ZBT49_HUMAN
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 03-AUG-2022, entry version 168.
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};
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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; 23.
DR IntAct; Q6ZSB9; 17.
DR STRING; 9606.ENSP00000338807; -.
DR iPTMnet; Q6ZSB9; -.
DR PhosphoSitePlus; Q6ZSB9; -.
DR BioMuta; ZBTB49; -.
DR DMDM; 296453078; -.
DR MassIVE; Q6ZSB9; -.
DR MaxQB; Q6ZSB9; -.
DR PaxDb; Q6ZSB9; -.
DR PeptideAtlas; Q6ZSB9; -.
DR PRIDE; Q6ZSB9; -.
DR ProteomicsDB; 68212; -. [Q6ZSB9-1]
DR ProteomicsDB; 68213; -. [Q6ZSB9-2]
DR Antibodypedia; 9229; 105 antibodies from 21 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 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; 1318335at2759; -.
DR PhylomeDB; Q6ZSB9; -.
DR TreeFam; TF330993; -.
DR PathwayCommons; Q6ZSB9; -.
DR SignaLink; Q6ZSB9; -.
DR BioGRID-ORCS; 166793; 10 hits in 1138 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 131 other tissues.
DR ExpressionAtlas; Q6ZSB9; baseline and differential.
DR Genevisible; Q6ZSB9; HS.
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: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
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 Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
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
