ID   ZN549_PONAB             Reviewed;         640 AA.
AC   Q5RBQ3;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Zinc finger protein 549;
GN   Name=ZNF549;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; CR858585; CAH90807.1; -; mRNA.
DR   RefSeq; NP_001125458.1; NM_001131986.1.
DR   AlphaFoldDB; Q5RBQ3; -.
DR   SMR; Q5RBQ3; -.
DR   GeneID; 100172366; -.
DR   KEGG; pon:100172366; -.
DR   CTD; 256051; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q5RBQ3; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 15.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 8.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..640
FT                   /note="Zinc finger protein 549"
FT                   /id="PRO_0000234584"
FT   DOMAIN          27..140
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         217..241
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         247..269
FT                   /note="C2H2-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         275..298
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         304..326
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         332..355
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         361..383
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         389..411
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         417..439
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         445..467
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         473..495
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         501..523
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         529..551
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         557..579
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         585..607
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         613..635
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        223
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P9A3"
SQ   SEQUENCE   640 AA;  74413 MW;  4E247917465926CE CRC64;
     MAAAALVNTP QIPMVTEEFV KPSQGHVTFE DIAVYFSQEE WGLLDEAQRC LYHDVMLENF
     LLMASVGCLH GIEAEEAPSE QTISAQGVSQ ARTPKLGPSI PNAHSCEMCI LVMKDILYLT
     EHQGTLPWQK PYTSVASGKW FSFGSNLQQH QNQDSGEKHI RKEESSALLL NSCKIPLSDN
     LFPCKDVEKD FPTILGLLQH QTTHSREEYA HRSRETFQQR RYKCEQVFNE KVHVTEHQRV
     HTGEKAYKRR EYGKSLNSKY SFVEHQRTHN TEKPYVCNVC GKSFLHKQTL VGHQQRIHTR
     ERSYVCIECG KSLSSKYSLV EHQRTHNGEK PYVCNVCGKS FRHKQTFVGH QQRIHTGERP
     YVCIECGKSF IHSYDRIRHQ RVHTGERAYQ CSECGKSFIY KQSLLDHQRI HTGERPYECK
     ECGKAFIHKK RLLEHQRIHT GEKPYACIIC GKSFIRSSDY MRHQRIHTGE RAYECGDCGK
     AFISKQTLIK HHKIHTRERP YECSECGKGF YLEVKLLQHQ RIHTREKLCE CNECGKVFSH
     QKRLLEHQKV HTGEKPCECS ECGKCFRHRT SLVQHQKVHS GERPYNCTAC EKAFIYKNKL
     VEHQRIHTGE KPYECGKCGK AFNKRYSLVR HQKVHITEEP