1 and egl-27 to ensure robust
CC       transdifferentiation of the Y rectal cell to the PDA motor neuron
CC       during larval development (PubMed:25124442).
CC       {ECO:0000250|UniProtKB:P38827, ECO:0000269|PubMed:11729150,
CC       ECO:0000269|PubMed:12242227, ECO:0000269|PubMed:12724425,
CC       ECO:0000269|PubMed:17967446, ECO:0000269|PubMed:20555324,
CC       ECO:0000269|PubMed:21527717, ECO:0000269|PubMed:22012258,
CC       ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:28379943}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC         COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC         Evidence={ECO:0000250|UniProtKB:P38827};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC         = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC         COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000269|PubMed:20555324, ECO:0000269|PubMed:21527717};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3]
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60272, Rhea:RHEA-
CC         COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC         ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:20555324,
CC         ECO:0000269|PubMed:21527717};
CC   -!- SUBUNIT: Component of the Set1C/COMPASS complex (also known as the SET2
CC       complex), which contains at least set-2, swd-2.1, cfp-1, rbbp-5,
CC       wdr-5.1, dpy-30 and ash-2. {ECO:0000269|PubMed:31602465}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11729150}.
CC       Note=Localized in mitotic and mid-late-stage meiotic nuclei but is
CC       undetectable in early pachytene nuclei.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a; Synonyms=L;
CC         IsoId=Q18221-1; Sequence=Displayed;
CC       Name=b; Synonyms=S;
CC         IsoId=Q18221-2; Sequence=VSP_007217, VSP_007218;
CC       Name=c;
CC         IsoId=Q18221-3; Sequence=VSP_038347;
CC   -!- TISSUE SPECIFICITY: Expressed in all cells of embryo. In L1 larva, it
CC       is predominantly expressed in Z2 and Z3 primordial germ cells. In
CC       adults, it is predominantly expressed in the germline.
CC       {ECO:0000269|PubMed:11729150}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in disruption of
CC       invariant Y-to-PDA transdifferentiation (PubMed:25124442). Results in
CC       decreased trimethylation at 'Lys-4' of histone H3 (PubMed:20555324).
CC       Leads to an extension of lifespan (PubMed:20555324). Leads to a
CC       deregulation of fat metabolism and to an enrichment of mono-unsaturated
CC       fatty acids (PubMed:28379943). {ECO:0000269|PubMed:20555324,
CC       ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:28379943}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR   EMBL; FO080680; CCD65735.1; -; Genomic_DNA.
DR   EMBL; FO080680; CCD65734.1; -; Genomic_DNA.
DR   EMBL; FO080680; CCD65736.1; -; Genomic_DNA.
DR   PIR; A88445; A88445.
DR   RefSeq; NP_498039.1; NM_065638.3. [Q18221-3]
DR   RefSeq; NP_498040.1; NM_065639.4. [Q18221-1]
DR   RefSeq; NP_498041.1; NM_065640.3. [Q18221-2]
DR   AlphaFoldDB; Q18221; -.
DR   SMR; Q18221; -.
DR   BioGRID; 40896; 4.
DR   ELM; Q18221; -.
DR   STRING; 6239.C26E6.9c.1; -.
DR   EPD; Q18221; -.
DR   PaxDb; 6239-C26E6-9c; -.
DR   PeptideAtlas; Q18221; -.
DR   EnsemblMetazoa; C26E6.9a.1; C26E6.9a.1; WBGene00004782. [Q18221-1]
DR   EnsemblMetazoa; C26E6.9b.1; C26E6.9b.1; WBGene00004782. [Q18221-2]
DR   EnsemblMetazoa; C26E6.9c.1; C26E6.9c.1; WBGene00004782. [Q18221-3]
DR   GeneID; 175662; -.
DR   KEGG; cel:CELE_C26E6.9; -.
DR   UCSC; C26E6.9a; c. elegans. [Q18221-1]
DR   AGR; WB:WBGene00004782; -.
DR   WormBase; C26E6.9a; CE27735; WBGene00004782; set-2. [Q18221-1]
DR   WormBase; C26E6.9b; CE01158; WBGene00004782; set-2. [Q18221-2]
DR   WormBase; C26E6.9c; CE27736; WBGene00004782; set-2. [Q18221-3]
DR   eggNOG; KOG1080; Eukaryota.
DR   GeneTree; ENSGT00940000169211; -.
DR   InParanoid; Q18221; -.
DR   OMA; YCTIPPK; -.
DR   OrthoDB; 5490909at2759; -.
DR   Reactome; R-CEL-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-CEL-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   PRO; PR:Q18221; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00004782; Expressed in germ line (C elegans) and 8 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IDA:WormBase.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0060290; P:transdifferentiation; IMP:WormBase.
DR   CDD; cd19169; SET_SETD1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR044570; Set1-like.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR037841; SET_SETD1A/B.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Developmental protein;
KW   Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN           1..1507
FT                   /note="Histone-lysine N-methyltransferase set-2"
FT                   /id="PRO_0000097695"
FT   DOMAIN          128..199
FT                   /note="RRM"
FT   DOMAIN          1368..1485
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          1491..1507
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..1058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1163..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1340..1345
FT                   /note="RxxxRR motif"
FT                   /evidence="ECO:0000250|UniProtKB:P38827"
FT   COMPBIAS        293..319
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..519
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..564
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..823
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..866
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..941
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..973
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1048
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1164..1179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1484
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   VAR_SEQ         1..768
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_007217"
FT   VAR_SEQ         769..831
FT                   /note="MDELSRKVAEDIRQQIMRQCFAALDEKLHLKAIADEEKRKKEREEKARQEAE
FT                   KPSNHLIADMM -> MYNNSAPYLNHSSLNTVRKKVVTVRRVLPSLPPPPPPPPSLYPP
FT                   CSVFKVPYIPQRVYRSINS (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_007218"
FT   VAR_SEQ         831
FT                   /note="M -> MPSQ (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038347"
SQ   SEQUENCE   1507 AA;  171683 MW;  E7D9689DA720C34A CRC64;
     MSTHDMNHHP PRKSHSKRDK PSSSNSGPKI ENHKCKWAWQ KVFETGKSFL RRDGFPQDCK
     SKEDFERIKR TGVRKTSENM LEDPRKNFES LQQSSVYQTN SFRNPRYLCR AHLRVDSYYC
     TIPPKREVSL FNMDDNCTEV LLRDFAKDCG KVEKAYVCIH PETKRHMKMA YVKFATVKEA
     HNFYSMYHAQ NLLATKCTPR IDPFLSILNE EYEVATNGQV LPILPDDLAS IDPSVLRDLR
     ANFLRDQNEK YELAMRNTYE DEGGMLSGVI MDTSDHYERD YTMDHDVGPS SMKMSPIPPP
     PIKEESPPPP PPPPVASVSN LAPVPSVQLP YYNNIQPSSS TMHMPEFRPT EPPPSYSRED
     PYRSTSRSSL SRHRNRSRSP SDGMDRSGRS SSRRTHRRPE SRNGSKNANG DVVKYETYKM
     EKRKIKYEGG NKKYEQVHIK ERTAVIRGKN QLENVSSESA SGSSSVDTYP DFSDEERKKK
     KRPKSPNRSK KDSRAFGWDS TDESDEDTRR RRSGRSQNRS SERKFQTTSS SSTRRELSST
     HTNSVPNLKS HETPPPPPPK GHPSVHLQTP YQHVQPQMIP ATYYNLPPQH MAPPPITTSL
     PPFCDFSQPP PGFTPTFKPI TNAPLPTPYQ ASNIPQPGLV QIAALSAAPE PFSSIPGPPP
     GPAPIQEDVG RAESPEKPSL SERFSGIFGP TQREEPAQVE VEYDYPLKHS ESHDDRHSLE
     DMDVEVSSDG ETVSNVEKIE CMEEKKRQDL ERIAIARTPI VKKCKKRMMD ELSRKVAEDI
     RQQIMRQCFA ALDEKLHLKA IADEEKRKKE REEKARQEAE KPSNHLIADM MTLYNNQSFA
     SSSRGFYRKQ KPIPKSHPKH QEHHHHAKAS VSTPVHSSST SRNSSVAPTP QRTVSTSSSS
     SSAATSARVS EDESDSDSTP GEVQRRKTSV LSNDKRRRRA SFSSTSIQSS PERQRDVSSS
     SRTSSSSSTS SMKQEETADE KSRKRKLIMS SDESSTTGST ATSVVSSRQS SLEPQQEKTD
     GEPPKKKSQT DFISERVSKI EGEERPLPEP VETSGPIIGD SSYLPYKIVH WEKAGIIEMN
     LPANSIRAHE YHPFTTEHCY FGIDDPRQPK IQIFDHSPCK SEPGSEPLKI TPAPWGPIDN
     VAETGPLIYM DVVTAPKTVQ KKQKPRKQVF EKDPYEYYEP PPTKRPAPPP RFKKTFKPRS
     EEEKKKIIGD CEDLPDLEDQ WYLRAALNEM QSEVKSADEL PWKKMLTFKE MLRSEDPLLR
     LNPIRSKKGL PDAFYEDEEL DGVIPVAAGC SRARPYEKMT MKQKRSLVRR PDNESHPTAI
     FSERDETAIR HQHLASKDMR LLQRRLLTSL GDANNDFFKI NQLKFRKKMI KFARSRIHGW
     GLYAMESIAP DEMIVEYIGQ TIRSLVAEER EKAYERRGIG SSYLFRIDLH HVIDATKRGN
     FARFINHSCQ PNCYAKVLTI EGEKRIVIYS RTIIKKGEEI TYDYKFPIED DKIDCLCGAK
     TCRGYLN
//