ID A0A1S3GCB4_DIPOR Unreviewed; 1003 AA.
AC A0A1S3GCB4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Zinc finger protein 445 {ECO:0000313|RefSeq:XP_012885657.1};
GN Name=Znf445 {ECO:0000313|RefSeq:XP_012885657.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012885657.1};
RN [1] {ECO:0000313|RefSeq:XP_012885657.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012885657.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
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DR RefSeq; XP_012885657.1; XM_013030203.1.
DR AlphaFoldDB; A0A1S3GCB4; -.
DR GeneID; 105996190; -.
DR KEGG; dord:105996190; -.
DR CTD; 353274; -.
DR InParanoid; A0A1S3GCB4; -.
DR OrthoDB; 5256517at2759; -.
DR Proteomes; UP000081671; 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 DNA-templated transcription; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 11.
DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24381; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24381:SF154; ZINC FINGER PROTEIN 550; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 56..138
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 222..292
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 500..527
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 528..555
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 582..609
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 610..637
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 738..765
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 766..789
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 817..844
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 845..872
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 952..979
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 980..1003
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 198..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 115054 MW; D5A6A0D47A1EB1B6 CRC64;
MPPGRWNFVH PVRAQAPRGR GRLSKIKKEE EEDEGYTLGE TARPQTLNHA GQELFRQLFR
QLRYHESSGP LETLSRLREL CRWWMRPDVL SKAQMLELLV LEQFLSILPG ELRAWVQLHS
PVSGQEAVAL LEELPRDFDG TSQMDPSPVS QAVHWLGTGA LQSPQIQPEA SSLGNSSAPW
DHLEPPSEIG VHDFLSRQSD TPSVQVSDPS QKEESPGDQE ALTFKDVEVI FSQDEWGCLN
SAQRNLYQDV MLENYGTLAS LVGSFSKPAL ISWLETREPW GLNIYTVQPE GETDTACPEG
GELQPQTSQI QSFLGHMKSD VPSEHPLTDI QEETGLRDSV EQENNDVHLP CGNPIQVRVK
TEETTFSPGI GDESQGSEQS NTFNLKPSTC SKTSRKKRAL KHGRGRPFRK NSHPYDYKKY
GKGLRHAQRA LSLHPRIPID TKENEKDTCG KSFSLPSPPP QEPTPDNPGM LNTSTDCGTP
FHPSPHLLFH PRLPTPEKIF KCRVCEKAFK WNSNCLRHEK IHTGVKPYKC SICEKAFQRL
SAYRLHQHTH AKQMCTPPPP PPLYEDAGLG YHVREQNGEK YLDCSHCGKS FHCKSYVLEH
QRIHTKEKPY RCGSCRKSFR WRSNFNRHVR QHREQEEGRQ HKYASQDPPT EEKTFHRPPP
KNTFNPKKKL LEHQIVHSRD KLYQCNECGQ GFAFRSAFIV HKKNHAIQRK TEGQRLSLGQ
ETACAAPHSR GNAEEKPYKC SQCDKVFRHH SFLLIHQRVH TREKPYQCKE CGKAFRWTSN
LYRHQRQHSV SLHYKYRRAP KEAPSPQPDS PSDGKHFWCQ ECGKTFTRKR SLVDHMGIHS
GEKRYKCNLC GKSYDRNYRL VNHQRIHATD RPFMSQWCGK EFRDLHTFSL HPKAHTRVAQ
TKRTRPTVTD LDAQVQEFKA GGTKSLESSE GPSTQDSVVP ELPNRPTEKK GHKCNLCGKA
FCKNSLLLSH KRFHTRERPF KCAVCGKTFR WSSNLARHMK NHI
//
