ID ZBT49_HUMAN Reviewed; 765 AA. AC Q6ZSB9; A8K936; Q32ML0; Q59FJ4; Q5EBN0; Q8TB80; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 27-MAR-2024, entry version 177. DE RecName: Full=Zinc finger and BTB domain-containing protein 49; DE AltName: Full=Zinc finger protein 509; GN Name=ZBTB49; Synonyms=ZNF509; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). 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 MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 265-765 (ISOFORM 2), AND VARIANTS ALA-556 AND RP VAL-642. RC TISSUE=Lymph, and Ovary; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-765. RC TISSUE=Brain; 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 [5] RP FUNCTION (ISOFORMS 1 AND 3), INTERACTION WITH EP300 AND KAT5 (ISOFORM 1), RP INTERACTION WITH ZBTB17 (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING (ISOFORMS RP 1; 3; 4 AND 5), SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TISSUE RP SPECIFICITY, AND INDUCTION BY ETOPOSIDE. RX PubMed=25245946; DOI=10.1093/nar/gku857; RA Jeon B.N., Kim M.K., Yoon J.H., Kim M.Y., An H., Noh H.J., Choi W.I., RA Koh D.I., Hur M.W.; RT "Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating RT transcription of p21/CDKN1A and RB upon exposure to genotoxic stress."; RL Nucleic Acids Res. 42:11447-11461(2014). CC -!- FUNCTION: Transcription factor. Inhibits cell proliferation by CC activating either CDKN1A/p21 transcription or RB1 transcription. CC {ECO:0000269|PubMed:25245946}. CC -!- FUNCTION: [Isoform 1]: Binds CDKN1A promoter and activates its CC transcription; this activity is further potentiated in the presence of CC EP300 (synergistic) and ZBTB17/Miz-1 (additive). CC {ECO:0000269|PubMed:25245946}. CC -!- FUNCTION: [Isoform 3]: Activates RB1 transcription most probably by CC antagonizing ZBTB17 repression of RB1. Does not bind directly RB1 CC promoter. {ECO:0000269|PubMed:25245946}. CC -!- SUBUNIT: Isoform 1 interacts with EP300 and KAT5/Tip60. The interaction CC with EP300 is direct and leads to synergistic induction of CDKN1A. On CC the CDKN1A promoter, forms a complex with ZBTB17/Miz-1; this CC interaction leads to additive CDKN1A transactivation. Isoform 3 also CC interacts with ZBTB17; this interaction may block ZBTB17 repressor CC activity. {ECO:0000269|PubMed:25245946}. CC -!- INTERACTION: CC Q6ZSB9; P13637: ATP1A3; NbExp=3; IntAct=EBI-2859943, EBI-948169; CC Q6ZSB9; Q8NHQ1: CEP70; NbExp=5; IntAct=EBI-2859943, EBI-739624; CC Q6ZSB9; Q99828: CIB1; NbExp=3; IntAct=EBI-2859943, EBI-372594; CC Q6ZSB9; Q9HD26: GOPC; NbExp=5; IntAct=EBI-2859943, EBI-349832; CC Q6ZSB9; Q9HD26-2: GOPC; NbExp=3; IntAct=EBI-2859943, EBI-11102276; CC Q6ZSB9; P16284: PECAM1; NbExp=3; IntAct=EBI-2859943, EBI-716404; CC Q6ZSB9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2859943, EBI-79165; CC Q6ZSB9; Q12933: TRAF2; NbExp=3; IntAct=EBI-2859943, EBI-355744; CC Q6ZSB9; Q13114: TRAF3; NbExp=3; IntAct=EBI-2859943, EBI-357631; CC Q6ZSB9; Q08AM6: VAC14; NbExp=3; IntAct=EBI-2859943, EBI-2107455; CC Q6ZSB9; P40337-2: VHL; NbExp=3; IntAct=EBI-2859943, EBI-12157263; CC Q6ZSB9; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-2859943, EBI-2515601; CC Q6ZSB9; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-2859943, EBI-742740; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000269|PubMed:25245946}. Nucleus {ECO:0000269|PubMed:25245946}. CC Note=Predominantly located in the nucleus. CC {ECO:0000269|PubMed:25245946}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm CC {ECO:0000269|PubMed:25245946}. Nucleus {ECO:0000269|PubMed:25245946}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=ZNF509L; CC IsoId=Q6ZSB9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6ZSB9-2; Sequence=VSP_016343; CC Name=3; Synonyms=ZNF509S1; CC IsoId=Q6ZSB9-3; Sequence=VSP_057623, VSP_057625; CC Name=4; Synonyms=ZNF509S2; CC IsoId=Q6ZSB9-4; Sequence=VSP_057624, VSP_057625; CC Name=5; Synonyms=ZNF509S3; CC IsoId=Q6ZSB9-5; Sequence=VSP_057626, VSP_057627; CC -!- TISSUE SPECIFICITY: Highly expressed in normal epidermis and in other CC epithelial tissues, including in colon and lung. Tends to be down- CC regulated in colon, lung and skin cancer tissues. CC {ECO:0000269|PubMed:25245946}. CC -!- INDUCTION: Induced by the DNA-damaging agent etoposide. This induction CC is mediated by TP53 at the transcriptional level. CC {ECO:0000269|PubMed:25245946}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH16477.1; Type=Erroneous termination; Note=Truncated C-terminus.; 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; AK127560; BAC87035.1; -; mRNA. DR EMBL; AK292551; BAF85240.1; -; mRNA. DR EMBL; AC011744; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105415; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC016477; AAH16477.1; ALT_SEQ; mRNA. DR EMBL; BC089401; AAH89401.1; -; mRNA. DR EMBL; BC109087; AAI09088.1; -; mRNA. DR EMBL; AB209466; BAD92703.1; -; Transcribed_RNA. DR CCDS; CCDS3375.1; -. [Q6ZSB9-1] DR RefSeq; NP_001317554.1; NM_001330625.1. [Q6ZSB9-1] DR RefSeq; NP_660334.3; NM_145291.3. [Q6ZSB9-1] DR RefSeq; XP_005248008.1; XM_005247951.4. [Q6ZSB9-5] DR RefSeq; XP_011511718.1; XM_011513416.1. [Q6ZSB9-2] DR AlphaFoldDB; Q6ZSB9; -. DR SMR; Q6ZSB9; -. DR BioGRID; 127934; 25. DR IntAct; Q6ZSB9; 18. DR STRING; 9606.ENSP00000338807; -. DR iPTMnet; Q6ZSB9; -. DR PhosphoSitePlus; Q6ZSB9; -. DR BioMuta; ZBTB49; -. DR DMDM; 296453078; -. DR MassIVE; Q6ZSB9; -. DR MaxQB; Q6ZSB9; -. DR PaxDb; 9606-ENSP00000338807; -. DR PeptideAtlas; Q6ZSB9; -. DR ProteomicsDB; 68212; -. [Q6ZSB9-1] DR ProteomicsDB; 68213; -. [Q6ZSB9-2] DR Antibodypedia; 9229; 119 antibodies from 22 providers. DR DNASU; 166793; -. DR Ensembl; ENST00000337872.9; ENSP00000338807.4; ENSG00000168826.16. [Q6ZSB9-1] DR GeneID; 166793; -. DR KEGG; hsa:166793; -. DR MANE-Select; ENST00000337872.9; ENSP00000338807.4; NM_145291.4; NP_660334.3. DR UCSC; uc003ghu.4; human. [Q6ZSB9-1] DR AGR; HGNC:19883; -. DR CTD; 166793; -. DR DisGeNET; 166793; -. DR GeneCards; ZBTB49; -. DR HGNC; HGNC:19883; ZBTB49. DR HPA; ENSG00000168826; Low tissue specificity. DR MIM; 616238; gene. DR neXtProt; NX_Q6ZSB9; -. DR OpenTargets; ENSG00000168826; -. DR PharmGKB; PA165664822; -. DR VEuPathDB; HostDB:ENSG00000168826; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000158750; -. DR HOGENOM; CLU_018392_0_0_1; -. DR InParanoid; Q6ZSB9; -. DR OMA; AVYGPYV; -. DR OrthoDB; 5295767at2759; -. DR PhylomeDB; Q6ZSB9; -. DR TreeFam; TF330993; -. DR PathwayCommons; Q6ZSB9; -. DR SignaLink; Q6ZSB9; -. DR BioGRID-ORCS; 166793; 13 hits in 1215 CRISPR screens. DR ChiTaRS; ZBTB49; human. DR GenomeRNAi; 166793; -. DR Pharos; Q6ZSB9; Tdark. DR PRO; PR:Q6ZSB9; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q6ZSB9; Protein. DR Bgee; ENSG00000168826; Expressed in oocyte and 132 other cell types or tissues. DR ExpressionAtlas; Q6ZSB9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor 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:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB. DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central. DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central. DR CDD; cd18233; BTB_POZ_ZBTB49; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 7. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR46105; AGAP004733-PA; 1. DR PANTHER; PTHR46105:SF5; AGAP004733-PA; 1. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 6. DR Pfam; PF13912; zf-C2H2_6; 1. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 7. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7. DR Genevisible; Q6ZSB9; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Cell cycle; Cytoplasm; DNA-binding; KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..765 FT /note="Zinc finger and BTB domain-containing protein 49" FT /id="PRO_0000047626" FT DOMAIN 25..91 FT /note="BTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037" FT ZN_FING 395..417 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 423..445 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 451..473 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 479..501 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 507..529 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 535..557 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 563..585 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 165..203 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 275..294 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 184..203 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 419..540 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016343" FT VAR_SEQ 420 FT /note="E -> N (in isoform 3)" FT /evidence="ECO:0000269|PubMed:25245946" FT /id="VSP_057623" FT VAR_SEQ 420 FT /note="E -> R (in isoform 4)" FT /evidence="ECO:0000269|PubMed:25245946" FT /id="VSP_057624" FT VAR_SEQ 421..765 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000269|PubMed:25245946" FT /id="VSP_057625" FT VAR_SEQ 460..466 FT /note="FAASGDV -> EMFWGIR (in isoform 5)" FT /evidence="ECO:0000269|PubMed:25245946" FT /id="VSP_057626" FT VAR_SEQ 467..765 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000269|PubMed:25245946" FT /id="VSP_057627" FT VARIANT 320 FT /note="Y -> S (in dbSNP:rs2920217)" FT /id="VAR_057422" FT VARIANT 348 FT /note="A -> T (in dbSNP:rs4689254)" FT /id="VAR_057423" FT VARIANT 556 FT /note="T -> A (in dbSNP:rs146575965)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_073227" FT VARIANT 642 FT /note="A -> V (in dbSNP:rs34293093)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_057424" FT CONFLICT 449 FT /note="K -> E (in Ref. 1; BAC87035)" FT /evidence="ECO:0000305" FT CONFLICT 506 FT /note="V -> I (in Ref. 1; BAC87035)" FT /evidence="ECO:0000305" FT CONFLICT 618 FT /note="S -> P (in Ref. 1; BAF85240)" FT /evidence="ECO:0000305" SQ SEQUENCE 765 AA; 85061 MW; 287EC40D48764399 CRC64; MDPVATHSCH LLQQLHEQRI QGLLCDCMLV VKGVCFKAHK NVLAAFSQYF RSLFQNSSSQ KNDVFHLDVK NVSGIGQILD FMYTSHLDLN QDNIQVMLDT AQCLQVQNVL SLCHTFLKSA TVVQPPGMPC NSTLSLQSTL TPDATCVISE NYPPHLLQEC SADAQQNKTL DESHPHASPS VNRHHSAGEI SKQAPDTSDG SCTELPFKQP NYYYKLRNFY SKQYHKHAAG PSQERVVEQP FAFSTSTDLT TVESQPCAVS HSECILESPE HLPSNFLAQP VNDSAPHPES DATCQQPVKQ MRLKKAIHLK KLNFLKSQKY AEQVSEPKSD DGLTKRLESA SKNTLEKASS QSAEEKESEE VVSCENFNCI SETERPEDPA ALEDQSQTLQ SQRQYACELC GKPFKHPSNL ELHKRSHTGE KPFECNICGK HFSQAGNLQT HLRRHSGEKP YICEICGKRF AASGDVQRHI IIHSGEKPHL CDICGRGFSN FSNLKEHKKT HTADKVFTCD ECGKSFNMQR KLVKHRIRHT GERPYSCSAC GKCFGGSGDL RRHVRTHTGE KPYTCEICNK CFTRSAVLRR HKKMHCKAGD ESPDVLEELS QAIETSDLEK SQSSDSFSQD TSVTLMPVSV KLPVHPVENS VAEFDSHSGG SYCKLRSMIQ PHGVSDQEKL SLDPGKLAKP QMQQTQPQAY AYSDVDTPAG GEPLQADGMA MIRSSLAALD NHGGDPLGSR ASSTTYRNSE GQFFSSMTLW GLAMKTLQNE NELDQ //