ZSC21_PANTR
ID ZSC21_PANTR Reviewed; 473 AA.
AC A2T712;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 21;
GN Name=ZSCAN21;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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; DQ977351; ABM91967.1; -; Genomic_DNA.
DR RefSeq; NP_001129089.1; NM_001135617.1.
DR RefSeq; XP_009451515.1; XM_009453240.1.
DR RefSeq; XP_009451517.1; XM_009453242.1.
DR RefSeq; XP_009451518.1; XM_009453243.2.
DR AlphaFoldDB; A2T712; -.
DR SMR; A2T712; -.
DR STRING; 9598.ENSPTRP00000054464; -.
DR PaxDb; A2T712; -.
DR Ensembl; ENSPTRT00000061919; ENSPTRP00000054464; ENSPTRG00000019469.
DR GeneID; 463584; -.
DR KEGG; ptr:463584; -.
DR CTD; 7589; -.
DR VGNC; VGNC:4591; ZSCAN21.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161607; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; A2T712; -.
DR OMA; WEPLYIQ; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF338304; -.
DR Proteomes; UP000002277; Chromosome 7.
DR Bgee; ENSPTRG00000019469; Expressed in testis and 21 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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_0000285489"
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..167
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..167
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; 53675 MW; C5D4D048A6690FB8 CRC64;
MMTKVLGMAP VLGPRPPQEQ VGPLMVKVEE KEEKGKYLPS LEMFRQRFRQ FGYHDTPGPR
EALSQLRVLC CEWLRPEIHT KEQILELLVL EQFLTILPQE LQAWVQEHCP ESAEEAVTLL
EDLERELDEP GHQVSTPPNE QKPVWEKISS SGTAKESPSS MQPQPLETCH KYESWGPLYI
QESGEEQEFA QDPRKVRDCR LSTQHEESAD EQKGSEAEGL KGDIISVIIA 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
