FOG1_XENLA
ID FOG1_XENLA Reviewed; 1061 AA.
AC Q9I9K0;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Zinc finger protein ZFPM1;
DE AltName: Full=Friend of GATA;
DE Short=xFOG;
DE AltName: Full=Friend of GATA protein 1;
DE Short=FOG-1;
DE Flags: Fragment;
GN Name=zfpm1; Synonyms=fog, fog1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH CTBP.
RC TISSUE=Spleen;
RX PubMed=10769228; DOI=10.1242/dev.127.10.2031;
RA Deconinck A.E., Mead P.E., Tevosian S.G., Crispino J.D., Katz S.G.,
RA Zon L.I., Orkin S.H.;
RT "FOG acts as a repressor of red blood cell development in Xenopus.";
RL Development 127:2031-2041(2000).
CC -!- FUNCTION: Transcription regulator that plays an central role in red
CC blood cell differentiation. Essential cofactor that acts via the
CC formation of a heterodimer with transcription factors of the GATA
CC family GATA1 and GATA2. Such heterodimer can both activate or repress
CC transcriptional activity, depending on the cell and promoter context.
CC Acts as a repressor of red blood cells, probably by modulating activity
CC of GATA1. {ECO:0000269|PubMed:10769228}.
CC -!- SUBUNIT: Interacts with corepressor CTBP. Interacts with the N-terminal
CC zinc-finger of GATA1 and probably GATA2. {ECO:0000269|PubMed:10769228}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart and brain. Also
CC expressed in ventral blood island and adult spleen.
CC {ECO:0000269|PubMed:10769228}.
CC -!- DOMAIN: Some of the CCHC FOG-type zinc fingers probably directly bind
CC to GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of
CC the CCHC FOG-type zinc finger is probably essential for the interaction
CC with 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; AF241228; AAF64473.1; -; mRNA.
DR AlphaFoldDB; Q9I9K0; -.
DR Proteomes; UP000186698; Genome assembly.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0010604; P:positive regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0045595; P:regulation of cell differentiation; IEA:UniProt.
DR InterPro; IPR039746; FOG.
DR InterPro; IPR034731; ZF_CCHC_FOG.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12958; PTHR12958; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS51810; ZF_CCHC_FOG; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 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..1061
FT /note="Zinc finger protein ZFPM1"
FT /id="PRO_0000221046"
FT ZN_FING 152..185
FT /note="CCHC FOG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 204..228
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 234..256
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..285
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 508..541
FT /note="CCHC FOG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 623..656
FT /note="CCHC FOG-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 759..792
FT /note="CCHC FOG-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT ZN_FING 869..892
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1023..1056
FT /note="CCHC FOG-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT REGION 349..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..742
FT /note="Interaction with CTBP"
FT /evidence="ECO:0000250"
FT REGION 917..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 770
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 783
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 788
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1031
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1034
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1047
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT BINDING 1052
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153"
FT NON_TER 1
SQ SEQUENCE 1061 AA; 114181 MW; 0119E6C377500F6E CRC64;
WNGPDELELE ISSTDGVGHI RARNQLHKGF SWGPYKGNFT GSSSSPGPAD LNISPSWDVD
GDCWLKYVTL VSCEAEANAV LYRKGDLIWC KTSQIVEQDE VIQAFLKAEP QAIPNYTIKE
EPGETSQCTS TLPEFQLLPQ QAGMAAILAT AVVNKDVFPC KDCGIWYRSE RNLQAHLMYY
CASRQSSTSP SMEEKAKDSY PNERICPFPQ CKKSCPSTSS LEIHMRSHSG ERPFVCLICL
SAFTTKANCE RHLKVHTDTL NGVCHGCGFI STTRDILYSH LVTNHMICQP GSKVDVYPVV
KAVPAVKSSN PVVSQIASSS LLKCGLCGFL AEDFQVFNHA LLHTTNPVPS ATHSVKSPPE
NINEKQNPES QENGNAKSPI SSSSSASSRS EETPLKLYIK QEPEGQLSIS EAGSTTCEAK
DGVALVQSPA IKVKTEMSSP TPGSSPVPNE TGAATGGGTV IIPHYVFGHE ATAAIVPQAS
EILAKMSELV HSRLKQGQAV TPAGFSGSAV PKGATCFECE ITFNNINNYY VHKRLYCSGR
HVSDENSSSA RKVKALPART ALASGFSSTE QEASPPQEDA GEESSAPVVA VKLEENSGMD
CEGAGSGHVS EGSQSPSSLD DPEEDPNRTV CGACNIRFSR HETYVVHKRY YCASRHDPPL
RRREVNKPGP PYTTQPTPRT RKRRKLYEIH GVAPTESTPP SPHTLGRVEA MALMPGLIPA
PVMPSPSSSP DAVDGPIDLS KKPRLVAEAP VPSAAATVAP LADYHECTAC RISFNSLESY
LAHKKFSCPT APLQQKTIQQ LQKVKSPSSA TGKLVDDTVK VKVESKAALS PGSVSDTIQP
LALPFSTISD PKQLQQYSSV TEASLSATTT CPYCPHNVII RGDLLEHFRS VHGLILAKPT
AGHRLQTTIM EVLVPARGQT SSASENSLPS PPVSSASPLQ LPGLRRENSN YKDTTSSSSS
VNGSPILTST PRPLLPTSPA PPSNSLPLAE SRREDGLPRV PSQVLLPGDK AMQPPKPSLI
SPVPNGNHRY CRLCNIKFSS LSTFIAHKKY YCSSHAAEHV K
