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Database: UniProt
Entry: A0A6P6KFM5_CARAU
LinkDB: A0A6P6KFM5_CARAU
Original site: A0A6P6KFM5_CARAU 
ID   A0A6P6KFM5_CARAU        Unreviewed;       615 AA.
AC   A0A6P6KFM5;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JAN-2026, entry version 22.
DE   RecName: Full=Zinc finger protein 750 {ECO:0000256|ARBA:ARBA00040216};
GN   Name=znf750 {ECO:0000313|RefSeq:XP_026071083.1};
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957 {ECO:0000313|Proteomes:UP000515129, ECO:0000313|RefSeq:XP_026071083.1};
RN   [1] {ECO:0000313|RefSeq:XP_026071083.1}
RP   IDENTIFICATION.
RC   STRAIN=Wakin {ECO:0000313|RefSeq:XP_026071083.1};
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_026071083.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_026071083.1; XM_026215298.1.
DR   AlphaFoldDB; A0A6P6KFM5; -.
DR   GeneID; 113051498; -.
DR   KEGG; caua:113051498; -.
DR   CTD; 79755; -.
DR   OrthoDB; 8933073at2759; -.
DR   Proteomes; UP000515129; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:TreeGrafter.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IEA:TreeGrafter.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0008544; P:epidermis development; IEA:TreeGrafter.
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:UP000515129};
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          5..58
FT                   /note="Zinc finger protein 750-like zinc finger"
FT                   /evidence="ECO:0000259|Pfam:PF15269"
FT   REGION          63..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..436
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..559
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..600
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  69423 MW;  2ED50F50043E9EB0 CRC64;
     MDTLQGRKPK KPHYIPRPPG KPFKYQCFQC PFTCNIKSHL FNHMKYNLCK NSISMVSQRI
     EQTGKTQRPS QHNFPFNQKG KEPPLEAEVR KSIERVNEKV EQEKMGKGTR ESPIKEVTKD
     VTEQICETRD KKGDIDIEQN KISSAFSPVA RTCESEALAQ SPHKDDQSST SAIPQFYHQM
     APWAPPASTA PLLPLIPEYP SYMVSERPLH SLYTSYSHNQ ANTPAYQLIP RETQRPLVPS
     PLVPPSTSLL HPYHYRYAHS IIPGPPLPYS LYQHPEFSMS LQRTRYLPLD VYSNRFYPRE
     YGGHLVPLPH PESYSRLSED RAFQEHKTVD KGTRQSPLEG CAASGSPDRP STADVTQRIP
     VTLRHASHGE SFPVSQSQHV EPVATTVTEN LPKKSFGQTQ ESMLQNKERN EPQTTASARS
     SDISSEKEDE DTEEEPAPLN LSKRDQAVSN SNMTHHYPDC KLHYDSESSE EEAPLNLCLR
     VQSNNLALLD TTGSETPERQ TIINAEVCTI APPKEQEIDP CDQRHSAAFA LCQLASSKDI
     FNDSSFGQQE TTEGQSSQSL PPPDKSPAKD TPDTPRQSTR AMGQKRVNNR PLRHTTKRAK
     VKEPARTQRK RSQNC
//
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