ID A0A091D206_FUKDA Unreviewed; 1382 AA.
AC A0A091D206;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Zinc finger protein 536 {ECO:0000313|EMBL:KFO26124.1};
GN ORFNames=H920_12480 {ECO:0000313|EMBL:KFO26124.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO26124.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO26124.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO26124.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000256|ARBA:ARBA00006991}.
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DR EMBL; KN123237; KFO26124.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000013207; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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 Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45925; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR45925:SF2; ZINC FINGER PROTEIN 536; 1.
DR Pfam; PF00096; zf-C2H2; 5.
DR Pfam; PF16606; zf-C2H2_assoc; 1.
DR Pfam; PF13909; zf-H2C2_5; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
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|PROSITE-ProRule:PRU00042}.
FT DOMAIN 130..157
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 158..180
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 278..306
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 349..376
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 377..404
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 634..661
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 754..781
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 782..809
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1382 AA; 150475 MW; 81F51AD8A62A9DC0 CRC64;
MEEASLCLGV SSAAPEAEPH LSSPVLNGQY AMSQKLHQIT SQLSHAFPEL HPRPNPEEKI
PAPLDEKAHV AMSGQPMGSQ MALLANQLGR DVDTSLNGRV DLQQFLNGQN LGIMSQMSDI
EDDARKNRKY PCPLCGKRFR FNSILSLHMR THTGEKPFKC PYCDHRAAQK GNLKIHLRTH
KLGNLGKGRG RVREENRLLH ELEERAILRD KQMKSSLLQP RPDLKPPPHV QQAPQAAPLA
ACNLALPANH SVPDVANPVP SPKPVNVQED AVAPAAGFRC TFCKGKFKKR EELDRHIRIL
HKPYKCTLCD FAASQEEELI SHVEKAHITA ESAQGQGPNS AGEQSANEFR CEVCGQVFSQ
AWFLKGHMRK HKDSFEHCCQ ICGRRFKEPW FLKNHMKVHL NKLSVKNKSP SEPEVPVPMG
SISQEAHANL YSRYLSCLQS GFIAPDKAGL SEPGQLYGKG ELPMKEKEVL GKLLSPISSM
AHVPEGDKHS LLGCLNLVPP LKSSCIERLQ AAAKAAEMDP VNSYQAWQLM ARGMAMEHGF
LSKEHQLQRN HEDVLANAGV MFDKEKREYV LVGADGSKQK MPADLVHSTK VGNQRDLPNK
LDPLEGSRDF LSHGLNQTLE YNLQGPGNMK EKPTECPDCG RVFRTYHQVV VHSRVHKRER
RGEEDGLHTG LDERRGSGSD QESQSVSRST TPGSSNVTEE SGVGGGLSQP GSAQEDSPHP
SSPSSSDIGE EAGRSAGVQQ PALLRDRSLG SAMKDCPYCG KTFRTSHHLK VHLRIHTGEK
PYKCPHCDYA GTQSASLKYH LERHHRERQN GAGPLSGQPS SQDHKDEMSG KASLFIRPDI
LRGAFKGLPG IDFRGGPASQ QWTSGVLSSG DHSGQATGMC TDAPPDALKG ADLHSKSTHF
SEIGRAYQSI VSNGVNFQGS LQAFMDSFVL SSLKKKDMKD KALSDPLSMK VHGVEGNEEK
SSGKSSQRKS EKSQYEPLDL SVRPDAASLP GSSVTVQDSI TWHGCLFCAF TTSSMELMAL
HLQANHLGKA KRKDNATGGT ANCKEQVREA SRMALLPSVQ SNKEMGLSST MGSLDSVSEK
MAQGQAKETL GDQKSGPWPS HVDPAFCNFP PDFYKQFGVY PGMVGSGASS SCPNKDPDGK
AHPEDDAPIL IPETSKSTAD DLSDIASSED MDSSKGENND EEDLETEPEM MSSSKPLSAL
SKDSSSDSGD SLLPTGTPQP VQGLVSPLAP AMEKQWHSPG LLPAQDPSGG LPKPERGPAG
LEKPLNMLSV LRAYSADGLA AFNGLASSTA NSGCIKRPDL CGHRPFQCRY CPYSASQKGN
LKTHVLCVHR MPFDNSQYPD RRFKRSRVDS EASGNFEEPT AVKAGSSAEL TEEGTKGQEE
SN
//
