ZSCA4_AILME
ID ZSCA4_AILME Reviewed; 430 AA.
AC D2HQI1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 4;
GN Name=ZSCAN4; ORFNames=PANDA_014157;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- FUNCTION: Embryonic stem (ES) cell-specific transcription factor
CC required to regulate ES cell pluripotency. Binds telomeres and plays a
CC key role in genomic stability in ES cells by regulating telomere
CC elongation. Acts as an activator of spontaneous telomere sister
CC chromatid exchange (T-SCE) and telomere elongation in undifferentiated
CC ES cells (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC Chromosome, telomere {ECO:0000250}.
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DR EMBL; GL193184; EFB14447.1; -; Genomic_DNA.
DR AlphaFoldDB; D2HQI1; -.
DR SMR; D2HQI1; -.
DR STRING; 9646.ENSAMEP00000005165; -.
DR PRIDE; D2HQI1; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; D2HQI1; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
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:0010833; P:telomere maintenance via telomere lengthening; ISS:UniProtKB.
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; 3.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 3: Inferred from homology;
KW Chromosome; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Telomere; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..430
FT /note="Zinc finger and SCAN domain-containing protein 4"
FT /id="PRO_0000394243"
FT DOMAIN 44..126
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 309..331
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..359
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..387
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 393..415
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 48888 MW; 7EF2EEDD716F55E4 CRC64;
MASDLRISFQ GEPSRNDPGS ENLEHKPSQG PAVQEEEETY EFLRTQLSLL QNSNNSCARQ
ELQNLYKLFH SWLQPEKHSK DEIISCLVLE QFMINGHCSD RSMLKEKWNA SGRNLEKFME
DLTDESMKPP GLVHVHMQGQ EALFSENMPL KEVIVHLTKQ LSVGSPTGTD METPSWTPQD
TSLETGQGEW GDKENGDNIY HINDSITSQG NEIPSLLIIR EEDYPRPEED SVSLKNPLSS
RKAGLGMSGS QEGSLKGPSY QDVLMEGGPG FLSQSIQVSP EPVPTHQRTE GNSTRGGHQE
RCREAQNSYR CEKCPKIFRY FSQLKAHQRR HNNERTFTCA ECNRGFFQAS DLHVHQKIHA
EEKPFTCSTC EKSFSHKTNL LAHERIHTGE KPYECSLCHR SYRQSSTYHR HLRNHQKSAF
RGVSSTPEAS
