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 12-OCT-2022, entry version 192. 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}; 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; 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 17 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 //