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ZFP69_BOVIN
ID   ZFP69_BOVIN             Reviewed;         524 AA.
AC   A7MBI1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Zinc finger protein 69 homolog {ECO:0000250|UniProtKB:A2A761};
DE   AltName: Full=Zinc finger protein 642;
GN   Name=ZFP69; Synonyms=ZNF642;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative transcription factor that appears to regulate lipid
CC       metabolism. {ECO:0000250|UniProtKB:A2A761}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A2A761}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; BC151573; AAI51574.1; -; mRNA.
DR   RefSeq; NP_001095533.1; NM_001102063.1.
DR   AlphaFoldDB; A7MBI1; -.
DR   SMR; A7MBI1; -.
DR   STRING; 9913.ENSBTAP00000048845; -.
DR   PaxDb; A7MBI1; -.
DR   PRIDE; A7MBI1; -.
DR   Ensembl; ENSBTAT00000052349; ENSBTAP00000048845; ENSBTAG00000039287.
DR   GeneID; 521549; -.
DR   KEGG; bta:521549; -.
DR   CTD; 339559; -.
DR   VEuPathDB; HostDB:ENSBTAG00000039287; -.
DR   VGNC; VGNC:37168; ZFP69.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162278; -.
DR   HOGENOM; CLU_002678_0_9_1; -.
DR   InParanoid; A7MBI1; -.
DR   OMA; QTILTHK; -.
DR   OrthoDB; 1318335at2759; -.
DR   TreeFam; TF337055; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000039287; Expressed in oocyte and 104 other tissues.
DR   ExpressionAtlas; A7MBI1; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   2: Evidence at transcript level;
KW   DNA-binding; Lipid metabolism; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..524
FT                   /note="Zinc finger protein 69 homolog"
FT                   /id="PRO_0000355566"
FT   DOMAIN          1..39
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   DOMAIN          74..146
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         269..291
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         297..319
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         325..347
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         353..375
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         381..403
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         409..431
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         437..459
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         465..487
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         493..515
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          49..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  60808 MW;  1607942ABF596FBA CRC64;
     MLQQLLITLP TEASTWVKLH HPENAKEGAP LWEDVTKMFE GGALLSQDAD ETQGESLKDE
     LTPGTPTTDS QELLTFKDIS VDFTQEEWGQ LAPAHRNLYR EVMLENYGNL VSVAGCQLSK
     PSVISQLEKG EEPWMTEKEG PGDPNSDLKS KTETSASNAK YNILQEQLYH GMMMERFMRD
     DVIYSTLKKV SEYDDELEKH QDRHGRNVRQ TIMTHKKRSQ ETYKFGKNIV SSNVVIEQRL
     RKCDTPRKRN KCKSDVINHP TSYIRVKTYE CNICEKAFKQ PIHLTEHMRI HTGEKPFRCK
     ECGRAFSQSA SLTTHQRIHT GEKPFECEEC GKAFRHRSSL NQHHRTHTGE KPYICDKCQK
     AFSQNISLIQ HLRTHSGEKP FTCNECGKTF RQIRHLSEHI RIHTGEKPYA CTACCKTFSH
     RAYLTHHQRI HTGERPYKCK ECGKAFRQRI HLSNHKTVHT GVKAYECNRC GKAYRHDSSF
     KKHQRHHTGE KPYECNECGK AFSYNSSLTR HHEIHRRNVF QNNI
 
 
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