ID ZEP3_HUMAN Reviewed; 2406 AA. AC Q5T1R4; A7YY91; Q5T1R5; Q9BZS0; Q9HCL7; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 12-AUG-2020, entry version 148. DE RecName: Full=Transcription factor HIVEP3; DE AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 3; DE AltName: Full=Kappa-B and V(D)J recombination signal sequences-binding protein; DE AltName: Full=Kappa-binding protein 1; DE Short=KBP-1; DE AltName: Full=Zinc finger protein ZAS3; GN Name=HIVEP3; Synonyms=KBP1, KIAA1555, KRC, ZAS3; 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), FUNCTION, ALTERNATIVE SPLICING, RP DOMAIN, AND VARIANTS ARG-575; PRO-2023; ALA-2109; ARG-2272 AND ALA-2339. RC TISSUE=Brain; RX PubMed=11161801; DOI=10.1006/geno.2000.6425; RA Hicar M.D., Liu Y., Allen C.E., Wu L.-C.; RT "Structure of the human zinc finger protein HIVEP3: molecular cloning, RT expression, exon-intron structure, and comparison with paralogous genes RT HIVEP1 and HIVEP2."; RL Genomics 71:89-100(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-575; RP PRO-2023; ALA-2109 AND ALA-2339. RC TISSUE=Brain; RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-575; RP PRO-2023; ALA-2109 AND ALA-2339. 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 [6] RP VARIANT [LARGE SCALE ANALYSIS] MET-484. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role of transcription factor; binds to recognition CC signal sequences (Rss heptamer) for somatic recombination of CC immunoglobulin and T-cell receptor gene segments; Binds also to the CC kappa-B motif of gene such as S100A4, involved in cell progression and CC differentiation. Kappa-B motif is a gene regulatory element found in CC promoters and enhancers of genes involved in immunity, inflammation, CC and growth and that responds to viral antigens, mitogens, and CC cytokines. Involvement of HIVEP3 in cell growth is strengthened by the CC fact that its down-regulation promotes cell cycle progression with CC ultimate formation of multinucleated giant cells. Strongly inhibits CC TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor CC NF-kappa-B by several mechanisms: as transcription factor, by competing CC for Kappa-B motif and by repressing transcription in the nucleus; CC through a non transcriptional process, by inhibiting nuclear CC translocation of RELA by association with TRAF2, an adapter molecule in CC the tumor necrosis factor signaling, which blocks the formation of IKK CC complex. Interaction with TRAF proteins inhibits both NF-Kappa-B- CC mediated and c-Jun N-terminal kinase/JNK-mediated responses that CC include apoptosis and proinflammatory cytokine gene expression. CC Positively regulates the expression of IL2 in T-cell. Essential CC regulator of adult bone formation. {ECO:0000269|PubMed:11161801}. CC -!- SUBUNIT: Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms a CC multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms can be generated by alternative splicing CC or polyadenylation. HIVEP3L transcript may lack exon 7 leading to a CC premature codon stop. {ECO:0000269|PubMed:11161801}; CC Name=1; Synonyms=HIVEP3S; CC IsoId=Q5T1R4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5T1R4-2; Sequence=VSP_033279; CC -!- INDUCTION: By 12-O-tetradecanoylphorbol-13 acetate (TPA). CC -!- DOMAIN: The ZAS2 domain binds DNA as dimers, tetramers, and multiple of CC tetramers and readily forms highly ordred DNA-protein structures. CC {ECO:0000250}. CC -!- PTM: Phosphorylated on threonine and serine residues. {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13381.2; 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; AF278765; AAK01082.1; -; mRNA. DR EMBL; AB046775; BAB13381.2; ALT_INIT; mRNA. DR EMBL; AL445933; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC152563; AAI52564.1; -; mRNA. DR CCDS; CCDS44124.1; -. [Q5T1R4-2] DR CCDS; CCDS463.1; -. [Q5T1R4-1] DR RefSeq; NP_001121186.1; NM_001127714.2. [Q5T1R4-2] DR RefSeq; NP_078779.2; NM_024503.4. [Q5T1R4-1] DR RefSeq; XP_011540186.1; XM_011541884.2. [Q5T1R4-1] DR RefSeq; XP_016857481.1; XM_017001992.1. [Q5T1R4-1] DR RefSeq; XP_016857482.1; XM_017001993.1. [Q5T1R4-1] DR RefSeq; XP_016857483.1; XM_017001994.1. [Q5T1R4-2] DR SMR; Q5T1R4; -. DR BioGRID; 121861; 12. DR CORUM; Q5T1R4; -. DR STRING; 9606.ENSP00000361664; -. DR iPTMnet; Q5T1R4; -. DR PhosphoSitePlus; Q5T1R4; -. DR BioMuta; HIVEP3; -. DR DMDM; 74756245; -. DR EPD; Q5T1R4; -. DR jPOST; Q5T1R4; -. DR MassIVE; Q5T1R4; -. DR MaxQB; Q5T1R4; -. DR PaxDb; Q5T1R4; -. DR PeptideAtlas; Q5T1R4; -. DR PRIDE; Q5T1R4; -. DR ProteomicsDB; 64282; -. [Q5T1R4-1] DR ProteomicsDB; 64283; -. [Q5T1R4-2] DR Antibodypedia; 32189; 28 antibodies. DR Ensembl; ENST00000372583; ENSP00000361664; ENSG00000127124. [Q5T1R4-1] DR Ensembl; ENST00000372584; ENSP00000361665; ENSG00000127124. [Q5T1R4-2] DR Ensembl; ENST00000643665; ENSP00000494598; ENSG00000127124. [Q5T1R4-2] DR GeneID; 59269; -. DR KEGG; hsa:59269; -. DR UCSC; uc001cgz.5; human. [Q5T1R4-1] DR CTD; 59269; -. DR DisGeNET; 59269; -. DR EuPathDB; HostDB:ENSG00000127124.13; -. DR GeneCards; HIVEP3; -. DR HGNC; HGNC:13561; HIVEP3. DR HPA; ENSG00000127124; Tissue enhanced (brain, lymphoid tissue). DR MIM; 606649; gene. DR neXtProt; NX_Q5T1R4; -. DR OpenTargets; ENSG00000127124; -. DR PharmGKB; PA29299; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000157218; -. DR HOGENOM; CLU_000719_1_0_1; -. DR InParanoid; Q5T1R4; -. DR KO; K09239; -. DR OMA; GHQKQPK; -. DR OrthoDB; 212048at2759; -. DR PhylomeDB; Q5T1R4; -. DR TreeFam; TF331837; -. DR PathwayCommons; Q5T1R4; -. DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity. DR BioGRID-ORCS; 59269; 15 hits in 894 CRISPR screens. DR ChiTaRS; HIVEP3; human. DR GeneWiki; HIVEP3; -. DR GenomeRNAi; 59269; -. DR Pharos; Q5T1R4; Tbio. DR PRO; PR:Q5T1R4; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5T1R4; protein. DR Bgee; ENSG00000127124; Expressed in buccal mucosa cell and 194 other tissues. DR Genevisible; Q5T1R4; HS. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI. DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl. DR InterPro; IPR034729; ZF_CCHC_HIVEP. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR Pfam; PF00096; zf-C2H2; 4. DR SMART; SM00355; ZnF_C2H2; 5. DR SUPFAM; SSF57667; SSF57667; 3. DR PROSITE; PS51811; ZF_CCHC_HIVEP; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. PE 2: Evidence at transcript level; KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..2406 FT /note="Transcription factor HIVEP3" FT /id="PRO_0000331627" FT REPEAT 1964..1967 FT /note="1" FT REPEAT 1970..1973 FT /note="2" FT REPEAT 1993..1996 FT /note="3" FT REPEAT 1998..2001 FT /note="4" FT REPEAT 2067..2070 FT /note="5" FT REPEAT 2079..2082 FT /note="6" FT ZN_FING 192..214 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 220..242 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 640..670 FT /note="CCHC HIVEP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01154" FT ZN_FING 1754..1776 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1782..1806 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 192..242 FT /note="ZAS1" FT REGION 211..1074 FT /note="No DNA binding activity or transactivation activity, FT but complete prevention of TRAF-dependent NF-Kappa-B FT activation; associates with TRAF2 and JUN" FT /evidence="ECO:0000250" FT REGION 264..287 FT /note="Acidic 1" FT REGION 862..883 FT /note="Acidic 2" FT REGION 1754..1806 FT /note="ZAS2" FT REGION 1817..1872 FT /note="Acidic 3" FT REGION 2053..2148 FT /note="6 X 4 AA tandem repeats of S-P-X-[RK]" FT COILED 1442..1466 FT /evidence="ECO:0000255" FT MOTIF 903..909 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 308..334 FT /note="Ser-rich" FT COMPBIAS 378..414 FT /note="Ser-rich" FT COMPBIAS 797..819 FT /note="Ser-rich" FT COMPBIAS 844..880 FT /note="Glu/Pro-rich" FT COMPBIAS 916..948 FT /note="Ser-rich" FT COMPBIAS 1907..1936 FT /note="Ser-rich" FT VAR_SEQ 2136 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10997877, FT ECO:0000303|PubMed:15489334" FT /id="VSP_033279" FT VARIANT 35 FT /note="V -> I (in dbSNP:rs2146315)" FT /id="VAR_042910" FT VARIANT 484 FT /note="V -> M (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs780211835)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_042911" FT VARIANT 575 FT /note="H -> R (in dbSNP:rs2810566)" FT /evidence="ECO:0000269|PubMed:10997877, FT ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334" FT /id="VAR_042912" FT VARIANT 1087 FT /note="Q -> H (in dbSNP:rs17363472)" FT /id="VAR_042913" FT VARIANT 2023 FT /note="A -> P (in dbSNP:rs2483689)" FT /evidence="ECO:0000269|PubMed:10997877, FT ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334" FT /id="VAR_042914" FT VARIANT 2109 FT /note="D -> A (in dbSNP:rs2991344)" FT /evidence="ECO:0000269|PubMed:10997877, FT ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334" FT /id="VAR_042915" FT VARIANT 2272 FT /note="G -> R (in dbSNP:rs11809423)" FT /evidence="ECO:0000269|PubMed:11161801" FT /id="VAR_042916" FT VARIANT 2339 FT /note="T -> A (in dbSNP:rs9439043)" FT /evidence="ECO:0000269|PubMed:10997877, FT ECO:0000269|PubMed:11161801, ECO:0000269|PubMed:15489334" FT /id="VAR_042917" FT CONFLICT 44 FT /note="A -> P (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 94..95 FT /note="QL -> HV (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 123 FT /note="D -> S (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="P -> L (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 133..134 FT /note="FV -> LL (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 589 FT /note="R -> P (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 901 FT /note="L -> A (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 961 FT /note="S -> D (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 1034..1035 FT /note="RV -> GE (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 1048..1049 FT /note="QA -> SP (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 1110 FT /note="P -> A (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 1180 FT /note="P -> L (in Ref. 2; BAB13381 and 5; AAI52564)" FT /evidence="ECO:0000305" FT CONFLICT 1279 FT /note="T -> Q (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 1524 FT /note="T -> Q (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" FT CONFLICT 2376 FT /note="P -> S (in Ref. 1; AAK01082)" FT /evidence="ECO:0000305" SQ SEQUENCE 2406 AA; 259465 MW; AFCCFDAF87014A7D CRC64; MDPEQSVKGT KKAEGSPRKR LTKGEAIQTS VSSSVPYPGS GTAATQESPA QELLAPQPFP GPSSVLREGS QEKTGQQQKP PKRPPIEASV HISQLPQHPL TPAFMSPGKP EHLLEGSTWQ LVDPMRPGPS GSFVAPGLHP QSQLLPSHAS IIPPEDLPGV PKVFVPRPSQ VSLKPTEEAH KKERKPQKPG KYICQYCSRP CAKPSVLQKH IRSHTGERPY PCGPCGFSFK TKSNLYKHRK SHAHRIKAGL ASGMGGEMYP HGLEMERIPG EEFEEPTEGE STDSEEETSA TSGHPAELSP RPKQPLLSSG LYSSGSHSSS HERCSLSQSS TAQSLEDPPP FVEPSSEHPL SHKPEDTHTI KQKLALRLSE RKKVIDEQAF LSPGSKGSTE SGYFSRSESA EQQVSPPNTN AKSYAEIIFG KCGRIGQRTA MLTATSTQPL LPLSTEDKPS LVPLSVPRTQ VIEHITKLIT INEAVVDTSE IDSVKPRRSS LSRRSSMESP KSSLYREPLS SHSEKTKPEQ SLLSLQHPPS TAPPVPLLRS HSMPSAACTI STPHHPFRGS YSFDDHITDS EALSHSSHVF TSHPRMLKRQ PAIELPLGGE YSSEEPGPSS KDTASKPSDE VEPKESELTK KTKKGLKTKG VIYECNICGA RYKKRDNYEA HKKYYCSELQ IAKPISAGTH TSPEAEKSQI EHEPWSQMMH YKLGTTLELT PLRKRRKEKS LGDEEEPPAF ESTKSQFGSP GPSDAARNLP LESTKSPAEP SKSVPSLEGP TGFQPRTPKP GSGSESGKER RTTSKEISVI QHTSSFEKSD SLEQPSGLEG EDKPLAQFPS PPPAPHGRSA HSLQPKLVRQ PNIQVPEILV TEEPDRPDTE PEPPPKEPEK TEEFQWPQRS QTLAQLPAEK LPPKKKRLRL AEMAQSSGES SFESSVPLSR SPSQESNVSL SGSSRSASFE RDDHGKAEAP SPSSDMRPKP LGTHMLTVPS HHPHAREMRR SASEQSPNVS HSAHMTETRS KSFDYGSLSL TGPSAPAPVA PPARVAPPER RKCFLVRQAS LSRPPESELE VAPKGRQESE EPQPSSSKPS AKSSLSQISS AATSHGGPPG GKGPGQDRPP LGPTVPYTEA LQVFHHPVAQ TPLHEKPYLP PPVSLFSFQH LVQHEPGQSP EFFSTQAMSS LLSSPYSMPP LPPSLFQAPP LPLQPTVLHP GQLHLPQLMP HPANIPFRQP PSFLPMPYPT SSALSSGFFL PLQSQFALQL PGDVESHLPQ IKTSLAPLAT GSAGLSPSTE YSSDIRLPPV APPASSSAPT SAPPLALPAC PDTMVSLVVP VRVQTNMPSY GSAMYTTLSQ ILVTQSQGSS ATVALPKFEE PPSKGTTVCG ADVHEVGPGP SGLSEEQSRA FPTPYLRVPV TLPERKGTSL SSESILSLEG SSSTAGGSKR VLSPAGSLEL TMETQQQKRV KEEEASKADE KLELVKPCSV VLTSTEDGKR PEKSHLGNQG QGRRELEMLS SLSSDPSDTK EIPPLPHPAL SHGTAPGSEA LKEYPQPSGK PHRRGLTPLS VKKEDSKEQP DLPSLAPPSS LPLSETSSRP AKSQEGTDSK KVLQFPSLHT TTNVSWCYLN YIKPNHIQHA DRRSSVYAGW CISLYNPNLP GVSTKAALSL LRSKQKVSKE TYTMATAPHP EAGRLVPSSS RKPRMTEVHL PSLVSPEGQK DLARVEKEEE RRGEPEEDAP ASQRGEPARI KIFEGGYKSN EEYVYVRGRG RGKYVCEECG IRCKKPSMLK KHIRTHTDVR PYVCKHCHFA FKTKGNLTKH MKSKAHSKKC QETGVLEELE AEEGTSDDLF QDSEGREGSE AVEEHQFSDL EDSDSDSDLD EDEDEDEEES QDELSRPSSE APPPGPPHAL RADSSPILGP QPPDAPASGT EATRGSSVSE AERLTASSCS MSSQSMPGLP WLGPAPLGSV EKDTGSALSY KPVSPRRPWS PSKEAGSRPP LARKHSLTKN DSSPQRCSPA REPQASAPSP PGLHVDPGRG MGALPCGSPR LQLSPLTLCP LGRELAPRAH VLSKLEGTTD PGLPRYSPTR RWSPGQAESP PRSAPPGKWA LAGPGSPSAG EHGPGLGLDP RVLFPPAPLP HKLLSRSPET CASPWQKAES RSPSCSPGPA HPLSSRPFSA LHDFHGHILA RTEENIFSHL PLHSQHLTRA PCPLIPIGGI QMVQARPGAH PTLLPGPTAA WVSGFSGGGS DLTGAREAQE RGRWSPTESS SASVSPVAKV SKFTLSSELE GGDYPKERER TGGGPGRPPD WTPHGTGAPA EPTPTHSPCT PPDTLPRPPQ GRRAAQSWSP RLESPRAPTN PEPSATPPLD RSSSVGCLAE ASARFPARTR NLSGEPRTRQ DSPKPSGSGE PRAHPHQPED RVPPNA //