ID   ZN331_CANLF             Reviewed;         490 AA.
AC   Q6JLC9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Zinc finger protein 331;
GN   Name=ZNF331;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=15147412; DOI=10.1111/j.1365-2052.2004.01146.x;
RA   Meiboom M., Murua Escobar H., Winkler S., Nolte I., Bullerdiek J.;
RT   "Molecular characterization and mapping of the canine KRAB zinc finger gene
RT   ZNF331.";
RL   Anim. Genet. 35:262-263(2004).
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; AY375188; AAR21107.1; -; mRNA.
DR   RefSeq; NP_001003331.1; NM_001003331.2.
DR   AlphaFoldDB; Q6JLC9; -.
DR   SMR; Q6JLC9; -.
DR   STRING; 9612.ENSCAFP00000040347; -.
DR   PaxDb; Q6JLC9; -.
DR   GeneID; 414288; -.
DR   KEGG; cfa:414288; -.
DR   CTD; 55422; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q6JLC9; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000002254; Unplaced.
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..490
FT                   /note="Zinc finger protein 331"
FT                   /id="PRO_0000047534"
FT   DOMAIN          6..78
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         132..154
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         160..182
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         188..210
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         216..238
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         244..266
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         272..294
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         300..322
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         328..350
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         356..378
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         384..406
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         412..434
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         440..462
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          470..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        401
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQX6"
SQ   SEQUENCE   490 AA;  56874 MW;  2A400D18F9B69A9E CRC64;
     MAHGLVTFSD VAIDFSQEEW ACLDSRQRDL YWDVMLENYS NLVSLDLESP YGTKSLPTEK
     GIYEINLSKW NSNGKSKSLG LDWMCEGEFE GPQGPRESCF NQMIINYEKT PTCRENTSVR
     PHQRLHTREN SYECKECGKA FSRGYQLTQH QKIHTGEKPY ECKECKKAFR WGNQLTQHQK
     IHTGEKPYEC KDCGKAFRWG SSLVIHKRIH TGEKPYECKD CEKAFRRGDE LTQHQRFHTG
     EKDYECKDCG KTFSRVYKLI QHKRIHSGEK PYECKDCGKA FICGSSLVQH KRIHTGEKPY
     ECQECGKAFT RVNYLTQHQK IHTGEKPHEC KECGKAFRWG SSLVKHERIH TGEKPYKCTE
     CGKAFNCGYH LTQHERIHTG ETPYKCKECG KAFIYGSSLV KHERIHTGEK PYECKECGKA
     FSHGHQLTQH QKIHTGEKSF ECKECGKACN HVNHLREHQR VHTAEKPFEQ KEGAEASIQH
     SFLPQHKENP