ZBT7A_HUMAN
ID ZBT7A_HUMAN Reviewed; 584 AA.
AC O95365; D6W619; O00456; Q14D41; Q5XG86;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Zinc finger and BTB domain-containing protein 7A {ECO:0000305};
DE AltName: Full=Factor binding IST protein 1 {ECO:0000303|PubMed:9973611};
DE Short=FBI-1 {ECO:0000303|PubMed:9973611};
DE AltName: Full=Factor that binds to inducer of short transcripts protein 1;
DE AltName: Full=HIV-1 1st-binding protein 1;
DE AltName: Full=Leukemia/lymphoma-related factor {ECO:0000303|PubMed:9927193};
DE AltName: Full=POZ and Krueppel erythroid myeloid ontogenic factor {ECO:0000303|PubMed:15662416};
DE Short=POK erythroid myeloid ontogenic factor {ECO:0000303|PubMed:15662416};
DE Short=Pokemon {ECO:0000303|PubMed:15662416};
DE Short=Pokemon 1 {ECO:0000303|PubMed:17595526};
DE AltName: Full=TTF-I-interacting peptide 21 {ECO:0000312|EMBL:AAB58414.1};
DE Short=TIP21 {ECO:0000312|EMBL:AAB58414.1};
DE AltName: Full=Zinc finger protein 857A;
GN Name=ZBTB7A {ECO:0000312|HGNC:HGNC:18078};
GN Synonyms=FBI1, LRF {ECO:0000303|PubMed:9927193},
GN ZBTB7 {ECO:0000312|HGNC:HGNC:18078}, ZNF857A;
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], AND SUBUNIT.
RC TISSUE=Carcinoma;
RX PubMed=9973611; DOI=10.1093/nar/27.5.1251;
RA Morrison D.J., Pendergrast P.S., Stavropoulos P., Colmenares S.U.,
RA Kobayashi R., Hernandez N.;
RT "FBI-1, a factor that binds to the HIV-1 inducer of short transcripts
RT (IST), is a POZ domain protein.";
RL Nucleic Acids Res. 27:1251-1262(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Jansa P., Grummt I.;
RT "cDNA encoding TTF-I interacting peptide 21 (TIP21).";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Pancreas;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=9927193; DOI=10.1038/sj.onc.1202332;
RA Davies J.M., Hawe N., Kabarowski J., Huang Q.-H., Zhu J., Brand N.J.,
RA Leprince D., Dhordain P., Cook M., Moriss-Kay G., Zelent A.;
RT "Novel BTB/POZ domain zinc-finger protein, LRF, is a potential target of
RT the LAZ-3/BCL-6 oncogene.";
RL Oncogene 18:365-375(1999).
RN [6]
RP FUNCTION, INTERACTION WITH SP1, AND DOMAIN.
RX PubMed=12004059; DOI=10.1074/jbc.m202078200;
RA Lee D.K., Suh D., Edenberg H.J., Hur M.W.;
RT "POZ domain transcription factor, FBI-1, represses transcription of
RT ADH5/FDH by interacting with the zinc finger and interfering with DNA
RT binding activity of Sp1.";
RL J. Biol. Chem. 277:26761-26768(2002).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14701838; DOI=10.1074/jbc.m310240200;
RA Laudes M., Christodoulides C., Sewter C., Rochford J.J., Considine R.V.,
RA Sethi J.K., Vidal-Puig A., O'Rahilly S.;
RT "Role of the POZ zinc finger transcription factor FBI-1 in human and murine
RT adipogenesis.";
RL J. Biol. Chem. 279:11711-11718(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=15662416; DOI=10.1038/nature03203;
RA Maeda T., Hobbs R.M., Merghoub T., Guernah I., Zelent A., Cordon-Cardo C.,
RA Teruya-Feldstein J., Pandolfi P.P.;
RT "Role of the proto-oncogene Pokemon in cellular transformation and ARF
RT repression.";
RL Nature 433:278-285(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-549, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION, AND MUTAGENESIS OF LYS-61;
RP LYS-354; LYS-371; LYS-379; LYS-383; LYS-396; LYS-486; LYS-487; LYS-536 AND
RP LYS-539.
RX PubMed=17595526; DOI=10.1159/000104164;
RA Roh H.E., Lee M.N., Jeon B.N., Choi W.I., Kim Y.J., Yu M.Y., Hur M.W.;
RT "Regulation of pokemon 1 activity by sumoylation.";
RL Cell. Physiol. Biochem. 20:167-180(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511 AND SER-525, AND
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; SER-341 AND SER-549, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP FUNCTION, INTERACTION WITH AR; NCOR1 AND NCOR2, AND DOMAIN.
RX PubMed=20812024; DOI=10.1007/s00018-010-0511-7;
RA Cui J., Yang Y., Zhang C., Hu P., Kan W., Bai X., Liu X., Song H.;
RT "FBI-1 functions as a novel AR co-repressor in prostate cancer cells.";
RL Cell. Mol. Life Sci. 68:1091-1103(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-549, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [18]
RP FUNCTION, INTERACTION WITH KHDRBS1, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=24514149; DOI=10.1002/embr.201338241;
RA Bielli P., Busa R., Di Stasi S.M., Munoz M.J., Botti F., Kornblihtt A.R.,
RA Sette C.;
RT "The transcription factor FBI-1 inhibits SAM68-mediated BCL-X alternative
RT splicing and apoptosis.";
RL EMBO Rep. 15:419-427(2014).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-549, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-539, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-539, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [22]
RP FUNCTION, INTERACTION WITH HDAC1 AND SMAD4, DOMAIN, AND REGION.
RX PubMed=25514493; DOI=10.1016/j.bbagrm.2014.12.008;
RA Yang Y., Cui J., Xue F., Zhang C., Mei Z., Wang Y., Bi M., Shan D.,
RA Meredith A., Li H., Xu Z.Q.;
RT "Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced
RT transcriptional responses.";
RL Biochim. Biophys. Acta 1849:270-281(2015).
RN [23]
RP INTERACTION WITH THE DNA-DEPENDENT PROTEIN KINASE COMPLEX.
RX PubMed=26446488; DOI=10.1038/ncomms9325;
RA Liu X.S., Chandramouly G., Rass E., Guan Y., Wang G., Hobbs R.M.,
RA Rajendran A., Xie A., Shah J.V., Davis A.J., Scully R., Lunardi A.,
RA Pandolfi P.P.;
RT "LRF maintains genome integrity by regulating the non-homologous end
RT joining pathway of DNA repair.";
RL Nat. Commun. 6:8325-8325(2015).
RN [24]
RP FUNCTION, AND MUTAGENESIS OF PRO-14; SER-22; ARG-49; LYS-60; ASP-78;
RP ARG-112; PRO-184; GLN-322; SER-326; SER-357; ARG-377; CYS-387; ILE-391;
RP ARG-399; ARG-402; THR-403; HIS-404; GLY-406; PRO-409; CYS-412; LYS-424;
RP ARG-430; THR-461; LEU-463; TYR-466; ALA-522; GLU-541; GLY-562 AND ASP-576.
RX PubMed=26455326; DOI=10.1038/onc.2015.371;
RA Liu X.S., Liu Z., Gerarduzzi C., Choi D.E., Ganapathy S., Pandolfi P.P.,
RA Yuan Z.M.;
RT "Somatic human ZBTB7A zinc finger mutations promote cancer progression.";
RL Oncogene 35:3071-3078(2016).
RN [25]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=26816381; DOI=10.1126/science.aad3312;
RA Masuda T., Wang X., Maeda M., Canver M.C., Sher F., Funnell A.P.,
RA Fisher C., Suciu M., Martyn G.E., Norton L.J., Zhu C., Kurita R.,
RA Nakamura Y., Xu J., Higgs D.R., Crossley M., Bauer D.E., Orkin S.H.,
RA Kharchenko P.V., Maeda T.;
RT "Transcription factors LRF and BCL11A independently repress expression of
RT fetal hemoglobin.";
RL Science 351:285-289(2016).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-436 AND LYS-539, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP INTERACTION WITH RELA.
RX PubMed=29813070; DOI=10.1371/journal.pbio.2004526;
RA Ramos Pittol J.M., Oruba A., Mittler G., Saccani S., van Essen D.;
RT "Zbtb7a is a transducer for the control of promoter accessibility by NF-
RT kappa B and multiple other transcription factors.";
RL PLoS Biol. 16:E2004526-E2004526(2018).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-128.
RX PubMed=17052694; DOI=10.1016/j.bbrc.2006.09.167;
RA Schubot F.D., Tropea J.E., Waugh D.S.;
RT "Structure of the POZ domain of human LRF, a master regulator of
RT oncogenesis.";
RL Biochem. Biophys. Res. Commun. 351:1-6(2006).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-131.
RX PubMed=17189472; DOI=10.1110/ps.062660907;
RA Stogios P.J., Chen L., Prive G.G.;
RT "Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional
RT regulator.";
RL Protein Sci. 16:336-342(2007).
CC -!- FUNCTION: Transcription factor that represses the transcription of a
CC wide range of genes involved in cell proliferation and differentiation
CC (PubMed:14701838, PubMed:17595526, PubMed:20812024, PubMed:25514493,
CC PubMed:26455326, PubMed:26816381). Directly and specifically binds to
CC the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses
CC transcription both by regulating the organization of chromatin and
CC through the direct recruitment of transcription factors to gene
CC regulatory regions (PubMed:12004059, PubMed:17595526, PubMed:20812024,
CC PubMed:25514493, PubMed:26816381). Negatively regulates SMAD4
CC transcriptional activity in the TGF-beta signaling pathway through
CC these two mechanisms (PubMed:25514493). That is, recruits the chromatin
CC regulator HDAC1 to the SMAD4-DNA complex and in parallel prevents the
CC recruitment of the transcriptional activators CREBBP and EP300
CC (PubMed:25514493). Collaborates with transcription factors like RELA to
CC modify the accessibility of gene transcription regulatory regions to
CC secondary transcription factors (By similarity). Also directly
CC interacts with transcription factors like SP1 to prevent their binding
CC to DNA (PubMed:12004059). Functions as an androgen receptor/AR
CC transcriptional corepressor by recruiting NCOR1 and NCOR2 to the
CC androgen response elements/ARE on target genes (PubMed:20812024).
CC Thereby, negatively regulates androgen receptor signaling and androgen-
CC induced cell proliferation (PubMed:20812024). Involved in the switch
CC between fetal and adult globin expression during erythroid cells
CC maturation (PubMed:26816381). Through its interaction with the NuRD
CC complex regulates chromatin at the fetal globin genes to repress their
CC transcription (PubMed:26816381). Specifically represses the
CC transcription of the tumor suppressor ARF isoform from the CDKN2A gene
CC (By similarity). Efficiently abrogates E2F1-dependent CDKN2A
CC transactivation (By similarity). Regulates chondrogenesis through the
CC transcriptional repression of specific genes via a mechanism that also
CC requires histone deacetylation (By similarity). Regulates cell
CC proliferation through the transcriptional regulation of genes involved
CC in glycolysis (PubMed:26455326). Involved in adipogenesis through the
CC regulation of genes involved in adipocyte differentiation
CC (PubMed:14701838). Plays a key role in the differentiation of lymphoid
CC progenitors into B and T lineages (By similarity). Promotes
CC differentiation towards the B lineage by inhibiting the T-cell
CC instructive Notch signaling pathway through the specific
CC transcriptional repression of Notch downstream target genes (By
CC similarity). Also regulates osteoclast differentiation (By similarity).
CC May also play a role, independently of its transcriptional activity, in
CC double-strand break repair via classical non-homologous end
CC joining/cNHEJ (By similarity). Recruited to double-strand break sites
CC on damage DNA, interacts with the DNA-dependent protein kinase complex
CC and directly regulates its stability and activity in DNA repair (By
CC similarity). May also modulate the splicing activity of KHDRBS1 toward
CC BCL2L1 in a mechanism which is histone deacetylase-dependent and
CC thereby negatively regulates the pro-apoptotic effect of KHDRBS1
CC (PubMed:24514149). {ECO:0000250|UniProtKB:O88939,
CC ECO:0000250|UniProtKB:Q9QZ48, ECO:0000269|PubMed:12004059,
CC ECO:0000269|PubMed:14701838, ECO:0000269|PubMed:17595526,
CC ECO:0000269|PubMed:20812024, ECO:0000269|PubMed:24514149,
CC ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:26455326,
CC ECO:0000269|PubMed:26816381}.
CC -!- SUBUNIT: Homodimer (PubMed:9973611). Interacts with BCL6 (By
CC similarity). Interacts with RELA; involved in the control by RELA of
CC the accessibility of target gene promoters (PubMed:29813070). Interacts
CC with AR (via NR LBD domain); the interaction is direct and androgen-
CC dependent (PubMed:20812024). Interacts with NCOR1 (PubMed:20812024).
CC Interacts with NCOR2 (PubMed:20812024). Interacts with SMAD4; the
CC interaction is direct and stimulated by TGFB1 (PubMed:25514493).
CC Interacts with HDAC1 (PubMed:25514493). Interacts with SP1; ZBTB7A
CC prevents the binding to GC-rich motifs in promoters and represses the
CC transcriptional activity of SP1 (PubMed:12004059). Interacts with the
CC DNA-dependent protein kinase complex/DNA-PKc (PubMed:26446488).
CC Interacts with KHDRBS1; negatively regulates KHDRBS1 splicing activity
CC (PubMed:24514149). {ECO:0000250|UniProtKB:O88939,
CC ECO:0000269|PubMed:12004059, ECO:0000269|PubMed:20812024,
CC ECO:0000269|PubMed:24514149, ECO:0000269|PubMed:25514493,
CC ECO:0000269|PubMed:26446488, ECO:0000269|PubMed:29813070,
CC ECO:0000269|PubMed:9973611}.
CC -!- INTERACTION:
CC O95365; Q9NRL2: BAZ1A; NbExp=2; IntAct=EBI-2795384, EBI-927511;
CC O95365; Q12873: CHD3; NbExp=2; IntAct=EBI-2795384, EBI-523590;
CC O95365; Q9HCK8: CHD8; NbExp=2; IntAct=EBI-2795384, EBI-1169146;
CC O95365; Q8WXI9: GATAD2B; NbExp=4; IntAct=EBI-2795384, EBI-923440;
CC O95365; Q13547: HDAC1; NbExp=2; IntAct=EBI-2795384, EBI-301834;
CC O95365; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-2795384, EBI-10172004;
CC O95365; Q07666: KHDRBS1; NbExp=9; IntAct=EBI-2795384, EBI-1364;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17595526,
CC ECO:0000269|PubMed:24514149}. Note=Recruited to double-strand break
CC sites of damaged DNA. {ECO:0000250|UniProtKB:O88939}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9927193). In normal
CC thymus, expressed in medullary epithelial cells and Hassle's corpuscles
CC (at protein level) (PubMed:15662416). In tonsil, expressed in squamous
CC epithelium and germinal center lymphocytes (at protein level)
CC (PubMed:15662416). Up-regulated in a subset of lymphomas, as well as in
CC a subset of breast, lung, colon, prostate and bladder carcinomas (at
CC protein level) (PubMed:15662416). Expressed in adipose tissues
CC (PubMed:14701838). {ECO:0000269|PubMed:14701838,
CC ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:9927193}.
CC -!- DEVELOPMENTAL STAGE: Expression is increased in differentiating
CC erythroid cells (at protein level) (PubMed:26816381). Up-regulated
CC during adipocyte differentiation (PubMed:14701838).
CC {ECO:0000269|PubMed:14701838, ECO:0000269|PubMed:26816381}.
CC -!- DOMAIN: The BTB domain mediates the interaction with the androgen
CC receptor/AR and HDAC1 (PubMed:20812024, PubMed:25514493). Also mediates
CC the interaction with SP1 (PubMed:12004059).
CC {ECO:0000269|PubMed:12004059, ECO:0000269|PubMed:20812024,
CC ECO:0000269|PubMed:25514493}.
CC -!- PTM: Sumoylated. Undergoes sumoylation with SUMO1 that may regulate its
CC transcriptional activity. {ECO:0000269|PubMed:17595526}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58414.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ZBTB7AID42863ch19p13.html";
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DR EMBL; AF097916; AAC72973.1; -; mRNA.
DR EMBL; AF000561; AAB58414.1; ALT_FRAME; mRNA.
DR EMBL; CH471139; EAW69267.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69268.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69270.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69271.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69272.1; -; Genomic_DNA.
DR EMBL; BC084568; AAH84568.1; -; mRNA.
DR EMBL; BC113511; AAI13512.1; -; mRNA.
DR CCDS; CCDS12119.1; -.
DR RefSeq; NP_001304919.1; NM_001317990.1.
DR RefSeq; NP_056982.1; NM_015898.3.
DR RefSeq; XP_005259628.1; XM_005259571.4.
DR PDB; 2IF5; X-ray; 2.00 A; A=9-128.
DR PDB; 2NN2; X-ray; 2.10 A; A/B=1-131.
DR PDB; 7EYI; X-ray; 2.40 A; G/H=382-506.
DR PDB; 7N5S; X-ray; 2.86 A; A=369-500.
DR PDB; 7N5T; X-ray; 2.90 A; A=369-500.
DR PDBsum; 2IF5; -.
DR PDBsum; 2NN2; -.
DR PDBsum; 7EYI; -.
DR PDBsum; 7N5S; -.
DR PDBsum; 7N5T; -.
DR AlphaFoldDB; O95365; -.
DR SMR; O95365; -.
DR BioGRID; 119488; 129.
DR DIP; DIP-56307N; -.
DR IntAct; O95365; 18.
DR MINT; O95365; -.
DR STRING; 9606.ENSP00000323670; -.
DR iPTMnet; O95365; -.
DR PhosphoSitePlus; O95365; -.
DR BioMuta; ZBTB7A; -.
DR EPD; O95365; -.
DR jPOST; O95365; -.
DR MassIVE; O95365; -.
DR MaxQB; O95365; -.
DR PaxDb; O95365; -.
DR PeptideAtlas; O95365; -.
DR PRIDE; O95365; -.
DR ProteomicsDB; 50825; -.
DR Antibodypedia; 11338; 359 antibodies from 39 providers.
DR DNASU; 51341; -.
DR Ensembl; ENST00000322357.9; ENSP00000323670.3; ENSG00000178951.9.
DR Ensembl; ENST00000601588.1; ENSP00000471865.1; ENSG00000178951.9.
DR GeneID; 51341; -.
DR KEGG; hsa:51341; -.
DR MANE-Select; ENST00000322357.9; ENSP00000323670.3; NM_015898.4; NP_056982.1.
DR UCSC; uc002lzh.4; human.
DR CTD; 51341; -.
DR DisGeNET; 51341; -.
DR GeneCards; ZBTB7A; -.
DR HGNC; HGNC:18078; ZBTB7A.
DR HPA; ENSG00000178951; Low tissue specificity.
DR MIM; 605878; gene.
DR neXtProt; NX_O95365; -.
DR OpenTargets; ENSG00000178951; -.
DR PharmGKB; PA134885165; -.
DR VEuPathDB; HostDB:ENSG00000178951; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162053; -.
DR HOGENOM; CLU_025627_1_0_1; -.
DR InParanoid; O95365; -.
DR OMA; CKVRFTQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O95365; -.
DR TreeFam; TF331824; -.
DR PathwayCommons; O95365; -.
DR SignaLink; O95365; -.
DR SIGNOR; O95365; -.
DR BioGRID-ORCS; 51341; 210 hits in 1157 CRISPR screens.
DR ChiTaRS; ZBTB7A; human.
DR EvolutionaryTrace; O95365; -.
DR GeneWiki; ZBTB7A; -.
DR GenomeRNAi; 51341; -.
DR Pharos; O95365; Tbio.
DR PRO; PR:O95365; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95365; protein.
DR Bgee; ENSG00000178951; Expressed in buccal mucosa cell and 201 other tissues.
DR Genevisible; O95365; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070418; C:DNA-dependent protein kinase complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0046332; F:SMAD binding; IDA:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IDA:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0043249; P:erythrocyte maturation; IMP:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
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; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..584
FT /note="Zinc finger and BTB domain-containing protein 7A"
FT /id="PRO_0000047715"
FT DOMAIN 34..101
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 382..404
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..490
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 220..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..584
FT /note="Mediates interaction with KHDRBS1"
FT /evidence="ECO:0000269|PubMed:24514149"
FT REGION 349..584
FT /note="Mediates interaction with RELA"
FT /evidence="ECO:0000250|UniProtKB:O88939"
FT REGION 377..584
FT /note="Mediates interaction with SMAD4"
FT /evidence="ECO:0000269|PubMed:25514493"
FT REGION 486..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT MUTAGEN 14
FT /note="P->S: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 22
FT /note="S->R: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 49
FT /note="R->H: Increased proteasomal degradation. No effect
FT on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 60
FT /note="K->R: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 61
FT /note="K->R: Loss of sumoylation with SUMO1. May decrease
FT interaction with transcriptional corepressors."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 78
FT /note="D->E: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 112
FT /note="R->C: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 184
FT /note="P->S: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 322
FT /note="Q->L: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 326
FT /note="S->R: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 354
FT /note="K->R: No effect on sumoylation with SUMO1. No effect
FT on promoter binding."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 357
FT /note="S->R: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 371
FT /note="K->R: No effect on sumoylation with SUMO1. No effect
FT on promoter binding."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 377
FT /note="R->L: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 379
FT /note="K->R: No effect on sumoylation with SUMO1. Decreased
FT transcription repression activity. No effect on promoter
FT binding."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 383
FT /note="K->R: No effect on sumoylation with SUMO1. No effect
FT on promoter binding."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 387
FT /note="C->F: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 391
FT /note="I->L: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 396
FT /note="K->R: No effect on sumoylation with SUMO1. Decreased
FT transcription repression activity. No effect on promoter
FT binding."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 399
FT /note="R->L: Decreased transcription repressor activity,
FT dominant negative effect. Increased glycolysis and cell
FT proliferation, dominant negative effect. No effect on
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 402
FT /note="R->H: Decreased transcription repressor activity.
FT Acts as a dominant negative. No effect on nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 403
FT /note="T->N: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 404
FT /note="H->R: Decreased transcription repressor activity.
FT Acts as a dominant negative. No effect on nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 406
FT /note="G->V: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 409
FT /note="P->S: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 412
FT /note="C->Y: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 424
FT /note="K->N: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 424
FT /note="K->T: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 430
FT /note="R->W: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 461
FT /note="T->M: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 463
FT /note="L->M: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 466
FT /note="Y->D: Decreased transcription repressor activity. No
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 486
FT /note="K->R: No effect on sumoylation with SUMO1. No effect
FT on promoter binding. No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 487
FT /note="K->R: No effect on sumoylation with SUMO1. No effect
FT on promoter binding. No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 522
FT /note="A->T: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 536
FT /note="K->R: No effect on sumoylation with SUMO1. Decreased
FT transcription repression activity. No effect on promoter
FT binding."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 539
FT /note="K->R: No effect on sumoylation with SUMO1. Decreased
FT transcription repression activity. No effect on promoter
FT binding."
FT /evidence="ECO:0000269|PubMed:17595526"
FT MUTAGEN 541
FT /note="E->K: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 562
FT /note="G->D: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT MUTAGEN 576
FT /note="D->V: No effect on transcription repressor activity.
FT No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:26455326"
FT CONFLICT 554
FT /note="G -> C (in Ref. 4; AAH84568)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2NN2"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:2IF5"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2IF5"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2IF5"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:2IF5"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:2IF5"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2IF5"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:2IF5"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:2NN2"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2IF5"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:2IF5"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:2IF5"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:7EYI"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:7EYI"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:7N5S"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:7EYI"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:7EYI"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:7EYI"
FT HELIX 422..433
FT /evidence="ECO:0007829|PDB:7EYI"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:7EYI"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:7EYI"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:7EYI"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:7EYI"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:7EYI"
FT HELIX 478..486
FT /evidence="ECO:0007829|PDB:7EYI"
SQ SEQUENCE 584 AA; 61439 MW; 50073663F3D393A0 CRC64;
MAGGVDGPIG IPFPDHSSDI LSGLNEQRTQ GLLCDVVILV EGREFPTHRS VLAACSQYFK
KLFTSGAVVD QQNVYEIDFV SAEALTALMD FAYTATLTVS TANVGDILSA ARLLEIPAVS
HVCADLLDRQ ILAADAGADA GQLDLVDQID QRNLLRAKEY LEFFQSNPMN SLPPAAAAAA
ASFPWSAFGA SDDDLDATKE AVAAAVAAVA AGDCNGLDFY GPGPPAERPP TGDGDEGDSN
PGLWPERDED APTGGLFPPP VAPPAATQNG HYGRGGEEEA ASLSEAAPEP GDSPGFLSGA
AEGEDGDGPD VDGLAASTLL QQMMSSVGRA GAAAGDSDEE SRADDKGVMD YYLKYFSGAH
DGDVYPAWSQ KVEKKIRAKA FQKCPICEKV IQGAGKLPRH IRTHTGEKPY ECNICKVRFT
RQDKLKVHMR KHTGEKPYLC QQCGAAFAHN YDLKNHMRVH TGLRPYQCDS CCKTFVRSDH
LHRHLKKDGC NGVPSRRGRK PRVRGGAPDP SPGATATPGA PAQPSSPDAR RNGQEKHFKD
EDEDEDVASP DGLGRLNVAG AGGGGDSGGG PGAATDGNFT AGLA
