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 27-MAR-2024, entry version 115.
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; ENSPPYT00000012048.3; ENSPPYP00000011604.2; ENSPPYG00000010360.3.
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; LDWMCEG; -.
DR OrthoDB; 3120634at2759; -.
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 DNA-templated transcription; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 12.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24399:SF78; C2H2-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24399; ZINC FINGER AND BTB DOMAIN-CONTAINING; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR Pfam; PF13912; zf-C2H2_6; 2.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
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
//
