ZEP2_HUMAN
ID ZEP2_HUMAN Reviewed; 2446 AA.
AC P31629; Q02646; Q5THT5; Q9NS05;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Transcription factor HIVEP2;
DE AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 2;
DE Short=HIV-EP2;
DE AltName: Full=MHC-binding protein 2;
DE Short=MBP-2;
GN Name=HIVEP2;
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 [GENOMIC DNA], AND VARIANT PRO-1538.
RX PubMed=2022670; DOI=10.1016/s0021-9258(18)93015-2;
RA Nomura N., Zhao M.-J., Nagase T., Maekawa T., Ishizaki R., Tabata S.,
RA Ishii S.;
RT "HIV-EP2, a new member of the gene family encoding the human
RT immunodeficiency virus type 1 enhancer-binding protein. Comparison with
RT HIV-EP1/PRDII-BF1/MBP-1.";
RL J. Biol. Chem. 266:8590-8594(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-1538.
RX PubMed=1409593; DOI=10.1073/pnas.89.19.8971;
RA Van't Veer L.J., Lutz P., Isselbacher K.J., Bernards R.;
RT "Structure and expression of MBP-2: a 275 kDa zinc finger protein that
RT binds to an enhancer of major histocompatibility complex class 1 genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8971-8975(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-1538.
RA Kukita Y., Komiya T., Tahira T., Asakawa S., Shimizu N., Suzuki Y.,
RA Sugano S., Hayashi K.;
RT "Characterization of the human MBP-2/HIV-EP2 gene: identification of
RT multiple promoters and alternative splicing of 5' untranslated region.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1797-1936.
RX PubMed=2247438; DOI=10.1073/pnas.87.22.8707;
RA Rustgi A.K., Van't Veer L.J., Bernards R.;
RT "Two genes encode factors with NF-kappa B- and H2TF1-like DNA-binding
RT properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8707-8710(1990).
RN [6]
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10207097; DOI=10.1128/mcb.19.5.3736;
RA Doerflinger U., Pscherer A., Moser M., Ruemmele P., Schuele R.,
RA Buettner R.;
RT "Activation of somatostatin receptor II expression by transcription factors
RT MIBP1 and SEF-2 in the murine brain.";
RL Mol. Cell. Biol. 19:3736-3747(1999).
RN [7]
RP IDENTIFICATION 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 [8]
RP INVOLVEMENT IN MRD43.
RX PubMed=23020937; DOI=10.1016/s0140-6736(12)61480-9;
RA Rauch A., Wieczorek D., Graf E., Wieland T., Endele S., Schwarzmayr T.,
RA Albrecht B., Bartholdi D., Beygo J., Di Donato N., Dufke A., Cremer K.,
RA Hempel M., Horn D., Hoyer J., Joset P., Roepke A., Moog U., Riess A.,
RA Thiel C.T., Tzschach A., Wiesener A., Wohlleber E., Zweier C., Ekici A.B.,
RA Zink A.M., Rump A., Meisinger C., Grallert H., Sticht H., Schenck A.,
RA Engels H., Rappold G., Schroeck E., Wieacker P., Riess O., Meitinger T.,
RA Reis A., Strom T.M.;
RT "Range of genetic mutations associated with severe non-syndromic sporadic
RT intellectual disability: an exome sequencing study.";
RL Lancet 380:1674-1682(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2118; SER-2297 AND SER-2301,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP INVOLVEMENT IN MRD43.
RX PubMed=26153216; DOI=10.1038/ejhg.2015.151;
RA Srivastava S., Engels H., Schanze I., Cremer K., Wieland T., Menzel M.,
RA Schubach M., Biskup S., Kreiss M., Endele S., Strom T.M., Wieczorek D.,
RA Zenker M., Gupta S., Cohen J., Zink A.M., Naidu S.;
RT "Loss-of-function variants in HIVEP2 are a cause of intellectual
RT disability.";
RL Eur. J. Hum. Genet. 24:556-561(2016).
CC -!- FUNCTION: This protein specifically binds to the DNA sequence 5'-
CC GGGACTTTCC-3' which is found in the enhancer elements of numerous viral
CC promoters such as those of SV40, CMV, or HIV1. In addition, related
CC sequences are found in the enhancer elements of a number of cellular
CC promoters, including those of the class I MHC, interleukin-2 receptor,
CC somatostatin receptor II, and interferon-beta genes. It may act in T-
CC cell activation.
CC -!- SUBUNIT: Interacts with TCF4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in brain and skeletal muscle.
CC {ECO:0000269|PubMed:10207097}.
CC -!- INDUCTION: By mitogens and phorbol ester.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 43
CC (MRD43) [MIM:616977]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD43
CC patients manifest developmental delay, intellectual disability,
CC hypotonia, and dysmorphic features. {ECO:0000269|PubMed:23020937,
CC ECO:0000269|PubMed:26153216}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88218.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA46596.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M60119; AAB88218.1; ALT_INIT; Genomic_DNA.
DR EMBL; X65644; CAA46596.1; ALT_INIT; mRNA.
DR EMBL; AF153836; AAF81365.1; -; Genomic_DNA.
DR EMBL; AL023584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M61744; AAA36202.1; -; mRNA.
DR CCDS; CCDS43510.1; -.
DR PIR; S26661; WMHUE2.
DR RefSeq; NP_006725.3; NM_006734.3.
DR RefSeq; XP_016866294.1; XM_017010805.1.
DR AlphaFoldDB; P31629; -.
DR BioGRID; 109344; 19.
DR IntAct; P31629; 18.
DR STRING; 9606.ENSP00000356575; -.
DR ChEMBL; CHEMBL4523214; -.
DR GlyGen; P31629; 23 sites, 2 O-linked glycans (23 sites).
DR iPTMnet; P31629; -.
DR PhosphoSitePlus; P31629; -.
DR BioMuta; HIVEP2; -.
DR DMDM; 83305815; -.
DR EPD; P31629; -.
DR jPOST; P31629; -.
DR MassIVE; P31629; -.
DR MaxQB; P31629; -.
DR PaxDb; P31629; -.
DR PeptideAtlas; P31629; -.
DR PRIDE; P31629; -.
DR ProteomicsDB; 54794; -.
DR Antibodypedia; 46676; 44 antibodies from 18 providers.
DR DNASU; 3097; -.
DR Ensembl; ENST00000012134.7; ENSP00000012134.2; ENSG00000010818.10.
DR Ensembl; ENST00000367603.8; ENSP00000356575.2; ENSG00000010818.10.
DR Ensembl; ENST00000367604.6; ENSP00000356576.1; ENSG00000010818.10.
DR GeneID; 3097; -.
DR KEGG; hsa:3097; -.
DR MANE-Select; ENST00000367603.8; ENSP00000356575.2; NM_006734.4; NP_006725.3.
DR UCSC; uc003qjd.4; human.
DR CTD; 3097; -.
DR DisGeNET; 3097; -.
DR GeneCards; HIVEP2; -.
DR HGNC; HGNC:4921; HIVEP2.
DR HPA; ENSG00000010818; Low tissue specificity.
DR MalaCards; HIVEP2; -.
DR MIM; 143054; gene.
DR MIM; 616977; phenotype.
DR neXtProt; NX_P31629; -.
DR OpenTargets; ENSG00000010818; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR PharmGKB; PA29298; -.
DR VEuPathDB; HostDB:ENSG00000010818; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156512; -.
DR HOGENOM; CLU_000719_0_0_1; -.
DR InParanoid; P31629; -.
DR OMA; KYPIWKV; -.
DR OrthoDB; 212048at2759; -.
DR PhylomeDB; P31629; -.
DR TreeFam; TF331837; -.
DR PathwayCommons; P31629; -.
DR SignaLink; P31629; -.
DR SIGNOR; P31629; -.
DR BioGRID-ORCS; 3097; 7 hits in 1097 CRISPR screens.
DR ChiTaRS; HIVEP2; human.
DR GeneWiki; HIVEP2; -.
DR GenomeRNAi; 3097; -.
DR Pharos; P31629; Tbio.
DR PRO; PR:P31629; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P31629; protein.
DR Bgee; ENSG00000010818; Expressed in tendon of biceps brachii and 213 other tissues.
DR Genevisible; P31629; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS: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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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; 3.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Intellectual disability; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..2446
FT /note="Transcription factor HIVEP2"
FT /id="PRO_0000047371"
FT REPEAT 2053..2056
FT /note="1"
FT REPEAT 2059..2062
FT /note="2"
FT REPEAT 2071..2074
FT /note="3"
FT REPEAT 2083..2086
FT /note="4"
FT REPEAT 2089..2092
FT /note="5"
FT REPEAT 2106..2109
FT /note="6"
FT REPEAT 2112..2115
FT /note="7"
FT REPEAT 2118..2121
FT /note="8"
FT REPEAT 2130..2133
FT /note="9"
FT REPEAT 2145..2148
FT /note="10"
FT ZN_FING 189..211
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 217..239
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1799..1821
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1827..1851
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2024..2129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2148
FT /note="10 X 4 AA tandem repeats of S-P-[RGMKC]-[RK]"
FT REGION 2242..2325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2371..2403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2423..2446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 937..943
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 30..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1900..1924
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2033..2054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2067..2111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2291..2313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00900"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 1048
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 1443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 1447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 2118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT MOD_RES 2431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHF7"
FT VARIANT 46
FT /note="R -> Q (in dbSNP:rs17072013)"
FT /id="VAR_052754"
FT VARIANT 1041
FT /note="A -> V (in dbSNP:rs34875559)"
FT /id="VAR_052755"
FT VARIANT 1293
FT /note="L -> I (in dbSNP:rs35675714)"
FT /id="VAR_052756"
FT VARIANT 1538
FT /note="L -> P (in dbSNP:rs109836)"
FT /evidence="ECO:0000269|PubMed:1409593,
FT ECO:0000269|PubMed:2022670, ECO:0000269|Ref.3"
FT /id="VAR_052757"
FT CONFLICT 2091
FT /note="R -> T (in Ref. 2; CAA46596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2446 AA; 269053 MW; 482E2C577EF9449A CRC64;
MDTGDTALGQ KATSRSGETD KASGRWRQEQ SAVIKMSTFG SHEGQRQPQI EPEQIGNTAS
AQLFGSGKLA SPSEVVQQVA EKQYPPHRPS PYSCQHSLSF PQHSLPQGVM HSTKPHQSLE
GPPWLFPGPL PSVASEDLFP FPIHGHSGGY PRKKISSLNP AYSQYSQKSI EQAEEAHKKE
HKPKKPGKYI CPYCSRACAK PSVLKKHIRS HTGERPYPCI PCGFSFKTKS NLYKHRKSHA
HAIKAGLVPF TESAVSKLDL EAGFIDVEAE IHSDGEQSTD TDEESSLFAE ASDKMSPGPP
IPLDIASRGG YHGSLEESLG GPMKVPILII PKSGIPLPNE SSQYIGPDML PNPSLNTKAD
DSHTVKQKLA LRLSEKKGQD SEPSLNLLSP HSKGSTDSGY FSRSESAEQQ ISPPNTNAKS
YEEIIFGKYC RLSPRNALSV TTTSQERAAM GRKGIMEPLP HVNTRLDVKM FEDPVSQLIP
SKGDVDPSQT SMLKSTKFNS ESRQPQIIPS SIRNEGKLYP ANFQGSNPVL LEAPVDSSPL
IRSNSVPTSS ATNLTIPPSL RGSHSFDERM TGSDDVFYPG TVGIPPQRML RRQAAFELPS
VQEGHVEVEH HGRMLKGISS SSLKEKKLSP GDRVGYDYDV CRKPYKKWED SETPKQNYRD
ISCLSSLKHG GEYFMDPVVP LQGVPSMFGT TCENRKRRKE KSVGDEEDTP MICSSIVSTP
VGIMASDYDP KLQMQEGVRS GFAMAGHENL SHGHTERFDP CRPQLQPGSP SLVSEESPSA
IDSDKMSDLG GRKPPGNVIS VIQHTNSLSR PNSFERSESA ELVACTQDKA PSPSETCDSE
ISEAPVSPEW APPGDGAESG GKPSPSQQVQ QQSYHTQPRL VRQHNIQVPE IRVTEEPDKP
EKEKEAQSKE PEKPVEEFQW PQRSETLSQL PAEKLPPKKK RLRLADMEHS SGESSFESTG
TGLSRSPSQE SNLSHSSSFS MSFEREETSK LSALPKQDEF GKHSEFLTVP AGSYSLSVPG
HHHQKEMRRC SSEQMPCPHP AEVPEVRSKS FDYGNLSHAP VSGAAASTVS PSRERKKCFL
VRQASFSGSP EISQGEVGMD QSVKQEQLEH LHAGLRSGWH HGPPAVLPPL QQEDPGKQVA
GPCPPLSSGP LHLAQPQIMH MDSQESLRNP LIQPTSYMTS KHLPEQPHLF PHQETIPFSP
IQNALFQFQY PTVCMVHLPA QQPPWWQAHF PHPFAQHPQK SYGKPSFQTE IHSSYPLEHV
AEHTGKKPAE YAHTKEQTYP CYSGASGLHP KNLLPKFPSD QSSKSTETPS EQVLQEDFAS
ANAGSLQSLP GTVVPVRIQT HVPSYGSVMY TSISQILGQN SPAIVICKVD ENMTQRTLVT
NAAMQGIGFN IAQVLGQHAG LEKYPIWKAP QTLPLGLESS IPLCLPSTSD SVATLGGSKR
MLSPASSLEL FMETKQQKRV KEEKMYGQIV EELSAVELTN SDIKKDLSRP QKPQLVRQGC
ASEPKDGLQS GSSSFSSLSP SSSQDYPSVS PSSREPFLPS KEMLSGSRAP LPGQKSSGPS
ESKESSDELD IDETASDMSM SPQSSSLPAG DGQLEEEGKG HKRPVGMLVR MASAPSGNVA
DSTLLLTDMA DFQQILQFPS LRTTTTVSWC FLNYTKPNYV QQATFKSSVY ASWCISSCNP
NPSGLNTKTT LALLRSKQKI TAEIYTLAAM HRPGTGKLTS SSAWKQFTQM KPDASFLFGS
KLERKLVGNI LKERGKGDIH GDKDIGSKQT EPIRIKIFEG GYKSNEDYVY VRGRGRGKYI
CEECGIRCKK PSMLKKHIRT HTDVRPYVCK LCNFAFKTKG NLTKHMKSKA HMKKCLELGV
SMTSVDDTET EEAENLEDLH KAAEKHSMSS ISTDHQFSDA EESDGEDGDD NDDDDEDEDD
FDDQGDLTPK TRSRSTSPQP PRFSSLPVNV GAVPHGVPSD SSLGHSSLIS YLVTLPSIRV
TQLMTPSDSC EDTQMTEYQR LFQSKSTDSE PDKDRLDIPS CMDEECMLPS EPSSSPRDFS
PSSHHSSPGY DSSPCRDNSP KRYLIPKGDL SPRRHLSPRR DLSPMRHLSP RKEAALRREM
SQRDVSPRRH LSPRRPVSPG KDITARRDLS PRRERRYMTT IRAPSPRRAL YHNPPLSMGQ
YLQAEPIVLG PPNLRRGLPQ VPYFSLYGDQ EGAYEHPGSS LFPEGPNDYV FSHLPLHSQQ
QVRAPIPMVP VGGIQMVHSM PPALSSLHPS PTLPLPMEGF EEKKGASGES FSKDPYVLSK
QHEKRGPHAL QSSGPPSTPS SPRLLMKQST SEDSLNATER EQEENIQTCT KAIASLRIAT
EEAALLGPDQ PARVQEPHQN PLGSAHVSIR HFSRPEPGQP CTSATHPDLH DGEKDNFGTS
QTPLAHSTFY SKSCVDDKQL DFHSSKELSS STEESKDPSS EKSQLH
