ID   ZN322_MACFA             Reviewed;         402 AA.
AC   Q4R7X8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Zinc finger protein 322;
DE   AltName: Full=Zinc finger protein 322A;
GN   Name=ZNF322; Synonyms=ZNF322A; ORFNames=QtsA-14134;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional activator. Important for maintenance of
CC       pluripotency in embryonic stem cells. Binds directly to the POU5F1
CC       distal enhancer and the NANOG proximal promoter, and enhances
CC       expression of both genes. Can also bind to numerous other gene
CC       promoters and regulates expression of many other pluripotency factors,
CC       either directly or indirectly. Promotes inhibition of MAPK signaling
CC       during embryonic stem cell differentiation.
CC       {ECO:0000250|UniProtKB:Q8BZ89}.
CC   -!- SUBUNIT: Interacts with POU5F1. {ECO:0000250|UniProtKB:Q8BZ89}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BZ89}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8BZ89}. Note=Mainly found in the nucleus.
CC       {ECO:0000250|UniProtKB:Q8BZ89}.
CC   -!- MISCELLANEOUS: Significantly enhances POU5F1/OCT4-SOX2-KLF4-MYC (OSKM)
CC       mediated reprogramming of mouse embryonic fibroblasts into induced
CC       pluripotent stem cells, and can also substitute for SOX2 in this
CC       process. {ECO:0000250|UniProtKB:Q8BZ89}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AB168683; BAE00794.1; -; mRNA.
DR   RefSeq; NP_001274556.1; NM_001287627.1.
DR   RefSeq; XP_005553859.1; XM_005553802.2.
DR   RefSeq; XP_005553860.1; XM_005553803.2.
DR   RefSeq; XP_015304337.1; XM_015448851.1.
DR   AlphaFoldDB; Q4R7X8; -.
DR   SMR; Q4R7X8; -.
DR   STRING; 9541.XP_005553859.1; -.
DR   Ensembl; ENSMFAT00000050955; ENSMFAP00000011634; ENSMFAG00000017291.
DR   Ensembl; ENSMFAT00000089863; ENSMFAP00000046520; ENSMFAG00000017291.
DR   Ensembl; ENSMFAT00000095767; ENSMFAP00000055327; ENSMFAG00000017291.
DR   GeneID; 102146172; -.
DR   KEGG; mcf:102146172; -.
DR   CTD; 79692; -.
DR   VEuPathDB; HostDB:ENSMFAG00000017291; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162956; -.
DR   OMA; CNMGEKG; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000233100; Chromosome 4.
DR   Bgee; ENSMFAG00000017291; Expressed in pituitary gland and 13 other tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE   2: Evidence at transcript level;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..402
FT                   /note="Zinc finger protein 322"
FT                   /id="PRO_0000047530"
FT   ZN_FING         43..65
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         71..93
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         99..121
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         127..149
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         155..177
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         183..205
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         211..233
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         239..261
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         267..289
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         293..315
FT                   /note="C2H2-type 10; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         351..373
FT                   /note="C2H2-type 11; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6U7Q0"
SQ   SEQUENCE   402 AA;  46882 MW;  04C41BE0EC4725F3 CRC64;
     MYTSEERCNQ RTQKRKIYNV CPQKGKKIFI HVHAITQIDG HIYQCLECKQ NFCENLALIM
     CERTHTGEKP YKCDMCEKTF VQSSDLISHQ RIHNYEKPYK CSKCEKSFWH HLALSGHQRT
     HAGKKFYTCD ICGKNFGQSS DLLVHQRSHT GEKPYLCSEC DKCFSRSTNL IRHRRTHTGE
     KPFKCLECEK AFSGKSDLIS HQRTHTGERP YKCNKCEKSY RHRSAFIVHK RVHTGEKPYK
     CGACEKCFGQ KSDLIVHQRV HTGEKPYKCL ECMRSFTRSA NLIRHQATHT HTFKCLEYEK
     SFNCSSDLIV HQRIHMEEKP HQWSTCESGF LLGMDFVAQQ KMRTQTEELH YKYTVCDKSF
     HQSSALLQHQ TVHTGEKPFI CNVSEKGLEL SPPHASEASQ MS