ID   ZSC21_PONPY             Reviewed;         473 AA.
AC   A2T7L7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   02-JUN-2021, entry version 68.
DE   RecName: Full=Zinc finger and SCAN domain-containing protein 21;
GN   Name=ZSCAN21;
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: Strong transcriptional activator (By similarity). Plays an
CC       important role in spermatogenesis; essential for the progression of
CC       meiotic prophase I in spermatocytes (By similarity).
CC       {ECO:0000250|UniProtKB:Q07231}.
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; DQ977501; ABM89295.1; -; Genomic_DNA.
DR   PRIDE; A2T7L7; -.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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; 7.
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; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   3: Inferred from homology;
KW   Activator; Differentiation; DNA-binding; Isopeptide bond; Meiosis;
KW   Metal-binding; Nucleus; Repeat; Spermatogenesis; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..473
FT                   /note="Zinc finger and SCAN domain-containing protein 21"
FT                   /id="PRO_0000285490"
FT   DOMAIN          45..127
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   ZN_FING         277..299
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         305..327
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         333..354
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         360..382
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         388..410
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         416..438
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         444..466
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          123..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5A6"
FT   CROSSLNK        221
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5A6"
FT   CROSSLNK        232
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5A6"
FT   CROSSLNK        349
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5A6"
SQ   SEQUENCE   473 AA;  53647 MW;  9D48493E7722968D CRC64;
     MMTKVLGMAP VLGPRPPQEQ VGPLMVKVEE KEEKGKYLPS LEMFRQRFRQ FGYHDTPGPR
     EALSQLRVLC CEWLRPEIHT KEQILELLVL EQFLTILPQE LQAWVQEHCP ESAEEAVTLL
     EDLERELDEP GHQVSTPPNE QKPVWEKISS SGTAKESPSS VQPQPLETSH KYESWGPLYI
     QESGEEQAFA QDPRKVRDCR LSTQHEESAD EQKASEAEGL KGDIISVIIA NKPEARLERQ
     CVNLXXEKGT KPPLQESGSK KGRESVPTKP TPGERRYICA ECGKAFSNSS NLTKHRRTHT
     GEKPYVCTKC GKAFSHSSNL TLHYRTHLVD RPYDCKCGKA FGQSSDLLKH QRMHTEEAPY
     QCKDCGKAFS GKGSLIRHYR IHTGEKPYQC NECGKSFSQH AGLSSHQRLH TGEKPYKCKE
     CGKAFNHSSN FNKHHRIHTG EKPYWCHHCG KTFCSKSNLS KHQRVHTGEG EAP