ID   ZKSC1_PONAB             Reviewed;         563 AA.
AC   Q5R670;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Zinc finger protein with KRAB and SCAN domains 1;
GN   Name=ZKSCAN1;
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: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; CR860626; CAH92746.1; -; mRNA.
DR   RefSeq; NP_001126601.1; NM_001133129.1.
DR   RefSeq; XP_009240863.1; XM_009242588.1.
DR   RefSeq; XP_009240864.1; XM_009242589.1.
DR   AlphaFoldDB; Q5R670; -.
DR   SMR; Q5R670; -.
DR   STRING; 9601.ENSPPYP00000019491; -.
DR   Ensembl; ENSPPYT00000020261; ENSPPYP00000019491; ENSPPYG00000017394.
DR   GeneID; 100173598; -.
DR   KEGG; pon:100173598; -.
DR   CTD; 7586; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161592; -.
DR   InParanoid; Q5R670; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000001595; Chromosome 7.
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   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..563
FT                   /note="Zinc finger protein with KRAB and SCAN domains 1"
FT                   /id="PRO_0000047755"
FT   DOMAIN          56..138
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   DOMAIN          227..300
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         377..399
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         405..427
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         433..455
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         461..483
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         489..511
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         517..539
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          31..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        181
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        228
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        280
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        299
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        304
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        339
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        375
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        412
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        440
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        478
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
FT   CROSSLNK        560
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P17029"
SQ   SEQUENCE   563 AA;  63472 MW;  23D7E4B30A788069 CRC64;
     MMTAESREAT GLSPQAAQEK DGIVIVKVEE EDEEDHMWGQ DSSLQDTPPP DPEIFRQRFR
     RFCYQNTFGP REALSRLKEL CHQWLRPEIN TKEQILELLV LEQFLSILPK ELQVWLQEYR
     PDSGEEAVTL LEDLELDLSG QQVPGQVHGP EMLARGMVPL DPVQESSSFD LHHEATQSHF
     KHSSRKPRLL QSRALPAAHI PAPPHEGSPR DQAMASALFT ADSQAMVKIE DMAVSLILEE
     WGCQNLARRN LSRDNKQENY GSAFPQGGEN RNENEESTSK AETAEDSASH GETAGRFQKE
     FGEKRDQEGK TGERQQKNPE EKTGKEKRDS GPATGKDKKT ITGERGPREK GKGLGRSFSL
     SSNFTTPEEV PTGTKSHRCD ECGKCFTRSS SLIRHKIIHT GEKPYECSEC GKAFSLNSNL
     VLHQRIHTGE KPHECNECGK AFSHSSNLIL HQRIHSGEKP YECNECGKAF SQSSDLTKHQ
     RIHTGEKPYE CSECGKAFNR NSYLILHRRI HTREKPYKCT KCGKAFTRSS TLTLHHRIHA
     RERASEYSPA SLDAFGAFLK SCV