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COT1_BOVIN
ID   COT1_BOVIN              Reviewed;         424 AA.
AC   Q9TTR8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=COUP transcription factor 1;
DE            Short=COUP-TF1;
DE   AltName: Full=COUP transcription factor I;
DE            Short=COUP-TF I;
DE   AltName: Full=Nuclear receptor subfamily 2 group F member 1;
GN   Name=NR2F1; Synonyms=TFCOUP1;
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 [MRNA].
RC   TISSUE=Testis;
RA   Walther N.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Coup (chicken ovalbumin upstream promoter) transcription
CC       factor binds to the ovalbumin promoter and, in conjunction with another
CC       protein (S300-II) stimulates initiation of transcription. Binds to both
CC       direct repeats and palindromes of the 5'-AGGTCA-3' motif. Represses
CC       transcriptional activity of LHCG (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as dimer; homodimer and probable heterodimer with
CC       NR2F6. Interacts with GTF2B; this interaction is direct. Interacts with
CC       COPS2. {ECO:0000250|UniProtKB:P10589}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ249440; CAB55623.1; -; mRNA.
DR   PIR; JH0786; JH0786.
DR   RefSeq; NP_786998.1; NM_175804.2.
DR   AlphaFoldDB; Q9TTR8; -.
DR   SMR; Q9TTR8; -.
DR   BioGRID; 160099; 1.
DR   STRING; 9913.ENSBTAP00000023401; -.
DR   PaxDb; Q9TTR8; -.
DR   PRIDE; Q9TTR8; -.
DR   Ensembl; ENSBTAT00000023401; ENSBTAP00000023401; ENSBTAG00000017599.
DR   GeneID; 327684; -.
DR   KEGG; bta:327684; -.
DR   CTD; 7025; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017599; -.
DR   VGNC; VGNC:32240; NR2F1.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000157876; -.
DR   InParanoid; Q9TTR8; -.
DR   OMA; THLIHAE; -.
DR   OrthoDB; 666130at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000017599; Expressed in pigment epithelium of eye and 103 other tissues.
DR   ExpressionAtlas; Q9TTR8; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Receptor;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..424
FT                   /note="COUP transcription factor 1"
FT                   /id="PRO_0000053601"
FT   DOMAIN          185..411
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        84..159
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         87..107
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         123..147
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  46284 MW;  21B1829462CD5982 CRC64;
     MAMVVSSWRD PQDDVAGGNP GGPNPAAQAA RGGGGGAGEQ QQQQAGSGAP HTPQTPGQPG
     APATPGTAGD KGQGPPGSGQ SQQHIECVVC GDKSSGKHYG QFTCEGCKSF FKRSVRRNLT
     YTCRANRNCP IDQHHRNQCQ YCRLKKCLKV GMRREAVQRG RMPPTQPNPG QYALTNGDPL
     NGHCYLSGYI SLLLRAEPYP TSRYGSQCMQ PNNIMGIENI CELAARLLFS AVEWARNIPF
     FPDLQITDQV SLLRLTWSEL FVLNAAQCSM PLHVAPLLAA AGLHASPMSA DRVVAFMDHI
     RIFQEQVEKL KALHVDSAEY SCLKAIVLFT SDACGLSDAA HIESLQEKSQ CALEEYVRSQ
     YPNQPSRFGK LLLRLPSLRT VSSSVIEQLF FVRLVGKTPI ETLIRDMLLS GSSFNWPYMS
     IQCS
 
 
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