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AF4/FMR2 family member 1 (ALL1-fused gene from chromosome 4 protein) (Protein AF-4) (Protein FEL) (Proto-oncogene AF4)

 AFF1_HUMAN              Reviewed;        1210 AA.
P51825; B4DTU1; E9PBM3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-NOV-2018, entry version 157.
RecName: Full=AF4/FMR2 family member 1;
AltName: Full=ALL1-fused gene from chromosome 4 protein;
Short=Protein AF-4;
AltName: Full=Protein FEL;
AltName: Full=Proto-oncogene AF4;
Name=AFF1; Synonyms=AF4, FEL, MLLT2, PBM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8506309; DOI=10.1073/pnas.90.10.4631;
Nakamura T., Alder H., Gu Y., Prasad R., Canaani O., Kamada N.,
Gale R.P., Lange B., Crist W.M., Nowell P.C., Croce C.M., Canaani E.;
"Genes on chromosomes 4, 9, and 19 involved in 11q23 abnormalities in
acute leukemia share sequence homology and/or common motifs.";
Proc. Natl. Acad. Sci. U.S.A. 90:4631-4635(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHROMOSOMAL TRANSLOCATION
WITH KMT2A.
PubMed=8443374;
Morrissey J., Tkachuk D.C., Milatovich A., Francke U., Link M.,
Cleary M.L.;
"A serine/proline-rich protein is fused to HRX in t(4;11) acute
leukemias.";
Blood 81:1124-1131(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
CHROMOSOMAL TRANSLOCATION WITH KMT2A.
PubMed=1423625; DOI=10.1016/0092-8674(92)90603-A;
Gu Y., Nakamura T., Alder H., Prasad R., Canaani O., Cimino G.,
Croce C.M., Canaani E.;
"The t(4;11) chromosome translocation of human acute leukemias fuses
the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene.";
Cell 71:701-708(1992).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212 AND
THR-697, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; THR-220;
SER-750 AND THR-755, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; SER-588
AND SER-750, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-750, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION IN THE SEC COMPLEX.
PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L.,
Washburn M.P., Eissenberg J.C., Shilatifard A.;
"The little elongation complex regulates small nuclear RNA
transcription.";
Mol. Cell 44:954-965(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-697, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
REVIEW ON THE SUPER ELONGATION COMPLEX.
PubMed=22895430; DOI=10.1038/nrm3417;
Luo Z., Lin C., Shilatifard A.;
"The super elongation complex (SEC) family in transcriptional
control.";
Nat. Rev. Mol. Cell Biol. 13:543-547(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-750, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
STRUCTURE BY NMR OF 738-779 IN COMPLEX WITH MLLT3.
PubMed=23260655; DOI=10.1016/j.str.2012.11.011;
Leach B.I., Kuntimaddi A., Schmidt C.R., Cierpicki T., Johnson S.A.,
Bushweller J.H.;
"Leukemia fusion target AF9 is an intrinsically disordered
transcriptional regulator that recruits multiple partners via coupled
folding and binding.";
Structure 21:176-183(2013).
[17]
VARIANT [LARGE SCALE ANALYSIS] LYS-1204.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- SUBUNIT: Component of the super elongation complex (SEC), at least
composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the
P-TEFb complex and ELL (ELL, ELL2 or ELL3).
{ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23260655}.
-!- INTERACTION:
P42568:MLLT3; NbExp=7; IntAct=EBI-2610180, EBI-716132;
P04608:tat (xeno); NbExp=3; IntAct=EBI-2610180, EBI-6164389;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P51825-1; Sequence=Displayed;
Name=2;
IsoId=P51825-2; Sequence=VSP_046095, VSP_046096;
Note=No experimental confirmation available.;
Name=3;
IsoId=P51825-3; Sequence=VSP_046096;
-!- DISEASE: Note=A chromosomal aberration involving AFF1 is
associated with acute leukemias. Translocation t(4;11)(q21;q23)
with KMT2A/MLL1. The result is a rogue activator protein.
-!- SIMILARITY: Belongs to the AF4 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA36642.1; Type=Frameshift; Positions=897, 905, 1178; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AF4ID3.html";
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EMBL; L13773; AAA58360.1; -; mRNA.
EMBL; L25050; AAA36642.1; ALT_FRAME; mRNA.
EMBL; AK300364; BAG62103.1; -; mRNA.
EMBL; AC092658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS3616.1; -. [P51825-1]
CCDS; CCDS54775.1; -. [P51825-2]
PIR; A58198; A58198.
PIR; I39410; I39410.
RefSeq; NP_001160165.1; NM_001166693.2. [P51825-2]
RefSeq; NP_001300888.1; NM_001313959.1. [P51825-3]
RefSeq; NP_001300889.1; NM_001313960.1.
RefSeq; NP_005926.1; NM_005935.3. [P51825-1]
RefSeq; XP_005263064.1; XM_005263007.3. [P51825-2]
RefSeq; XP_011530275.1; XM_011531973.2. [P51825-2]
UniGene; Hs.480190; -.
PDB; 2LM0; NMR; -; A=738-779.
PDBsum; 2LM0; -.
ProteinModelPortal; P51825; -.
SMR; P51825; -.
BioGrid; 110445; 43.
CORUM; P51825; -.
DIP; DIP-56407N; -.
IntAct; P51825; 24.
MINT; P51825; -.
STRING; 9606.ENSP00000378578; -.
iPTMnet; P51825; -.
PhosphoSitePlus; P51825; -.
BioMuta; AFF1; -.
DMDM; 1703194; -.
EPD; P51825; -.
MaxQB; P51825; -.
PaxDb; P51825; -.
PeptideAtlas; P51825; -.
PRIDE; P51825; -.
ProteomicsDB; 56427; -.
Ensembl; ENST00000307808; ENSP00000305689; ENSG00000172493. [P51825-1]
Ensembl; ENST00000395146; ENSP00000378578; ENSG00000172493. [P51825-2]
GeneID; 4299; -.
KEGG; hsa:4299; -.
UCSC; uc003hqj.5; human. [P51825-1]
CTD; 4299; -.
DisGeNET; 4299; -.
EuPathDB; HostDB:ENSG00000172493.20; -.
GeneCards; AFF1; -.
HGNC; HGNC:7135; AFF1.
HPA; HPA069947; -.
MalaCards; AFF1; -.
MIM; 159557; gene.
neXtProt; NX_P51825; -.
OpenTargets; ENSG00000172493; -.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
PharmGKB; PA30851; -.
eggNOG; ENOG410IGJB; Eukaryota.
eggNOG; ENOG410XRXU; LUCA.
GeneTree; ENSGT00530000063217; -.
HOGENOM; HOG000246991; -.
HOVERGEN; HBG004189; -.
InParanoid; P51825; -.
KO; K15184; -.
OMA; MAMFRYK; -.
OrthoDB; EOG091G0KKW; -.
PhylomeDB; P51825; -.
TreeFam; TF326216; -.
SIGNOR; P51825; -.
ChiTaRS; AFF1; human.
GeneWiki; AFF1; -.
GenomeRNAi; 4299; -.
PRO; PR:P51825; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000172493; Expressed in 249 organ(s), highest expression level in placenta.
CleanEx; HS_AFF1; -.
ExpressionAtlas; P51825; baseline and differential.
Genevisible; P51825; HS.
GO; GO:0032783; C:ELL-EAF complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
InterPro; IPR007797; TF_AF4/FMR2.
PANTHER; PTHR10528; PTHR10528; 1.
Pfam; PF05110; AF-4; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Chromosomal rearrangement; Complete proteome; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome.
CHAIN 1 1210 AF4/FMR2 family member 1.
/FTId=PRO_0000215910.
COMPBIAS 483 492 Poly-Ser.
COMPBIAS 835 843 Poly-Ser.
COMPBIAS 866 869 Poly-Pro.
COMPBIAS 871 874 Poly-Ser.
MOD_RES 199 199 Phosphoserine.
{ECO:0000250|UniProtKB:O88573}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 681 681 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 697 697 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:21406692}.
MOD_RES 750 750 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 755 755 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 1 5 MAAQS -> MAFTERVNSSGN (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046095.
VAR_SEQ 1096 1096 A -> AR (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8443374}.
/FTId=VSP_046096.
VARIANT 209 209 P -> A (in dbSNP:rs3733378).
/FTId=VAR_020370.
VARIANT 1204 1204 Q -> K (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036130.
CONFLICT 46 46 K -> R (in Ref. 2; AAA36642).
{ECO:0000305}.
CONFLICT 624 624 E -> G (in Ref. 2; AAA36642).
{ECO:0000305}.
CONFLICT 762 762 M -> V (in Ref. 3; BAG62103).
{ECO:0000305}.
CONFLICT 820 820 R -> G (in Ref. 3; BAG62103).
{ECO:0000305}.
CONFLICT 899 905 SASSTKS -> VPAVPRV (in Ref. 2; AAA36642).
{ECO:0000305}.
CONFLICT 928 929 EH -> AD (in Ref. 2; AAA36642).
{ECO:0000305}.
CONFLICT 999 999 I -> N (in Ref. 2; AAA36642).
{ECO:0000305}.
CONFLICT 1140 1140 N -> I (in Ref. 2; AAA36642).
{ECO:0000305}.
TURN 768 770 {ECO:0000244|PDB:2LM0}.
SEQUENCE 1210 AA; 131422 MW; F0E334DF8FC2FF04 CRC64;
MAAQSSLYND DRNLLRIREK ERRNQEAHQE KEAFPEKIPL FGEPYKTAKG DELSSRIQNM
LGNYEEVKEF LSTKSHTHRL DASENRLGKP KYPLIPDKGS SIPSSSFHTS VHHQSIHTPA
SGPLSVGNIS HNPKMAQPRT EPMPSLHAKS CGPPDSQHLT QDRLGQEGFG SSHHKKGDRR
ADGDHCASVT DSAPERELSP LISLPSPVPP LSPIHSNQQT LPRTQGSSKV HGSSNNSKGY
CPAKSPKDLA VKVHDKETPQ DSLVAPAQPP SQTFPPPSLP SKSVAMQQKP TAYVRPMDGQ
DQAPSESPEL KPLPEDYRQQ TFEKTDLKVP AKAKLTKLKM PSQSVEQTYS NEVHCVEEIL
KEMTHSWPPP LTAIHTPSTA EPSKFPFPTK DSQHVSSVTQ NQKQYDTSSK THSNSQQGTS
SMLEDDLQLS DSEDSDSEQT PEKPPSSSAP PSAPQSLPEP VASAHSSSAE SESTSDSDSS
SDSESESSSS DSEENEPLET PAPEPEPPTT NKWQLDNWLT KVSQPAAPPE GPRSTEPPRR
HPESKGSSDS ATSQEHSESK DPPPKSSSKA PRAPPEAPHP GKRSCQKSPA QQEPPQRQTV
GTKQPKKPVK ASARAGSRTS LQGEREPGLL PYGSRDQTSK DKPKVKTKGR PRAAASNEPK
PAVPPSSEKK KHKSSLPAPS KALSGPEPAK DNVEDRTPEH FALVPLTESQ GPPHSGSGSR
TSGCRQAVVV QEDSRKDRLP LPLRDTKLLS PLRDTPPPQS LMVKITLDLL SRIPQPPGKG
SRQRKAEDKQ PPAGKKHSSE KRSSDSSSKL AKKRKGEAER DCDNKKIRLE KEIKSQSSSS
SSSHKESSKT KPSRPSSQSS KKEMLPPPPV SSSSQKPAKP ALKRSRREAD TCGQDPPKSA
SSTKSNHKDS SIPKQRRVEG KGSRSSSEHK GSSGDTANPF PVPSLPNGNS KPGKPQVKFD
KQQADLHMRE AKKMKQKAEL MTDRVGKAFK YLEAVLSFIE CGIATESESQ SSKSAYSVYS
ETVDLIKFIM SLKSFSDATA PTQEKIFAVL CMRCQSILNM AMFRCKKDIA IKYSRTLNKH
FESSSKVAQA PSPCIASTGT PSPLSPMPSP ASSVGSQSSA GSVGSSGVAA TISTPVTIQN
MTSSYVTITS HVLTAFDLWE QAEALTRKNK EFFARLSTNV CTLALNSSLV DLVHYTRQGF
QQLQELTKTP


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