ID   ZN331_PONAB             Reviewed;         463 AA.
AC   Q5REA0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Zinc finger protein 331;
GN   Name=ZNF331;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation. May play a
CC       role in spermatogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; CR857633; CAH89907.1; -; mRNA.
DR   RefSeq; NP_001124893.1; NM_001131421.1.
DR   AlphaFoldDB; Q5REA0; -.
DR   SMR; Q5REA0; -.
DR   STRING; 9601.ENSPPYP00000011604; -.
DR   Ensembl; ENSPPYT00000012048; ENSPPYP00000011604; ENSPPYG00000010360.
DR   GeneID; 100171759; -.
DR   KEGG; pon:100171759; -.
DR   CTD; 55422; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161267; -.
DR   HOGENOM; CLU_002678_44_0_1; -.
DR   InParanoid; Q5REA0; -.
DR   OMA; WACLDST; -.
DR   OrthoDB; 1318335at2759; -.
DR   TreeFam; TF341817; -.
DR   Proteomes; UP000001595; Chromosome 19.
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:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 8.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
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..463
FT                   /note="Zinc finger protein 331"
FT                   /id="PRO_0000289999"
FT   DOMAIN          6..78
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         131..153
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         159..181
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         187..209
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         215..237
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         243..265
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         271..293
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         299..321
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         327..349
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         355..377
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         383..405
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         411..433
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         439..461
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        109
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQX6"
FT   CROSSLNK        400
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQX6"
SQ   SEQUENCE   463 AA;  53769 MW;  732572D6BA027A65 CRC64;
     MAQGLVTFAD VAIDFSQEEW ACLNSAQRDL YWDVMLENYS NLVSLDLESA YENKSLPTEK
     NIHEIRASKR NSDRRSKSLG RNWICEGMLE RPQRSRGRYV NQMIINYVKR PATREGTPPR
     THQRHHKENS FECKDCGKAF SRGYQLSQHQ KIHTGEKPYE CKECKKAFRW GNQLTQHQKI
     HTGEKPYECK DCGKAFRWGS SLVIHKRIHT GEKPYECKDC GKAFRRGDEL TQHQRFHTGE
     KDYECKDCGK TFSRVYKLIQ HKRIHSGEKP YECKDCGKAF ICGSSLIQHK RIHTGEKPYE
     CQECGKAFTR VNYLTQHQKI HTGEKPHECK ECGKAFRWGS SLVKHERIHT GEKPYKCTEC
     GKAFNCGYHL TQHERIHTGE TPYKCKECGK AFIYGSSLVK HERIHTGVKP YGCTECGKSF
     SHGHQLTQHQ KTHSGAKSYE CKECGKACNH LNHLREHQRI HNS