ID I3N965_ICTTR Unreviewed; 736 AA.
AC I3N965;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Myeloid zinc finger 1 {ECO:0000313|Ensembl:ENSSTOP00000020911.1};
GN Name=MZF1 {ECO:0000313|Ensembl:ENSSTOP00000020911.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000020911.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000020911.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
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DR EMBL; AGTP01123227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005342466.1; XM_005342409.2.
DR AlphaFoldDB; I3N965; -.
DR STRING; 43179.ENSSTOP00000020911; -.
DR Ensembl; ENSSTOT00000026660.2; ENSSTOP00000020911.1; ENSSTOG00000020983.2.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00950000182890; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; I3N965; -.
DR OMA; CEGGFAH; -.
DR OrthoDB; 4850622at2759; -.
DR TreeFam; TF337913; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 13.
DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47772:SF4; REDUCED EXPRESSION 2-RELATED; 1.
DR PANTHER; PTHR47772; ZINC FINGER PROTEIN 200; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 44..126
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 358..385
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 386..413
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 414..441
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 442..464
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 487..514
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 515..542
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 543..570
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 571..598
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 599..626
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 627..654
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 655..682
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 683..710
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 711..736
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 82504 MW; A68A99B1B0679ACB CRC64;
MRPTVLGSPG NTPREDEEPV MVKLEDSEEE GEATLWDPGP EAAHLRFRCF RYEEAMGPQE
ALAQLRELCR QWLQPEVHSK EQMLELLVLE QFLGALPPEI QAHVQEQRPG NPEEAATLVD
RLRWELGGPR RWVTVQVQGQ EVLSEKMEAP SFQPLPQTKP QPPEPGPEMP PGTVQELPLG
LQVKEEPEVT ENPEYLESGP LPAAQKAVPA LLPKEAQAYG TALDHAYPQS ETGPEGPSWR
EHPGALWHDE TGSIFSPGFA LQMDSLSTEP GTVSNHLRVP WDMGVASLSS RIDSPSHEGG
FVHAVVLPSD PGSELDPTIE AVRPGMGPAL VAARWRTPRG RSRGRGRPST GAGAARGGRC
DMCGKVFSQR SNLLRHQKIH TGERPFVCGE CGRSFSRSSH LLRHQLTHTE ERPFVCCDCG
QGFVRSARLE EHRRVHTGEQ PFRCDECGQS FRQRSNLLQH QRIHGDPPGP GSAPPAPPGA
PEPPGPFPCS ECCESFTRRA VLLEHQAVHT GDKSFGCVEC GERFGRRSVL LQHRRVHSGE
RPFACTECGQ SFRQRSNLTQ HRRIHTGERP FACAECGKTF RQRPTLTQHL RVHTGEKPFG
CPECGQRFSQ RLKLTRHQRT HTGEKPYHCG ECGLGFTQVS RLTEHQRIHT GERPFACPEC
GQSFRQHANL TQHRRIHTGE RPYACPECGK AFRQRPTLTQ HLRTHRREKP FACQDCGRRF
HQSTKLIQHQ RVHSAE
//
