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ZSC12_PONPY
ID   ZSC12_PONPY             Reviewed;         604 AA.
AC   A2T7F4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Zinc finger and SCAN domain-containing protein 12;
DE   AltName: Full=Zinc finger protein 96;
GN   Name=ZSCAN12; Synonyms=ZNF96;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
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; DQ977463; ABM89232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2T7F4; -.
DR   SMR; A2T7F4; -.
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; Repeat;
KW   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_0000285486"
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          155..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..264
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;  70028 MW;  DE7AF33D58D48FF8 CRC64;
     MASTWAIQAH MDQDEPLEVK IEEEKYTTRQ DWDLRKNNTH SREVFRQYFR QFCYQETSGP
     REALSRLREL CHQWLRPETH TKEQILELLV LEQFLTILPE ELQAWVQEQH PESGEEVVTV
     LEDLERELDE PGEQVSAHTG EQEMFLQEMV PLGKEGEPSM SLQSMKAQPK YESPELESQQ
     EQVLDVETGN EYGNLKQEVS EEMEPHGNTS SKFENDMSKS ARCGETHKPE EITEEPSACS
     REDKQPTCDE NGVSLTENSD HTEHQRICPG EKSYGCDDCG KAFSQHSHLI EHQRIHTGDR
     PYKCEECGKA FRGRTVLIRH KIIHTGEKPY KCNECGKAFG RWSALNQHQR LHTGEKHYHC
     NDCGKAFSQK AGLFHHIKIH KRDKPYQCTQ CNKSFSRRSI LTQHQGVHTG AKPYECNECG
     KAFVYNSSLV SHQEIHHKEK CYQCKECGKS FSQSGLIQHQ RIHTGEKPYK CEVCEKAFIQ
     RTSLTEHQRI HTGERPYKCD KCGKAFTQRS VLTEHQRIHT GERPYKCDEC GNAFRGITSL
     IQHQRIHTGE KPYQCDECGK AFRQRRKTSY KEILLKNHSE PQAGVNLLLS SLIPEWQSCC
     RKDL
 
 
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