ID   SET1A_HUMAN             Reviewed;        1707 AA.
AC   O15047; A6NP62; Q6PIF3; Q8TAJ6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 3.
DT   19-MAR-2014, entry version 121.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD1A;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 2F;
DE   AltName: Full=SET domain-containing protein 1A;
DE            Short=hSET1A;
DE   AltName: Full=Set1/Ash2 histone methyltransferase complex subunit SET1;
GN   Name=SETD1A; Synonyms=KIAA0339, KMT2F, SET1, SET1A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-248 AND 1239-1707.
RC   TISSUE=Brain, and Duodenum;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH HCFC1.
RX   PubMed=12670868; DOI=10.1101/gad.252103;
RA   Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT   "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT   methyltransferase are tethered together selectively by the cell-
RT   proliferation factor HCF-1.";
RL   Genes Dev. 17:896-911(2003).
RN   [5]
RP   IDENTIFICATION IN THE SET1 COMPLEX.
RX   PubMed=16253997; DOI=10.1074/jbc.M508312200;
RA   Lee J.-H., Skalnik D.G.;
RT   "CpG-binding protein (CXXC finger protein 1) is a component of the
RT   mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue
RT   of the yeast Set1/COMPASS complex.";
RL   J. Biol. Chem. 280:41725-41731(2005).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SET1 COMPLEX.
RX   PubMed=17355966; DOI=10.1074/jbc.M609809200;
RA   Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
RT   "Identification and characterization of the human Set1B histone H3-
RT   Lys4 methyltransferase complex.";
RL   J. Biol. Chem. 282:13419-13428(2007).
RN   [8]
RP   IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH ASH2L; RBBP5;
RP   CXXC1; HCFC1; WDR5; WDR82 AND POLR2A.
RX   PubMed=17998332; DOI=10.1128/MCB.01356-07;
RA   Lee J.H., Skalnik D.G.;
RT   "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
RT   Histone H3-Lys4 methyltransferase complex to transcription start sites
RT   of transcribed human genes.";
RL   Mol. Cell. Biol. 28:609-618(2008).
RN   [9]
RP   IDENTIFICATION IN SET1 COMPLEX.
RX   PubMed=18838538; DOI=10.1128/MCB.00976-08;
RA   Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
RA   Shilatifard A.;
RT   "Molecular regulation of H3K4 trimethylation by Wdr82, a component of
RT   human Set1/COMPASS.";
RL   Mol. Cell. Biol. 28:7337-7344(2008).
RN   [10]
RP   IDENTIFICATION BY 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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [15]
RP   INTERACTION WITH ZNF335.
RX   PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
RA   Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
RA   Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
RA   Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A.,
RA   Mahajnah M., Shenhav R., Walsh C.A.;
RT   "Microcephaly gene links trithorax and REST/NRSF to control neural
RT   stem cell proliferation and differentiation.";
RL   Cell 151:1097-1112(2012).
RN   [16]
RP   INTERACTION WITH SUPT6H.
RX   PubMed=22843687; DOI=10.1074/jbc.M112.351569;
RA   Begum N.A., Stanlie A., Nakata M., Akiyama H., Honjo T.;
RT   "The histone chaperone Spt6 is required for activation-induced
RT   cytidine deaminase target determination through H3K4me3 regulation.";
RL   J. Biol. Chem. 287:32415-32429(2012).
CC   -!- FUNCTION: Histone methyltransferase that specifically methylates
CC       'Lys-4' of histone H3, when part of the SET1 histone
CC       methyltransferase (HMT) complex, but not if the neighboring 'Lys-
CC       9' residue is already methylated. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation. The non-overalpping localization with SETD1B suggests
CC       that SETD1A and SETD1B make non-redundant contributions to the
CC       epigenetic control of chromatin structure and gene expression.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBUNIT: Component of the SET1 complex, at least composed of the
CC       catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5,
CC       ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with HCFC1.
CC       Interacts with ASH2/ASH2L, CXXC1/CFP1, WDR5 and RBBP5. Interacts
CC       (via the RRM domain) with WDR82. Interacts (via the RRM domain)
CC       with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase
CC       II large subunit (POLR2A) only in the presence of WDR82. Binds
CC       specifically to CTD heptad repeats phosphorylated on 'Ser-5' of
CC       each heptad. Interacts with ZNF335. Interacts with SUPT6H.
CC   -!- INTERACTION:
CC       P51610:HCFC1; NbExp=2; IntAct=EBI-540779, EBI-396176;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle. Chromosome. Note=Localizes
CC       to a largely non-overlapping set of euchromatic nuclear speckles
CC       with SETD1B, suggesting that SETD1A and SETD1B each bind to a
CC       unique set of target genes.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH35795.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAA20797.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AB002337; BAA20797.2; ALT_INIT; mRNA.
DR   EMBL; AC135048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027450; AAH27450.1; -; mRNA.
DR   EMBL; BC035795; AAH35795.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_055527.1; NM_014712.1.
DR   RefSeq; XP_005255780.1; XM_005255723.1.
DR   UniGene; Hs.297483; -.
DR   PDB; 3S8S; X-ray; 1.30 A; A=89-197.
DR   PDB; 3UVN; X-ray; 1.79 A; B/D=1492-1502.
DR   PDB; 4EWR; X-ray; 1.50 A; C=1488-1501.
DR   PDBsum; 3S8S; -.
DR   PDBsum; 3UVN; -.
DR   PDBsum; 4EWR; -.
DR   ProteinModelPortal; O15047; -.
DR   SMR; O15047; 89-195.
DR   BioGrid; 115088; 18.
DR   DIP; DIP-33494N; -.
DR   IntAct; O15047; 5.
DR   STRING; 9606.ENSP00000262519; -.
DR   PhosphoSite; O15047; -.
DR   PaxDb; O15047; -.
DR   PRIDE; O15047; -.
DR   DNASU; 9739; -.
DR   Ensembl; ENST00000262519; ENSP00000262519; ENSG00000099381.
DR   GeneID; 9739; -.
DR   KEGG; hsa:9739; -.
DR   UCSC; uc002ead.1; human.
DR   CTD; 9739; -.
DR   GeneCards; GC16P030968; -.
DR   HGNC; HGNC:29010; SETD1A.
DR   HPA; HPA020646; -.
DR   MIM; 611052; gene.
DR   neXtProt; NX_O15047; -.
DR   PharmGKB; PA128394556; -.
DR   eggNOG; COG2940; -.
DR   HOGENOM; HOG000154291; -.
DR   HOVERGEN; HBG067119; -.
DR   InParanoid; O15047; -.
DR   KO; K11422; -.
DR   OMA; GYLRLTY; -.
DR   OrthoDB; EOG7GQXTT; -.
DR   TreeFam; TF106436; -.
DR   BRENDA; 2.1.1.43; 2681.
DR   ChiTaRS; SETD1A; human.
DR   GenomeRNAi; 9739; -.
DR   NextBio; 36651; -.
DR   PRO; PR:O15047; -.
DR   ArrayExpress; O15047; -.
DR   Bgee; O15047; -.
DR   CleanEx; HS_SETD1A; -.
DR   Genevestigator; O15047; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR015722; Histone-lysine_MeTfrase.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF10; PTHR22884:SF10; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Chromatin regulator; Chromosome;
KW   Complete proteome; Methyltransferase; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1   1707       Histone-lysine N-methyltransferase
FT                                SETD1A.
FT                                /FTId=PRO_0000186056.
FT   DOMAIN       84    172       RRM.
FT   DOMAIN     1568   1685       SET.
FT   DOMAIN     1691   1707       Post-SET.
FT   REGION     1415   1450       Interaction with CFP1.
FT   REGION     1450   1537       Interaction with ASH2L, RBBP5 and WDR5.
FT   MOTIF      1299   1303       HCFC1-binding motif (HBM).
FT   COMPBIAS    244    362       Ser-rich.
FT   COMPBIAS    383    654       Pro-rich.
FT   COMPBIAS    899   1010       Glu-rich.
FT   COMPBIAS   1011   1062       Ser-rich.
FT   COMPBIAS   1071   1194       Pro-rich.
FT   COMPBIAS   1334   1375       Glu-rich.
FT   COMPBIAS   1403   1417       Pro-rich.
FT   MOD_RES     508    508       Phosphoserine.
FT   VARIANT     639    639       D -> N (in dbSNP:rs897985).
FT                                /FTId=VAR_059318.
FT   CONFLICT    242    248       PCSQDTS -> ACPVTHV (in Ref. 3; AAH35795).
FT   CONFLICT   1240   1242       TEE -> FLG (in Ref. 3; AAH27450).
FT   STRAND       95    100
FT   HELIX       107    114
FT   TURN        115    117
FT   STRAND      120    127
FT   TURN        129    131
FT   STRAND      134    144
FT   HELIX       145    155
FT   STRAND      166    169
FT   HELIX       174    184
FT   TURN        190    192
FT   HELIX      1494   1497
SQ   SEQUENCE   1707 AA;  186034 MW;  0084217B0D425050 CRC64;
     MDQEGGGDGQ KAPSFQWRNY KLIVDPALDP ALRRPSQKVY RYDGVHFSVN DSKYIPVEDL
     QDPRCHVRSK NRDFSLPVPK FKLDEFYIGQ IPLKEVTFAR LNDNVRETFL KDMCRKYGEV
     EEVEILLHPR TRKHLGLARV LFTSTRGAKE TVKNLHLTSV MGNIIHAQLD IKGQQRMKYY
     ELIVNGSYTP QTVPTGGKAL SEKFQGSGAA TETAESRRRS SSDTAAYPAG TTAVGTPGNG
     TPCSQDTSFS SSRQDTPSSF GQFTPQSSQG TPYTSRGSTP YSQDSAYSSS TTSTSFKPRR
     SENSYQDAFS RRHFSASSAS TTASTAIAAT TAATASSSAS SSSLSSSSSS SSSSSSSQFR
     SSDANYPAYY ESWNRYQRHT SYPPRRATRE EPPGAPFAEN TAERFPPSYT SYLPPEPSRP
     TDQDYRPPAS EAPPPEPPEP GGGGGGGGPS PEREEVRTSP RPASPARSGS PAPETTNESV
     PFAQHSSLDS RIEMLLKEQR SKFSFLASDT EEEEENSSMV LGARDTGSEV PSGSGHGPCT
     PPPAPANFED VAPTGSGEPG ATRESPKANG QNQASPCSSG DDMEISDDDR GGSPPPAPTP
     PQQPPPPPPP PPPPPPYLAS LPLGYPPHQP AYLLPPRPDG PPPPEYPPPP PPPPHIYDFV
     NSLELMDRLG AQWGGMPMSF QMQTQMLTRL HQLRQGKGLI AASAGPPGGA FGEAFLPFPP
     PQEAAYGLPY ALYAQGQEGR GAYSREAYHL PMPMAAEPLP SSSVSGEEAR LPPREEAELA
     EGKTLPTAGT VGRVLAMLVQ EMKSIMQRDL NRKMVENVAF GAFDQWWESK EEKAKPFQNA
     AKQQAKEEDK EKTKLKEPGL LSLVDWAKSG GTTGIEAFAF GSGLRGALRL PSFKVKRKEP
     SEISEASEEK RPRPSTPAEE DEDDPEQEKE AGEPGRPGTK PPKRDEERGK TQGKHRKSFA
     LDSEGEEASQ ESSSEKDEED DEEDEEDEDR EEAVDTTKKE TEVSDGEDEE SDSSSKCSLY
     ADSDGENDST SDSESSSSSS SSSSSSSSSS SSSSSSSSES SSEDEEEEER PAALPSASPP
     PREVPVPTPA PVEVPVPERV AGSPVTPLPE QEASPARPAG PTEESPPSAP LRPPEPPAGP
     PAPAPRPDER PSSPIPLLPP PKKRRKTVSF SAIEVVPAPE PPPATPPQAK FPGPASRKAP
     RGVERTIRNL PLDHASLVKS WPEEVSRGGR SRAGGRGRLT EEEEAEPGTE VDLAVLADLA
     LTPARRGLPA LPAVEDSEAT ETSDEAERPR PLLSHILLEH NYALAVKPTP PAPALRPPEP
     VPAPAALFSS PADEVLEAPE VVVAEAEEPK PQQLQQQREE GEEEGEEEGE EEEEESSDSS
     SSSDGEGALR RRSLRSHARR RRPPPPPPPP PPRAYEPRSE FEQMTILYDI WNSGLDSEDM
     SYLRLTYERL LQQTSGADWL NDTHWVHHTI TNLTTPKRKR RPQDGPREHQ TGSARSEGYY
     PISKKEKDKY LDVCPVSARQ LEGVDTQGTN RVLSERRSEQ RRLLSAIGTS AIMDSDLLKL
     NQLKFRKKKL RFGRSRIHEW GLFAMEPIAA DEMVIEYVGQ NIRQMVADMR EKRYVQEGIG
     SSYLFRVDHD TIIDATKCGN LARFINHCCT PNCYAKVITI ESQKKIVIYS KQPIGVDEEI
     TYDYKFPLED NKIPCLCGTE SCRGSLN
//