ZSC21_GORGO
ID ZSC21_GORGO Reviewed; 473 AA.
AC A1YEV9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 21;
GN Name=ZSCAN21;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
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; DQ976474; ABM46677.1; -; Genomic_DNA.
DR AlphaFoldDB; A1YEV9; -.
DR SMR; A1YEV9; -.
DR STRING; 9593.ENSGGOP00000011164; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; A1YEV9; -.
DR Proteomes; UP000001519; Unplaced.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Reference proteome; Repeat; Spermatogenesis;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..473
FT /note="Zinc finger and SCAN domain-containing protein 21"
FT /id="PRO_0000285487"
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 127..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..171
FT /note="Polar 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; 53716 MW; F578A23C8DCC0D7F CRC64;
MMTKVLGMAP VLGPRPPQEQ VGPLMVKVEE KEEKGKYLPS LEMFRQRFRQ FGYHDTPGPR
EALSQLRVLC CEWLRPEIHT KEQILELLVL EQFLTILPQE LQAWVQEHCP ESAEEAVTLL
EDLERELDEP GHQVSTPPNE QKPVWEKISS SGTAKESPSS MQPQPLETSH NYESWGPLYI
QESGEEQEFA QDPRKVRDCR LSTQHEESAD EQKGSEAEGL KEDIISVIIA NKPEASLERQ
CVNLENEKGT KPPLQEAGSK KGRESVPTKP TPGERRYICA ECGKAFSNSS NLTKHRRTHT
GEKPYVCTKC GKAFSHSSNL TLHYRTHLVD RPYDCKCGKA FGQSSDLLKH QRMHTEEAPY
QCKDCGKAFS GKGSLIRHYR IHTGEKPYQC NECGKSFSQH AGLSSHQRLH TGEKPYKCKE
CGKAFNHSSN FNKHHRIHTG EKPYWCHHCG KTFCSKSNLS KHQRVHTGEG EAP
