NFX1_BOVIN
ID NFX1_BOVIN Reviewed; 1116 AA.
AC A6QLA0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Transcriptional repressor NF-X1;
DE EC=2.3.2.-;
DE AltName: Full=Nuclear transcription factor, X box-binding protein 1;
GN Name=NFX1;
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=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to the X-box motif of MHC class II genes and represses
CC their expression. May play an important role in regulating the duration
CC of an inflammatory response by limiting the period in which MHC class
CC II molecules are induced by interferon-gamma. Together with PABPC1 or
CC PABPC4, acts as a coactivator for TERT expression. Mediates E2-
CC dependent ubiquitination (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PABPC1 and PABPC4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
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DR EMBL; BC147890; AAI47891.1; -; mRNA.
DR RefSeq; NP_001095499.1; NM_001102029.2.
DR AlphaFoldDB; A6QLA0; -.
DR SMR; A6QLA0; -.
DR STRING; 9913.ENSBTAP00000042616; -.
DR PaxDb; A6QLA0; -.
DR PRIDE; A6QLA0; -.
DR Ensembl; ENSBTAT00000045206; ENSBTAP00000042616; ENSBTAG00000012385.
DR GeneID; 515680; -.
DR KEGG; bta:515680; -.
DR CTD; 4799; -.
DR VEuPathDB; HostDB:ENSBTAG00000012385; -.
DR VGNC; VGNC:32053; NFX1.
DR eggNOG; KOG1952; Eukaryota.
DR GeneTree; ENSGT00940000156325; -.
DR HOGENOM; CLU_005714_1_2_1; -.
DR InParanoid; A6QLA0; -.
DR OMA; WCEKEVD; -.
DR OrthoDB; 299100at2759; -.
DR TreeFam; TF105889; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000012385; Expressed in conceptus and 109 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd02643; R3H_NF-X1; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034076; R3H_NF-X1.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12360; PTHR12360; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 8.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00438; ZnF_NFX; 9.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1116
FT /note="Transcriptional repressor NF-X1"
FT /id="PRO_0000334613"
FT DOMAIN 991..1059
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 355..406
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 450..468
FT /note="NF-X1-type 1"
FT ZN_FING 503..522
FT /note="NF-X1-type 2"
FT ZN_FING 564..583
FT /note="NF-X1-type 3"
FT ZN_FING 629..652
FT /note="NF-X1-type 4"
FT ZN_FING 691..710
FT /note="NF-X1-type 5"
FT ZN_FING 718..737
FT /note="NF-X1-type 6"
FT ZN_FING 829..851
FT /note="NF-X1-type 7"
FT ZN_FING 860..881
FT /note="NF-X1-type 8"
FT REGION 9..26
FT /note="Interaction with PABPC1 and PABC4"
FT /evidence="ECO:0000250"
FT REGION 38..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12986"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AY10"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12986"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AY10"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12986"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12986"
SQ SEQUENCE 1116 AA; 123581 MW; C79B5AE6CC4CA649 CRC64;
MAEAPPVSGA FKFNTDAAEF IPQERKNSGL YCGSQRRLDS NRIGRRNYSS PPPCHLSRQI
SYDDISAVHQ HSFYPSGSKP KSQQTSFQSS VTNKSLKNHG LQNQPWQKLR SEKQHIRVKR
AQGLIDQTSD APGLENVAKS ESGTNLREHS PSESEKEIVG ADPRGAKPKK ATQFIYSYGR
GPKVKGKLKS EWGHRMTPKP EEAGPENTKP AGVIHPDSSD ASSRKVVADG ARRGEQRRHP
QKRSPWEVEG ARPRPGRNPP KQEGQRHTNA GSRDNMASIP KDDLNERPAK STCDSGNLAV
VSRSSRRADP EKCAVRRQDP QVASFPRGKQ NHMLKNVETH TGSLIEQLTT EKYECMVCCE
LVRVTAPVWS CQSCYHVFHL NCIKKWARSP ASQADGQSGW RCPACQNVSA HVPNTYTCFC
GKVKNPEWSR NEIPHSCGEV CRRKQPGQDC PHSCNLLCHP GPCPPCPAFM TKTCECGRTR
HTVRCGQAVS VHCSNPCDNI LNCGQHHCAE LCHGGPCQPC RVILNQVCYC GSTSRDVLCG
TDIGKSDGFG DFGCLKICGK DLKCGNHTCS QVCHPQPCQP CPRLPQLVRY CPCGQTPLSQ
LLELGSSGRK TCMDPVPSCG KVCGKPLPCG SLDFIHTCEK LCHEGDCGPC SRTSVISCRC
SFRTKELPCT SLKSEDATFM CDKRCNKKRL CGRHKCNEIC CVDKEHKCPL ICGRKLRCGL
HRCEEPCHRG NCQTCWQASF DELTCHCGAS VIYPPVPCGT RPPECTQTCA RVHECDHPVY
HSCHSEDKCP PCTFLTQKWC MGKHELRSNI PCHLVDISCG LPCGATLPCG MHKCQRLCHK
GECLGDEICK QPCTTSRANC GHPCMAPCHL SLPCPVTTCK AKIELQCECG RRKEIMVCSE
ASSTYQRIAA ISMASKITDM QLGDSVEISK LITKKEIHQA RLECDEECSA LERKKRLAEA
FHISDDSDPF NVRSSGSKFS DSLKEDARKD LRFVSDIEKE MEALVEAVNK GKSSKKSHCF
PPMNRDHRRI IHDLAQVYGL ESVSYDSEPK RNVVVTAVRG KSICPSTTLT GVLEKENQSR
PPPPIAHHRQ TDKNPGSSNL QKIAKEPVID YFDVQD
