TZAP_MOUSE
ID TZAP_MOUSE Reviewed; 681 AA.
AC Q1H9T6; A2A8B1; Q99K15;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Telomere zinc finger-associated protein {ECO:0000250|UniProtKB:P10074};
DE Short=TZAP {ECO:0000250|UniProtKB:P10074};
DE AltName: Full=Krueppel-related zinc finger protein 3 homolog {ECO:0000250|UniProtKB:P10074};
DE AltName: Full=Zinc finger and BTB domain-containing protein 48 {ECO:0000312|MGI:MGI:2140248};
GN Name=Zbtb48 {ECO:0000312|MGI:MGI:2140248};
GN Synonyms=Hkr3, Tzap {ECO:0000250|UniProtKB:P10074};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zink M., Weiler M., Michaelidis T.M., Neumann H., Dechant G.;
RT "Neurotrophins suppress neuronal MHC class II expression through a
RT conserved zinc finger protein and p75NTR.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 STRUCTURE BY NMR OF 284-394 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the tandem four zf-C2H2 domain repeats of murine
RT GLI-Kruppel family member Hkr3.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Telomere-binding protein that acts as a regulator of telomere
CC length. Directly binds the telomeric double-stranded 5'-TTAGGG-3'
CC repeat. Preferentially binds to telomeres that have a low concentration
CC of shelterin complex and acts as a regulator of telomere length by
CC initiating telomere trimming, a process that prevents the accumulation
CC of aberrantly long telomeres. Also acts as a transcription regulator
CC that binds to promoter regions. Regulates expression of a small subset
CC of genes, including MTFP1. Regulates expression the J and/or S elements
CC in MHC II promoter. Acts as a negative regulator of cell proliferation
CC by specifically activating expression of ARF, a tumor suppressor
CC isoform of CDKN2A. {ECO:0000250|UniProtKB:P10074}.
CC -!- SUBUNIT: Interacts with EP300. {ECO:0000250|UniProtKB:P10074}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10074}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:P10074}. Note=Directly
CC binds the telomeric double-stranded 5'-TTAGGG-3' repeat. According to a
CC report, preferentially binds to long telomeres that have a low
CC concentration of shelterin complex, competing with the telomeric repeat
CC binding factors TERF1 and TERF2. According to another report, binds
CC telomeres regardless of their length. {ECO:0000250|UniProtKB:P10074}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1H9T6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1H9T6-2; Sequence=VSP_026381;
CC -!- DOMAIN: The C2H2-type zinc fingers mediate binding to the telomeric
CC double-stranded 5'-TTAGGG-3' repeats. The last C2H2-type zinc finger is
CC required for telomeric-binding. {ECO:0000250|UniProtKB:P10074}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM24576.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM161454; CAJ44110.1; -; mRNA.
DR EMBL; AL611927; CAM24576.2; ALT_SEQ; Genomic_DNA.
DR EMBL; BC005515; AAH05515.1; -; mRNA.
DR CCDS; CCDS38982.1; -. [Q1H9T6-1]
DR RefSeq; NP_598640.2; NM_133879.2. [Q1H9T6-1]
DR PDB; 2DLQ; NMR; -; A=284-394.
DR PDB; 2YY9; X-ray; 2.60 A; A/B=8-129.
DR PDBsum; 2DLQ; -.
DR PDBsum; 2YY9; -.
DR AlphaFoldDB; Q1H9T6; -.
DR SMR; Q1H9T6; -.
DR BioGRID; 221379; 56.
DR IntAct; Q1H9T6; 32.
DR STRING; 10090.ENSMUSP00000067521; -.
DR iPTMnet; Q1H9T6; -.
DR PhosphoSitePlus; Q1H9T6; -.
DR EPD; Q1H9T6; -.
DR MaxQB; Q1H9T6; -.
DR PaxDb; Q1H9T6; -.
DR PeptideAtlas; Q1H9T6; -.
DR PRIDE; Q1H9T6; -.
DR ProteomicsDB; 297686; -. [Q1H9T6-1]
DR ProteomicsDB; 297687; -. [Q1H9T6-2]
DR Antibodypedia; 13109; 148 antibodies from 27 providers.
DR DNASU; 100090; -.
DR Ensembl; ENSMUST00000066715; ENSMUSP00000067521; ENSMUSG00000028952. [Q1H9T6-1]
DR Ensembl; ENSMUST00000155389; ENSMUSP00000114726; ENSMUSG00000028952. [Q1H9T6-2]
DR GeneID; 100090; -.
DR KEGG; mmu:100090; -.
DR UCSC; uc008vyz.1; mouse. [Q1H9T6-1]
DR CTD; 3104; -.
DR MGI; MGI:2140248; Zbtb48.
DR VEuPathDB; HostDB:ENSMUSG00000028952; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158981; -.
DR HOGENOM; CLU_497772_0_0_1; -.
DR InParanoid; Q1H9T6; -.
DR OMA; HEWEVVV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q1H9T6; -.
DR TreeFam; TF331310; -.
DR BioGRID-ORCS; 100090; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Zbtb48; mouse.
DR EvolutionaryTrace; Q1H9T6; -.
DR PRO; PR:Q1H9T6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q1H9T6; protein.
DR Bgee; ENSMUSG00000028952; Expressed in spermatocyte and 146 other tissues.
DR ExpressionAtlas; Q1H9T6; baseline and differential.
DR Genevisible; Q1H9T6; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISS:UniProtKB.
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; 6.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromosome; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Telomere; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..681
FT /note="Telomere zinc finger-associated protein"
FT /id="PRO_0000292136"
FT DOMAIN 26..89
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 284..306
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 343..365
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 371..394
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..423
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..452
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..480
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 486..508
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 514..537
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 543..565
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 571..593
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 121..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10074"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10074"
FT VAR_SEQ 402..681
FT /note="CPTCAKCFLSRTELQLHEAFKHRGEKLFVCEECGHRASSRNGLQMHIKAKHR
FT NERPYVCEFCSHAFTQKANLNMHLRTHTGEKPFQCHLCGKTFRTQASLDKHNRTHTGER
FT PFSCEFCEQRFTEKGPLLRHVASRHQEGRPHFCQICGKTFKAVEQLRVHVRRHKGVRKF
FT ECTECGYKFTRQAHLRRHMEIHDRVENYNPRQRKLRNLIIEDEKMVVVALQPPADLEVG
FT SAEVIVESLTQGGLASQLPSQRLCSEESFASPGVLEPSLIITAAVPEDCDT -> VSAS
FT QGWGSGGSGTAQSCPHLDVLPLPVSPTCSAPLVPSASCLGRSYSCTRLLSIVEKSSLCV
FT RNAGTGPRAATDCRCTSRPSTGMKGLMSVSSAAMPSPRRPTSTCTCAHTPARSLSSATS
FT VGRPSAPKFGQAQPHPHGREAFQL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026381"
FT CONFLICT 152
FT /note="R -> K (in Ref. 3; AAH05515)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="T -> S (in Ref. 3; AAH05515)"
FT /evidence="ECO:0000305"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:2YY9"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:2YY9"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2YY9"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2YY9"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:2YY9"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:2YY9"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2YY9"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2YY9"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:2YY9"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2YY9"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:2YY9"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:2YY9"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:2DLQ"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:2DLQ"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:2DLQ"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:2DLQ"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2DLQ"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2DLQ"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:2DLQ"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:2DLQ"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:2DLQ"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2DLQ"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2DLQ"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:2DLQ"
FT CONFLICT Q1H9T6-2:476
FT /note="D -> G (in Ref. 3; AAH05515)"
FT /evidence="ECO:0000305"
FT CONFLICT Q1H9T6-2:512
FT /note="H -> R (in Ref. 3; AAH05515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 681 AA; 76800 MW; CA2480B57098CCB3 CRC64;
MDGSFVQHSV RVLQELNKQR EKGQYCDATL DVGGLVFKAH WSVLACCSHF FQRIYGDGTG
GSVVLPAGFA EIFGLLLDFF YTGHLALTSG NRDQVLLAAK ELRVPEAVEL CQSFQPQTSV
GQAQSGLGQP ASQDVKSHLK EPTDLDEEEV FRTLSLASVD QEPRDTEQPQ LGTPAQSTTA
FLCGKLTQAL KPSPSEDKES EDCKEPPRPF EAGGAPLQGE SNEWEVVVQV EDDRDGDYVS
EPETVLTRRK SKVIRKPCAA EPALGAGSLT AEPTDSRKGA AVPVECPTCH KKFLSKYYLK
VHNRKHTGEK PFECPKCGKC YFRKENLLEH EARNCMNRSE QVFTCSVCQE TFRRRMELRL
HMVSHTGEMP YKCSSCSQQF MQKKDLQSHM IKLHGAPKPH ACPTCAKCFL SRTELQLHEA
FKHRGEKLFV CEECGHRASS RNGLQMHIKA KHRNERPYVC EFCSHAFTQK ANLNMHLRTH
TGEKPFQCHL CGKTFRTQAS LDKHNRTHTG ERPFSCEFCE QRFTEKGPLL RHVASRHQEG
RPHFCQICGK TFKAVEQLRV HVRRHKGVRK FECTECGYKF TRQAHLRRHM EIHDRVENYN
PRQRKLRNLI IEDEKMVVVA LQPPADLEVG SAEVIVESLT QGGLASQLPS QRLCSEESFA
SPGVLEPSLI ITAAVPEDCD T
