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Database: UniProt
Entry: A0A3B3RMC3_9TELE
LinkDB: A0A3B3RMC3_9TELE
Original site: A0A3B3RMC3_9TELE 
ID   A0A3B3RMC3_9TELE        Unreviewed;      1383 AA.
AC   A0A3B3RMC3;
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:ENSPKIP00000018881.1};
GN   Name=ZNF536 {ECO:0000313|Ensembl:ENSPKIP00000018881.1};
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:ENSPKIP00000018881.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000018881.1}
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}.
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DR   Ensembl; ENSPKIT00000035709.1; ENSPKIP00000018871.1; ENSPKIG00000004247.1.
DR   Ensembl; ENSPKIT00000035719.1; ENSPKIP00000018881.1; 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; 6.
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; 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   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          135..162
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          163..185
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          299..327
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          370..397
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          398..425
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          778..805
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          806..833
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          232..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          966..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..702
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..907
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..1003
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1168..1182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1194..1224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1225..1246
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1383 AA;  150624 MW;  12F5E5804BFB3C27 CRC64;
     MEESSLCLGV SSAVPEADAH LSNSVLNGRY PISQKLHQLT AQLGHAFPDL QSRQPIPEEK
     AAAPLDEKSH APLASQPISS QMALLANQLN RDIDATAGLN INGRVDLQQF LNGQNLGIMS
     QMNDIEDDAR KNRKYPCPLC GKRFRFNSIL SLHMRTHTGE KPFKCPYCDH RAAQKGNLKI
     HLRTHKLGNL GKGRGRVREE NRLLHELEER AILRDKQMRS SLLQPRLDLK QHPQAVQHQH
     PAPQSHQQQP QPTSACGLLT PAGQGPATAV AAADNPVQPS ASPKPAGPQD EQAAAPSGFR
     CTFCKGKFKK REELERHIRI LHKPYKCTLC EFAASHEEDL IGHVEKAHIT AESAPGQGSG
     FGGEKPANEF RCEVCGQVFS QAWFLKGHMR KHKDSFEHCC QICGRRFKEP WFLKNHMKVH
     LNKLAMKSKP PDADVPLGMN SLAQEAQANL YSRYISCLQS GLLSPDKSSL SDQHQMLAKA
     GIAMKEKEML GKLLSPMGGM GHGLADGEKR PLLGCLNLVP PLKSSCMERL QAAAKVAEMD
     PLNSYQTWQI LGRGMAMERS FMPKEPQRGT RGPDEDLLST SMLFAKDKHN FPLLGGSDVH
     KQKLHVETAQ GIKGGNGAPS CKDDGAFEGH RDFAGHCVRG PGFDCGPAGA KEKPVECPDC
     GRVFRTYHQM VVHSRVHGKE PRLPEEGPQH GGGLDERRGS ASDPESQSIS RSTTPGSSNV
     TEESGAGGGH SQTGSAQEDS PHPSSPSSDA GEDSGRPAGI QPPSTPQHRE RPMGSAMKDC
     PYCGKTFRTS HHLKVHLRIH TGEKPYRCPH CDYAGTQSAS LKYHLERHHR ERQNGGGSSY
     GHAAEHKEEH AASKSGVFVR PEVLRGVFKG VPGSMDFRGG QMLPHQWAAP GMQDRDRHGH
     GHGASTENPP DHTKSQETPS AEGPASFSDL SRAYQSMVGN GMNFQGSLQA FMDSFVLSSL
     KKDKEMRDKA QIQPHLGADG MEARAKRGEA AEERSDTKPT GSKPEKSQYE PLDLSVRPDS
     VSLPGSAVTI QDNVAWHGCL FCPFQTSSVE LMALHLQANH LGKAKRKEGG FLDAKAGEAS
     SMGKAGLMSA VLHPGYEAVS AKPEPHMDKL VQQELGKEIK GEPRGPAWSN HMESAGFQND
     FFKPFGMYDA APGGLVPQGF GGSGPEQQDP LKQPSDVKNS KPSAMAELSE GHPYSDSEPT
     KEREHPRSDD EFCPADRATR PGSDDDEDEA EEEDEDGEEE EMEEGEENRS MQLPVLSEDP
     QKAGAARATL SPLLEKPWRG LSLLSSAGVP QGSPRAEQGR LEQQMSILSV LRAYSAENLA
     AFNGLGSTSN NTGAIKRPDM PAVVHPWVRE EEAPPPPGLP ATPTPTQECH LVDTEMQEDP
     LTD
//
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