RLF_HUMAN
ID RLF_HUMAN Reviewed; 1914 AA.
AC Q13129; Q14CQ1; Q9NU60;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Zinc finger protein Rlf;
DE AltName: Full=Rearranged L-myc fusion gene protein;
DE AltName: Full=Zn-15-related protein;
GN Name=RLF;
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].
RX PubMed=8545128;
RA Makela T.P., Hellsten E., Vesa J., Hirvonen H., Palotie A., Peltonen L.,
RA Alitalo K.;
RT "The rearranged L-myc fusion gene (RLF) encodes a Zn-15 related zinc finger
RT protein.";
RL Oncogene 11:2699-2704(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [4]
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-839 AND LYS-1599, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-839, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-839; LYS-1599 AND LYS-1611, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-622; LYS-839; LYS-1423; LYS-1599;
RP LYS-1611; LYS-1696 AND LYS-1762, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBUNIT: Interacts with RIT1 and RIT2. {ECO:0000250}.
CC -!- INTERACTION:
CC Q13129; Q92963: RIT1; NbExp=3; IntAct=EBI-958266, EBI-365845;
CC Q13129; P70425: Rit2; Xeno; NbExp=2; IntAct=EBI-958266, EBI-2649620;
CC Q13129; PRO_0000045603 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-958266, EBI-6927928;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues.
CC -!- MISCELLANEOUS: In some small cell lung carcinoma (SCLC) cell lines,
CC there is an intrachromosomal rearrangements at 1p32 fusing the first
CC exon of the RLF gene with L-myc.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U22377; AAC50396.1; -; mRNA.
DR EMBL; AL050341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113666; AAI13667.1; -; mRNA.
DR CCDS; CCDS448.1; -.
DR PIR; S21662; S21662.
DR RefSeq; NP_036553.2; NM_012421.3.
DR AlphaFoldDB; Q13129; -.
DR BioGRID; 111950; 47.
DR IntAct; Q13129; 26.
DR MINT; Q13129; -.
DR STRING; 9606.ENSP00000361857; -.
DR iPTMnet; Q13129; -.
DR PhosphoSitePlus; Q13129; -.
DR BioMuta; RLF; -.
DR DMDM; 62296764; -.
DR EPD; Q13129; -.
DR jPOST; Q13129; -.
DR MassIVE; Q13129; -.
DR MaxQB; Q13129; -.
DR PaxDb; Q13129; -.
DR PeptideAtlas; Q13129; -.
DR PRIDE; Q13129; -.
DR ProteomicsDB; 59179; -.
DR Antibodypedia; 46843; 39 antibodies from 13 providers.
DR DNASU; 6018; -.
DR Ensembl; ENST00000372771.5; ENSP00000361857.4; ENSG00000117000.9.
DR GeneID; 6018; -.
DR KEGG; hsa:6018; -.
DR MANE-Select; ENST00000372771.5; ENSP00000361857.4; NM_012421.4; NP_036553.2.
DR UCSC; uc001cfc.5; human.
DR CTD; 6018; -.
DR DisGeNET; 6018; -.
DR GeneCards; RLF; -.
DR HGNC; HGNC:10025; RLF.
DR HPA; ENSG00000117000; Tissue enhanced (bone).
DR MIM; 180610; gene.
DR neXtProt; NX_Q13129; -.
DR OpenTargets; ENSG00000117000; -.
DR PharmGKB; PA34398; -.
DR VEuPathDB; HostDB:ENSG00000117000; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00950000183034; -.
DR HOGENOM; CLU_000520_0_0_1; -.
DR InParanoid; Q13129; -.
DR OMA; SMFQHRY; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q13129; -.
DR TreeFam; TF350813; -.
DR PathwayCommons; Q13129; -.
DR SignaLink; Q13129; -.
DR SIGNOR; Q13129; -.
DR BioGRID-ORCS; 6018; 28 hits in 1083 CRISPR screens.
DR ChiTaRS; RLF; human.
DR GeneWiki; RLF_(gene); -.
DR GenomeRNAi; 6018; -.
DR Pharos; Q13129; Tdark.
DR PRO; PR:Q13129; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13129; protein.
DR Bgee; ENSG00000117000; Expressed in secondary oocyte and 203 other tissues.
DR Genevisible; Q13129; HS.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1914
FT /note="Zinc finger protein Rlf"
FT /id="PRO_0000047325"
FT ZN_FING 582..604
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 671..696
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 714..736
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 742..766
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 771..795
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 801..825
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 954..979
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1127..1152
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1172..1195
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1310..1335
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1362..1387
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1407..1432
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1444..1469
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1549..1574
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 521..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1620..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1783..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 839
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1423
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1599
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1762
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 668
FT /note="R -> K (in dbSNP:rs35189918)"
FT /id="VAR_052739"
FT VARIANT 932
FT /note="V -> A (in dbSNP:rs35563960)"
FT /id="VAR_052740"
FT VARIANT 957
FT /note="G -> D (in dbSNP:rs35042446)"
FT /id="VAR_052741"
FT VARIANT 1629
FT /note="P -> L (in dbSNP:rs34123123)"
FT /id="VAR_061929"
FT VARIANT 1685
FT /note="Q -> E (in dbSNP:rs34141181)"
FT /id="VAR_061930"
FT VARIANT 1784
FT /note="E -> D (in dbSNP:rs10889205)"
FT /id="VAR_052742"
FT CONFLICT 1546..1548
FT /note="HTQ -> LSL (in Ref. 1; AAC50396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1914 AA; 217953 MW; 105C85C645563999 CRC64;
MADGKGDAAA VAGAGAEAPA VAGAGDGVET ESMVRGHRPV SPAPGASGLR PCLWQLETEL
REQEVSEVSS LNYCRSFCQT LLQYASNKNA SEHIVYLLEV YRLAIQSFAS ARPYLTTECE
DVLLVLGRLV LSCFELLLSV SESELPCEVW LPFLQSLQES HDALLEFGNN NLQILVHVTK
EGVWKNPVLL KILSQQPVET EEVNKLIAQE GPSFLQMRIK HLLKSNCIPQ ATALSKLCAE
SKEISNVSSF QQAYITCLCS MLPNEDAIKE IAKVDCKEVL DIICNLESEG QDNTAFVLCT
TYLTQQLQTA SVYCSWELTL FWSKLQRRID PSLDTFLERC RQFGVIAKTQ QHLFCLIRVI
QTEAQDAGLG VSILLCVRAL QLRSSEDEEM KASVCKTIAC LLPEDLEVRR ACQLTEFLIE
PSLDGFNMLE ELYLQPDQKF DEENAPVPNS LRCELLLALK AHWPFDPEFW DWKTLKRHCH
QLLGQEASDS DDDLSGYEMS INDTDVLESF LSDYDEGKED KQYRRRDLTD QHKEKRDKKP
IGSSERYQRW LQYKFFCLLC KRECIEARIL HHSKMHMEDG IYTCPVCIKK FKRKEMFVPH
VMEHVKMPPS RRDRSKKKLL LKGSQKGICP KSPSAIPEQN HSLNDQAKGE SHEYVTFSKL
EDCHLQDRDL YPCPGTDCSR VFKQFKYLSV HLKAEHQNND ENAKHYLDMK NRREKCTYCR
RHFMSAFHLR EHEQVHCGPQ PYMCVSIDCY ARFGSVNELL NHKQKHDDLR YKCELNGCNI
VFSDLGQLYH HEAQHFRDAS YTCNFLGCKK FYYSKIEYQN HLSMHNVENS NGDIKKSVKL
EESATGEKQD CINQPHLLNQ TDKSHLPEDL FCAESANSQI DTETAENLKE NSDSNSSDQL
SHSSSASMNE ELIDTLDHSE TMQDVLLSNE KVFGPSSLKE KCSSMAVCFD GTKFTCGFDG
CGSTYKNARG MQKHLRKVHP YHFKPKKIKT KDLFPSLGNE HNQTTEKLDA EPKPCSDTNS
DSPDEGLDHN IHIKCKREHQ GYSSESSICA SKRPCTEDTM LELLLRLKHL SLKNSITHGS
FSGSLQGYPS SGAKSLQSVS SISDLNFQNQ DENMPSQYLA QLAAKPFFCE LQGCKYEFVT
REALLMHYLK KHNYSKEKVL QLTMFQHRYS PFQCHICQRS FTRKTHLRIH YKNKHQIGSD
RATHKLLDNE KCDHEGPCSV DRLKGDCSAE LGGDPSSNSE KPHCHPKKDE CSSETDLESS
CEETESKTSD ISSPIGSHRE EQEGREGRGS RRTVAKGNLC YILNKYHKPF HCIHKTCNSS
FTNLKGLIRH YRTVHQYNKE QLCLEKDKAR TKRELVKCKK IFACKYKECN KRFLCSKALA
KHCSDSHNLD HIEEPKVLSE AGSAARFSCN QPQCPAVFYT FNKLKHHLME QHNIEGEIHS
DYEIHCDLNG CGQIFTHRSN YSQHVYYRHK DYYDDLFRSQ KVANERLLRS EKVCQTADTQ
GHEHQTTRRS FNAKSKKCGL IKEKKAPISF KTRAEALHMC VEHSEHTQYP CMVQGCLSVV
KLESSIVRHY KRTHQMSSAY LEQQMENLVV CVKYGTKIKE EPPSEADPCI KKEENRSCES
ERTEHSHSPG DSSAPIQNTD CCHSSERDGG QKGCIESSSV FDADTLLYRG TLKCNHSSKT
TSLEQCNIVQ PPPPCKIENS IPNPNGTESG TYFTSFQLPL PRIKESETRQ HSSGQENTVK
NPTHVPKENF RKHSQPRSFD LKTYKPMGFE SSFLKFIQES EEKEDDFDDW EPSEHLTLSN
SSQSSNDLTG NVVANNMVND SEPEVDIPHS SSDSTIHENL TAIPPLIVAE TTTVPSLENL
RVVLDKALTD CGELALKQLH YLRPVVVLER SKFSTPILDL FPTKKTDELC VGSS
