ID A0A3B3RJQ2_9TELE Unreviewed; 1410 AA.
AC A0A3B3RJQ2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Zinc finger protein 536 {ECO:0000313|Ensembl:ENSPKIP00000018862.1};
GN Name=ZNF536 {ECO:0000313|Ensembl:ENSPKIP00000018862.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000018862.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000018862.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSPKIT00000035698.1; ENSPKIP00000018862.1; ENSPKIG00000004247.1.
DR GeneTree; ENSGT00940000156397; -.
DR Proteomes; UP000261540; 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 Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
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; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
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 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 142..169
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 170..192
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 306..334
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 405..432
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 662..689
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 760..787
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 239..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 153683 MW; DA337FCEE1045E04 CRC64;
MRPPSKGMEE SSLCLGVSSA VPEADAHLSN SVLNGRYPIS QKLHQLTAQL GHAFPDLQSR
QPIPEEKAAA PLDEKSHAPL ASQPISSQMA LLANQLNRDI DATAGLNING RVDLQQFLNG
QNLGIMSQMN DIEDDARKNR KYPCPLCGKR FRFNSILSLH MRTHTGEKPF KCPYCDHRAA
QKGNLKIHLR THKLGNLGKG RGRVREENRL LHELEERAIL RDKQMRSSLL QPRLDLKQHP
QAVQHQHPAP QSHQQQPQPT SACGLLTPAG QGPATAVAAA DNPVQPSASP KPAGPQDEQA
AAPSGFRCTF CKGKFKKREE LERHIRILHK PYKCTLCEFA ASHEEDLIGH VEKAHITAES
APGQGSGFGG EKPANEFRCE VCGQVFSQAW FLKGHMRKHK DSFEHCCQIC GRRFKEPWFL
KNHMKVHLNK LAMKSKPPDA DVPLGMNSLA QEAQANLYSR YISCLQSGLL SPDKSSLSDQ
HQMLAKAGIA MKEKEMLGKL LSPMGGMGHG LADGEKRPLL GCLNLVPPLK SSCMERLQAA
AKVAEMDPLN SYQTWQILGR GMAMERSFMP KEPQRGTRGP DEDLLSTSML FAKDKHNFPL
LGGSDVHKQK LHVETAQGIK GGNGAPSCKD DGAFEGHRDF AGHCVRGPGF DCGPAGAKEK
PVECPDCGRV FRTYHQMVVH SRVHGKEPRL PEEGPQHGGG LDERRGSASD PESQSISRST
TPGSSNVTEE SGAGGGHSQT GSAQEDSPHP SSPSSGEKPY RCPHCDYAGT QSASLKYHLE
RHHRERQNGG GSSYGHAAEH KEEHAASKSG VFVRPEVLRG VFKGVPGSMD FRGGQMLPHQ
WAAPGMQDRD RHGHGHGAST ENPPDHTKSQ ETPSAEGPAS FSDLSRAYQS MVGNGMNFQG
SLQAFMDSFV LSSLKKDKEM RDKAQIQPHL GADGMEARAK RGEAAEERSD TKPTGSKPEK
SQYEPLDLSV RPDSVSLPGS AVTIQDNVAW HGCLFCPFQT SSVELMALHL QANHLGKAKR
KEGGFLDAKA GEASSMGKAG LMSAVLHPGY EAVSAKPEPH MDKLVQQELG KEIKGEPRGP
AWSNHMESAG FQNDFFKPFG MYDAAPGGLV PQGFGGSGPE QQDPLKQPSD VKNSKPSAMA
ELSEGHPYSD SEPTKEREHP RSDDEFCPAD RATRPGSDDD EDEAEEEDED GEEEEMEEGE
ENRSMQLPVL SEDPQKAGAA RATLSPLLEK PWRGLSLLSS AGVPQGSPRA EQGRLEQQMS
ILSVLRAYSA ENLAAFNGLG STSNNTGAIK RPDMPGQKPF QCRFCPYGAT QKGNLKTHVL
CVHRMPFDNS QYPDRRFKRP RVDADAPCKL EDSPPGVSHL SAGDPPALEG PQSGEPQQPG
DSEGLHSSRH CEAPPVWEFT LPRQPQPQQE
//