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Database: UniProt
Entry: A0A5N4D1V6_CAMDR
LinkDB: A0A5N4D1V6_CAMDR
Original site: A0A5N4D1V6_CAMDR 
ID   A0A5N4D1V6_CAMDR        Unreviewed;       684 AA.
AC   A0A5N4D1V6;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   08-OCT-2025, entry version 15.
DE   RecName: Full=Zinc finger protein 750 {ECO:0000256|ARBA:ARBA00040216};
GN   ORFNames=Cadr_000020001 {ECO:0000313|EMBL:KAB1265111.1};
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1265111.1, ECO:0000313|Proteomes:UP000299084};
RN   [1] {ECO:0000313|EMBL:KAB1265111.1, ECO:0000313|Proteomes:UP000299084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Drom800 {ECO:0000313|EMBL:KAB1265111.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:KAB1265111.1};
RX   PubMed=30972949; DOI=.1111/1755-0998.13020;
RA   Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A.,
RA   Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D.,
RA   Burger P.A.;
RT   "Improving Illumina assemblies with Hi-C and long reads: an example with
RT   the North African dromedary.";
RL   Mol. Ecol. Resour. 19:1015-1026(2019).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAB1265111.1}.
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DR   EMBL; JWIN03000016; KAB1265111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N4D1V6; -.
DR   STRING; 9838.ENSCDRP00005012943; -.
DR   OrthoDB; 8933073at2759; -.
DR   Proteomes; UP000299084; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR   GO; GO:0044091; P:membrane biogenesis; IEA:Ensembl.
DR   GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   InterPro; IPR039363; ZNF750.
DR   InterPro; IPR039064; ZNF750_Znf.
DR   PANTHER; PTHR14678; PROLINE-RICH PROTEIN 35-RELATED; 1.
DR   PANTHER; PTHR14678:SF1; ZINC FINGER PROTEIN 750; 1.
DR   Pfam; PF15269; zf-C2H2_7; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000299084};
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}.
FT   DOMAIN          6..57
FT                   /note="Zinc finger protein 750-like zinc finger"
FT                   /evidence="ECO:0000259|Pfam:PF15269"
FT   REGION          60..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..154
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..465
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..577
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  73232 MW;  C13EB272ED73374A CRC64;
     MSLLKERKPK KPHYIPRPPG KPFRYKCFQC PFTCNEKSHL FNHMKYGLCK NSITLVSEQD
     RAPRCPKPRS SDPGPAGQPG PTAMPASSKP GPGALAHLDT KPQHGPPTDD TKENPDLQAR
     GPHRGAGQRP ALHKEAAPPS PTAEATTRTP PSTEGATRPS AFVPIGEHRL KGQELTEAPE
     ALAPPHPAAK AASFHAKSAF HAPGYPWKAG SPFLPPEFPH KIPSTKGFGA TAPYMHPAVP
     EYPPHFYTEH GLATIYSPYL LAGNPAECDS PLLSVYGAQD QRHFLPHPGP LPKHLNPAPS
     TYDHYRVFQQ FHSNLPIPYG FYRPESAFSS YGLRLPPIAG ISRDQSPHLL EEATLVYPTS
     SPSKIHSSSS HRKHTEFEKE SPTHEAKDPS RDGQRDPEGT KMSPRAGSAA TGSPGRPSPT
     NFTQTSQPCT GLCGLPDQPA SSGPGRLQAP EQSPVAFPPE CPHPQAPESR DKSPKSLEAG
     SAEAPAQTGH TSPGLDPTPC SPEDGSRTAP LNLSKKPEVE LTATHTPAYG DFTEPQDVPL
     NLSVKDPCNA LTPRPSFHSP SRGPEPTTAP TARTKPASSG DASPGEAPDT QAVDSEEQKQ
     TAAVALCQLA AYSAGTSRPG EGEPTAQELS HHTPESQEAP CDLRPKGQKR TSPRDAGKSQ
     QGAKRAKPSD TTRVLTLRKR TRVS
//
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