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