FOG1_DANRE
ID FOG1_DANRE Reviewed; 224 AA.
AC P60622;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Zinc finger protein ZFPM1;
DE AltName: Full=Friend of GATA protein 1;
DE Short=FOG-1;
DE Short=Friend of GATA 1;
DE AltName: Full=Zinc finger protein multitype 1;
DE Flags: Fragment;
GN Name=zfpm1; Synonyms=fog1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH GATA1.
RX PubMed=14585986; DOI=10.1128/mcb.23.22.8295-8305.2003;
RA Nishikawa K., Kobayashi M., Masumi A., Lyons S.E., Weinstein B.M.,
RA Liu P.P., Yamamoto M.;
RT "Self-association of Gata1 enhances transcriptional activity in vivo in
RT zebra fish embryos.";
RL Mol. Cell. Biol. 23:8295-8305(2003).
CC -!- FUNCTION: Transcription regulator that modulates expression mediated by
CC transcription factors of the GATA family. Cofactor that acts via the
CC formation of a heterodimer with transcription factors of the GATA
CC family. Such heterodimer can both activate or repress transcriptional
CC activity, depending on the cell and promoter context (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the N-terminal zinc finger of gata1.
CC {ECO:0000269|PubMed:14585986}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at the lateral plate mesoderm.
CC {ECO:0000269|PubMed:14585986}.
CC -!- DOMAIN: The CCHC FOG-type zinc fingers probably directly bind to GATA-
CC type zinc fingers. The Tyr residue adjacent to the last Cys of the CCHC
CC FOG-type zinc finger is probably essential for the interaction with
CC GATA-type zinc fingers (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01153}.
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DR EMBL; AB112073; BAD00982.1; -; mRNA.
DR AlphaFoldDB; P60622; -.
DR STRING; 7955.ENSDARP00000060948; -.
DR PaxDb; P60622; -.
DR ZFIN; ZDB-GENE-050419-238; zfpm1.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0030218; P:erythrocyte differentiation; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IGI:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0030219; P:megakaryocyte differentiation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR039746; FOG.
DR InterPro; IPR034731; ZF_CCHC_FOG.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR12958; PTHR12958; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51810; ZF_CCHC_FOG; 2.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..>224
FT /note="Zinc finger protein ZFPM1"
FT /id="PRO_0000221045"
FT ZN_FING 29..62
FT /note="CCHC FOG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 162..195
FT /note="CCHC FOG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT NON_TER 1
FT NON_TER 224
SQ SEQUENCE 224 AA; 23956 MW; 8B8BDCDFF1A60476 CRC64;
MSEMVHSRLK QGQGPAAAQQ SFYPPGSPAS VHKGATCFEC DITFNNINNF YVHKRLYCSS
RHQQGETGGL VKEGAVTAAA PPVSHAASPQ ARPVSRAASA SPSCPDPAPG GTASEPKVVE
VKIEDPGLKD ATCSSSSEGE GPGGGQASEG SQSPSGSAED QDDDPTRTFC QACNIRFSRH
DNYIVHKRFY CASRHDPTNQ RPHSGKAAFL PQPIRTRKRK KMYE
