ID   ZSC12_PANPA             Reviewed;         604 AA.
AC   A1YFW2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Zinc finger and SCAN domain-containing protein 12;
DE   AltName: Full=Zinc finger protein 96;
GN   Name=ZSCAN12; Synonyms=ZNF96;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT   "Positive selection in transcription factor genes on the human lineage.";
RL   Submitted (AUG-2006) 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; DQ977163; ABM54187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1YFW2; -.
DR   SMR; A1YFW2; -.
DR   STRING; 9597.XP_008953309.1; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   Proteomes; UP000240080; 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   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; SSF57667; 6.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE   3: Inferred from homology;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..604
FT                   /note="Zinc finger and SCAN domain-containing protein 12"
FT                   /id="PRO_0000285484"
FT   DOMAIN          46..128
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   ZN_FING         274..296
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         302..324
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         330..352
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         358..380
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         386..408
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         414..436
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         442..463
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         469..491
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         497..519
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         525..547
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         553..578
FT                   /note="C2H2-type 11; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          154..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        20
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43309"
FT   CROSSLNK        25
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43309"
FT   CROSSLNK        196
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43309"
SQ   SEQUENCE   604 AA;  70239 MW;  64743A4DACD85A1C CRC64;
     MASTWAIQAH MDQDEPLEVK IEEEKYTTRQ DWDLRKNNTH SREVFRQYFR QFCYQETSGP
     REALSRLREL CHQWLRPETH TKEQILELLV LEQFLTILPE ELQAWVQEQH PESGEEVVTV
     LEDLERELDE PGEQVSAHTG EQEMFLQETV RLRKEGEPSM SLQSMKAQPK YESPELESQQ
     EQVLDVETGN EYGNLKQEVS EEMEPHGNTS SKFENDMSKS ARCGETREPE EITEEPSACS
     REDKQPTCDE NGVSLTENSD HTEHQRICPG EESYGCDYCG KTFSQHSHLI EHQRIHTGDR
     PYKCEECGKA FRGRTVLIRH KIIHTGEKPY KCNECGKAFG RWSALNQHQR LHTGEKHYHC
     NDCGKAFSQK AGLFHHIKIH TRDKPYQCTH CNKSFSRRSI LTQHQGVHTG AKPYECNECG
     KAFVYNSSLV SHQEIHHKEK CYQCKECGKS FSQSGLIQHQ RIHTGEKPYK CDVCEKAFIQ
     RTSLTEHQRI HTGERPYKCD KCGKAFTQRS VLTEHQRIHT GERPYKCDEC GNAFRGITSL
     IQHQRIHTGE KPYQCDECGK AFRQRKKTSY KEILLKNHSE PQAGVNLLLS SLIPEWQSCF
     RKDL