TZAP_PONAB
ID TZAP_PONAB Reviewed; 688 AA.
AC Q5R633;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
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:0000250|UniProtKB:P10074};
GN Name=ZBTB48 {ECO:0000250|UniProtKB:P10074};
GN Synonyms=TZAP {ECO:0000250|UniProtKB:P10074};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; CR860664; CAH92783.1; -; mRNA.
DR RefSeq; NP_001126624.1; NM_001133152.1.
DR AlphaFoldDB; Q5R633; -.
DR SMR; Q5R633; -.
DR STRING; 9601.ENSPPYP00000002248; -.
DR GeneID; 100173621; -.
DR KEGG; pon:100173621; -.
DR CTD; 3104; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5R633; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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 2: Evidence at transcript level;
KW Activator; Chromosome; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Telomere;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..688
FT /note="Telomere zinc finger-associated protein"
FT /id="PRO_0000292137"
FT DOMAIN 26..89
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 291..313
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..401
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..430
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 436..459
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 521..544
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 550..572
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 159..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10074"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10074"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10074"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10074"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10074"
SQ SEQUENCE 688 AA; 77178 MW; 3D305D80EB38C122 CRC64;
MDGSFVQHSV RVLQELNKQR EKGQYCDATL DVGGLVFKAH WSVLACCSHF FQSLYGDGSG
GSVVLPAGFA EIFGLLLDFF YTGHLALTSG NRDQVLLAAR ELRVPEAVEL CQSFKPKISV
GQAAGGQSGQ GPPASQNVNS HVKEPAGLEE EEVSRTLGLV PRDQEPRGSH SPQRPKLHSL
AQSESPSSLC GKLKQASKPC PPEDKKLEDC KVLPRPFEAE GAQLQGGSNE WEVVVQVEDD
GDGDYMSEPE AVLTRRKSNV IRKPCAAEPA LNAGSLAAEP AENRKGTAVP VECPTCHKKF
LSKYYLKVHN RKHTGEKPFE CPKCGKCYFR KENLLEHEAR NCMNRSEQVF TCSVCQETFR
RRMELRVHMV SHTGEMPYKC SSCSQQFMQK KDLQSHMIKL HGAPKPHACP TCAKCFLSRT
ELQLHEAFKH RGEKLFVCEE CGHRASSRNG LQMHIKAKHR NERPHVCEFC SHAFTQKANL
NMHLRTHTGE KPFQCHLCGK TFRTQASLDK HNRTHTGERP FSCEFCEQRF TEKGPLLRHV
ASRHQEGRPH FCQICGKTFK AVEQLRVHVR RHKGVRKFEC TECGYKFTRQ AHLRRHMEIH
DRVENYNPRQ RKLRNLIIED EKMVVVALQP PAELEVGSAE VIVESLAQGG LASQLPGQRL
CAEESFTGPG VLEPSLIITA AVPEDCDT
