AFF3_HUMAN
ID AFF3_HUMAN Reviewed; 1226 AA.
AC P51826; B7ZM46; B9EGL9; D3DVI6; Q53RD6; Q53S47; Q53SI6; Q53TB9; Q59F27;
AC Q8IWJ5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=AF4/FMR2 family member 3;
DE AltName: Full=Lymphoid nuclear protein related to AF4;
DE Short=Protein LAF-4;
GN Name=AFF3 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:6473};
GN Synonyms=LAF4;
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).
RX PubMed=8555498;
RA Ma C., Staudt L.M.;
RT "LAF-4 encodes a lymphoid nuclear protein with transactivation potential
RT that is homologous to AF-4, the gene fused to MLL in t(4;11) leukemias.";
RL Blood 87:734-745(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 689-1226.
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755 AND SER-881, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
RP VARIANT VAL-1215.
RX PubMed=28397838; DOI=10.1038/mp.2017.60;
RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA Vincent J.B.;
RT "Mapping autosomal recessive intellectual disability: combined microarray
RT and exome sequencing identifies 26 novel candidate genes in 192
RT consanguineous families.";
RL Mol. Psychiatry 23:973-984(2018).
RN [9]
RP VARIANT KINS THR-233, AND INVOLVEMENT IN KINS.
RX PubMed=31388108; DOI=10.1038/s10038-019-0650-0;
RA Shimizu D., Sakamoto R., Yamoto K., Saitsu H., Fukami M., Nishimura G.,
RA Ogata T.;
RT "De novo AFF3 variant in a patient with mesomelic dysplasia with foot
RT malformation.";
RL J. Hum. Genet. 64:1041-1044(2019).
RN [10]
RP VARIANTS KINS ALA-231; LEU-231; SER-233; THR-233; VAL-233 AND GLY-235, AND
RP INVOLVEMENT IN KINS.
RX PubMed=33961779; DOI=10.1016/j.ajhg.2021.04.001;
RA Voisin N., Schnur R.E., Douzgou S., Hiatt S.M., Rustad C.F., Brown N.J.,
RA Earl D.L., Keren B., Levchenko O., Geuer S., Verheyen S., Johnson D.,
RA Zarate Y.A., Hancarova M., Amor D.J., Bebin E.M., Blatterer J., Brusco A.,
RA Cappuccio G., Charrow J., Chatron N., Cooper G.M., Courtin T., Dadali E.,
RA Delafontaine J., Del Giudice E., Doco M., Douglas G., Eisenkoelbl A.,
RA Funari T., Giannuzzi G., Gruber-Sedlmayr U., Guex N., Heron D., Holla O.L.,
RA Hurst A.C.E., Juusola J., Kronn D., Lavrov A., Lee C., Lorrain S.,
RA Merckoll E., Mikhaleva A., Norman J., Pradervand S., Prchalova D.,
RA Rhodes L., Sanders V.R., Sedlacek Z., Seebacher H.A., Sellars E.A.,
RA Sirchia F., Takenouchi T., Tanaka A.J., Taska-Tench H., Toenne E.,
RA Tveten K., Vitiello G., Vlckova M., Uehara T., Nava C., Yalcin B.,
RA Kosaki K., Donnai D., Mundlos S., Brunetti-Pierri N., Chung W.K.,
RA Reymond A.;
RT "Variants in the degron of AFF3 are associated with intellectual
RT disability, mesomelic dysplasia, horseshoe kidney, and epileptic
RT encephalopathy.";
RL Am. J. Hum. Genet. 108:857-873(2021).
CC -!- FUNCTION: Putative transcription activator that may function in
CC lymphoid development and oncogenesis. Binds, in vitro, to double-
CC stranded DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51826-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51826-2; Sequence=VSP_041120;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in lymphoid tissues,
CC highest levels being found in the thymus.
CC -!- DISEASE: KINSSHIP syndrome (KINS) [MIM:619297]: An autosomal dominant
CC disease characterized by developmental delay, impaired intellectual
CC development, seizures, short stature, mesomelic dysplasia, dysmorphic
CC facial features, horseshoe or hypoplastic kidney, and failure to
CC thrive. {ECO:0000269|PubMed:31388108, ECO:0000269|PubMed:33961779}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the AF4 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LAF4ID315.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U34360; AAA98763.1; -; mRNA.
DR EMBL; AC092667; AAY24278.1; -; Genomic_DNA.
DR EMBL; AC010736; AAY14792.1; -; Genomic_DNA.
DR EMBL; AC073118; AAY24187.1; -; Genomic_DNA.
DR EMBL; AC018690; AAY24315.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01854.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01855.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01856.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01857.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01858.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01859.1; -; Genomic_DNA.
DR EMBL; BC036895; AAH36895.1; -; mRNA.
DR EMBL; BC136579; AAI36580.1; -; mRNA.
DR EMBL; BC144266; AAI44267.1; -; mRNA.
DR EMBL; AB209634; BAD92871.1; -; mRNA.
DR CCDS; CCDS33258.1; -. [P51826-2]
DR CCDS; CCDS42723.1; -. [P51826-1]
DR RefSeq; NP_001020279.1; NM_001025108.1. [P51826-2]
DR RefSeq; NP_002276.2; NM_002285.2. [P51826-1]
DR RefSeq; XP_005264000.2; XM_005263943.3. [P51826-1]
DR RefSeq; XP_011509475.1; XM_011511173.2. [P51826-2]
DR RefSeq; XP_011509476.1; XM_011511174.2. [P51826-2]
DR RefSeq; XP_011509477.1; XM_011511175.2. [P51826-1]
DR RefSeq; XP_011509478.1; XM_011511176.2. [P51826-1]
DR RefSeq; XP_011509479.1; XM_011511177.2. [P51826-1]
DR AlphaFoldDB; P51826; -.
DR SMR; P51826; -.
DR BioGRID; 110096; 11.
DR IntAct; P51826; 6.
DR STRING; 9606.ENSP00000386834; -.
DR iPTMnet; P51826; -.
DR PhosphoSitePlus; P51826; -.
DR BioMuta; AFF3; -.
DR DMDM; 126302515; -.
DR jPOST; P51826; -.
DR MassIVE; P51826; -.
DR PaxDb; P51826; -.
DR PeptideAtlas; P51826; -.
DR PRIDE; P51826; -.
DR ProteomicsDB; 56428; -. [P51826-1]
DR ProteomicsDB; 56429; -. [P51826-2]
DR Antibodypedia; 32831; 61 antibodies from 17 providers.
DR DNASU; 3899; -.
DR Ensembl; ENST00000317233.8; ENSP00000317421.4; ENSG00000144218.21. [P51826-1]
DR Ensembl; ENST00000409236.6; ENSP00000387207.1; ENSG00000144218.21. [P51826-1]
DR Ensembl; ENST00000409579.5; ENSP00000386834.1; ENSG00000144218.21. [P51826-2]
DR Ensembl; ENST00000672756.2; ENSP00000500419.1; ENSG00000144218.21. [P51826-1]
DR GeneID; 3899; -.
DR KEGG; hsa:3899; -.
DR MANE-Select; ENST00000672756.2; ENSP00000500419.1; NM_001386135.1; NP_001373064.1.
DR UCSC; uc002tag.4; human. [P51826-1]
DR CTD; 3899; -.
DR DisGeNET; 3899; -.
DR GeneCards; AFF3; -.
DR HGNC; HGNC:6473; AFF3.
DR HPA; ENSG00000144218; Low tissue specificity.
DR MIM; 601464; gene.
DR MIM; 619297; phenotype.
DR neXtProt; NX_P51826; -.
DR OpenTargets; ENSG00000144218; -.
DR PharmGKB; PA30264; -.
DR VEuPathDB; HostDB:ENSG00000144218; -.
DR eggNOG; ENOG502QU9C; Eukaryota.
DR GeneTree; ENSGT00950000182974; -.
DR HOGENOM; CLU_006484_1_1_1; -.
DR InParanoid; P51826; -.
DR OMA; CGNSRTG; -.
DR OrthoDB; 558558at2759; -.
DR PhylomeDB; P51826; -.
DR TreeFam; TF326216; -.
DR PathwayCommons; P51826; -.
DR SignaLink; P51826; -.
DR SIGNOR; P51826; -.
DR BioGRID-ORCS; 3899; 16 hits in 1071 CRISPR screens.
DR ChiTaRS; AFF3; human.
DR GeneWiki; AFF3; -.
DR GenomeRNAi; 3899; -.
DR Pharos; P51826; Tbio.
DR PRO; PR:P51826; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P51826; protein.
DR Bgee; ENSG00000144218; Expressed in cortical plate and 171 other tissues.
DR ExpressionAtlas; P51826; baseline and differential.
DR Genevisible; P51826; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0032783; C:super elongation complex; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0034612; P:response to tumor necrosis factor; IMP:BHF-UCL.
DR InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR InterPro; IPR043639; AF4_int.
DR PANTHER; PTHR10528; PTHR10528; 1.
DR Pfam; PF18876; AF-4_C; 1.
DR Pfam; PF18875; AF4_int; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Disease variant; DNA-binding; Dwarfism;
KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1226
FT /note="AF4/FMR2 family member 3"
FT /id="PRO_0000215916"
FT REGION 24..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 18
FT /note="C -> WGEDILNQRNDSLVVEFQSSASRCRS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041120"
FT VARIANT 231
FT /note="P -> A (in KINS)"
FT /evidence="ECO:0000269|PubMed:33961779"
FT /id="VAR_085675"
FT VARIANT 231
FT /note="P -> L (in KINS)"
FT /evidence="ECO:0000269|PubMed:33961779"
FT /id="VAR_085676"
FT VARIANT 233
FT /note="A -> S (in KINS)"
FT /evidence="ECO:0000269|PubMed:33961779"
FT /id="VAR_085677"
FT VARIANT 233
FT /note="A -> T (in KINS)"
FT /evidence="ECO:0000269|PubMed:31388108,
FT ECO:0000269|PubMed:33961779"
FT /id="VAR_085678"
FT VARIANT 233
FT /note="A -> V (in KINS)"
FT /evidence="ECO:0000269|PubMed:33961779"
FT /id="VAR_085679"
FT VARIANT 235
FT /note="V -> G (in KINS)"
FT /evidence="ECO:0000269|PubMed:33961779"
FT /id="VAR_085680"
FT VARIANT 358
FT /note="N -> S (in dbSNP:rs4851223)"
FT /id="VAR_030805"
FT VARIANT 494
FT /note="N -> S (in dbSNP:rs1047265)"
FT /id="VAR_030806"
FT VARIANT 1215
FT /note="G -> V (found in a consanguineous family with
FT intellectual disability; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28397838"
FT /id="VAR_080758"
FT CONFLICT 87
FT /note="S -> T (in Ref. 1; AAA98763)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="S -> T (in Ref. 1; AAA98763)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="T -> YL (in Ref. 1; AAA98763)"
FT /evidence="ECO:0000305"
FT CONFLICT 1120
FT /note="M -> I (in Ref. 1; AAA98763)"
FT /evidence="ECO:0000305"
FT CONFLICT 1125..1127
FT /note="SPA -> FPG (in Ref. 1; AAA98763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1226 AA; 133503 MW; BD2D90358609E156 CRC64;
MDSFDLALLQ EWDLESLCVY EPDRNALRRK ERERRNQETQ QDDGTFNSSY SLFSEPYKTN
KGDELSNRIQ NTLGNYDEMK DFLTDRSNQS HLVGVPKPGV PQTPVNKIDE HFVADSRAQN
QPSSICSTTT STPAAVPVQQ SKRGTMGWQK AGHPPSDGQQ RATQQGSLRT LLGDGVGRQQ
PRAKQVCNVE VGLQTQERPP AMAAKHSSSG HCVQNFPPSL ASKPSLVQQK PTAYVRPMDG
QDQAPDESPK LKSSSETSVH CTSYRGVPAS KPEPARAKAK LSKFSIPKQG EESRSGETNS
CVEEIIREMT WLPPLSAIQA PGKVEPTKFP FPNKDSQLVS SGHNNPKKGD AEPESPDNGT
SNTSMLEDDL KLSSDEEENE QQAAQRTALR ALSDSAVVQQ PNCRTSVPSS KGSSSSSSSG
SSSSSSDSES SSGSDSETES SSSESEGSKP PHFSSPEAEP ASSNKWQLDK WLNKVNPHKP
PILIQNESHG SESNQYYNPV KEDVQDCGKV PDVCQPSLRE KEIKSTCKEE QRPRTANKAP
GSKGVKQKSP PAAVAVAVSA AAPPPAVPCA PAENAPAPAR RSAGKKPTRR TERTSAGDGA
NCHRPEEPAA ADALGTSVVV PPEPTKTRPC GNNRASHRKE LRSSVTCEKR RTRGLSRIVP
KSKEFIETES SSSSSSSDSD LESEQEEYPL SKAQTVAASA SSGNDQRLKE AAANGGSGPR
APVGSINART TSDIAKELEE QFYTLVPFGR NELLSPLKDS DEIRSLWVKI DLTLLSRIPE
HLPQEPGVLS APATKDSESA PPSHTSDTPA EKALPKSKRK RKCDNEDDYR EIKKSQGEKD
SSSRLATSTS NTLSANHCNM NINSVAIPIN KNEKMLRSPI SPLSDASKHK YTSEDLTSSS
RPNGNSLFTS ASSSKKPKAD SQLQPHGGDL TKAAHNNSEN IPLHKSRPQT KPWSPGSNGH
RDCKRQKLVF DDMPRSADYF MQEAKRMKHK ADAMVEKFGK ALNYAEAALS FIECGNAMEQ
GPMESKSPYT MYSETVELIR YAMRLKTHSG PNATPEDKQL AALCYRCLAL LYWRMFRLKR
DHAVKYSKAL IDYFKNSSKA AQAPSPWGAS GKSTGTPSPM SPNPSPASSV GSQGSLSNAS
ALSPSTIVSI PQRIHQMAAN HVSITNSILH SYDYWEMADN LAKENREFFN DLDLLMGPVT
LHSSMEHLVQ YSQQGLHWLR NSAHLS
