ZSC12_MOUSE
ID ZSC12_MOUSE Reviewed; 501 AA.
AC Q9Z1D7; Q8R0D8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 12;
DE AltName: Full=Zinc finger protein 96;
DE Short=Zfp-96;
GN Name=Zscan12; Synonyms=Zfp96, Znf96;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12860387; DOI=10.1016/s0014-5793(03)00669-0;
RA Weissig H., Narisawa S., Sikstrom C., Olsson P.G., McCarrey J.R.,
RA Tsonis P.A., Del Rio-Tsonis K., Millan J.L.;
RT "Three novel spermatogenesis-specific zinc finger genes.";
RL FEBS Lett. 547:61-68(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12860387}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U62908; AAD00104.1; -; mRNA.
DR EMBL; CH466561; EDL32662.1; -; Genomic_DNA.
DR EMBL; CH466561; EDL32663.1; -; Genomic_DNA.
DR EMBL; BC027041; AAH27041.1; -; mRNA.
DR CCDS; CCDS26273.1; -.
DR RefSeq; NP_057893.2; NM_016684.2.
DR RefSeq; XP_006516723.1; XM_006516660.3.
DR AlphaFoldDB; Q9Z1D7; -.
DR SMR; Q9Z1D7; -.
DR BioGRID; 204685; 1.
DR IntAct; Q9Z1D7; 1.
DR STRING; 10090.ENSMUSP00000058904; -.
DR iPTMnet; Q9Z1D7; -.
DR PhosphoSitePlus; Q9Z1D7; -.
DR PaxDb; Q9Z1D7; -.
DR PRIDE; Q9Z1D7; -.
DR ProteomicsDB; 275105; -.
DR Antibodypedia; 1809; 105 antibodies from 17 providers.
DR DNASU; 22758; -.
DR Ensembl; ENSMUST00000053293; ENSMUSP00000058904; ENSMUSG00000036721.
DR Ensembl; ENSMUST00000099720; ENSMUSP00000097308; ENSMUSG00000036721.
DR Ensembl; ENSMUST00000225545; ENSMUSP00000153548; ENSMUSG00000036721.
DR GeneID; 22758; -.
DR KEGG; mmu:22758; -.
DR UCSC; uc007pqd.1; mouse.
DR CTD; 9753; -.
DR MGI; MGI:1099444; Zscan12.
DR VEuPathDB; HostDB:ENSMUSG00000036721; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163105; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; Q9Z1D7; -.
DR OMA; QCEPQAG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Z1D7; -.
DR TreeFam; TF338146; -.
DR BioGRID-ORCS; 22758; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9Z1D7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9Z1D7; protein.
DR Bgee; ENSMUSG00000036721; Expressed in undifferentiated genital tubercle and 248 other tissues.
DR Genevisible; Q9Z1D7; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 6.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
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..501
FT /note="Zinc finger and SCAN domain-containing protein 12"
FT /id="PRO_0000047404"
FT DOMAIN 51..132
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 269..291
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 297..319
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 325..347
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..375
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..403
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..431
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 455..477
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 483..501
FT /note="C2H2-type 8; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..255
FT /note="Polar 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 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43309"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O43309"
FT CONFLICT 67
FT /note="L -> V (in Ref. 1; AAD00104)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..150
FT /note="KP -> NA (in Ref. 1; AAD00104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 57492 MW; 6368CF1E1BC661D2 CRC64;
MTSTSDTKVC KNQGGLLEIK MEEECKYTTR QDRNLQKNTY NRDVFRKYFR QFCYQETSGP
REALSRLREL CRQWLRPDLN SKEQILELLV LEQFLTILPG ELQAWVQEQN PESVEEVVTV
LEDLERELDE LGYRASVQTE EQVTFQEVKP LATEQKPSVS LQFVKAKPGC ELAGREAQEE
QVSGVETGNE PRNVTLKQGL WEGTEAEQNP ASRLAKDALE CEEAHNPGEE SSGISHEDSQ
PLRNENGVNS PANSEYAKHQ SICPGRKVHG CDECGKSFTQ HSRLIEHKRV HTGDRPYKCE
VCGKTFRWRT VLIRHKVVHT GEKPYKCNEC GRAFGQWSAL NQHQRLHSGE KHYHCNECGK
AFCQKAGLFH HLKSHRRNRP YQCLQCNKSF NRRSTLSQHQ GVHTGAKPYE CNDCGKAFVY
NSSLATHQET HHKEKPFTQS GPIQQQRNHT KEKPYKCSVC GKAFIQKISL IEHEQIHTGE
RPYKCAEGGK AFIQMSELTE H
