DCAF6_PONAB
ID DCAF6_PONAB Reviewed; 860 AA.
AC Q5R9B8; Q5R659; Q5RC66;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=DDB1- and CUL4-associated factor 6;
DE AltName: Full=IQ motif and WD repeat-containing protein 1;
DE AltName: Full=Nuclear receptor interaction protein;
DE Short=NRIP;
GN Name=DCAF6; Synonyms=IQWD1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ligand-dependent coactivator of nuclear receptors. Enhance
CC transcriptional activity of the nuclear receptors NR3C1 and AR. May
CC function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein
CC ligase complex (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the nuclear receptors NR3C1 and AR in the
CC presence of ligand. Interacts with DDB1, CUL4A and CUL4B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R9B8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R9B8-2; Sequence=VSP_028022, VSP_028023;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH92757.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858414; CAH90642.1; -; mRNA.
DR EMBL; CR859471; CAH91642.1; -; mRNA.
DR EMBL; CR860637; CAH92757.1; ALT_INIT; mRNA.
DR RefSeq; NP_001125965.1; NM_001132493.1.
DR RefSeq; NP_001128877.1; NM_001135405.1.
DR AlphaFoldDB; Q5R9B8; -.
DR SMR; Q5R9B8; -.
DR STRING; 9601.ENSPPYP00000000636; -.
DR GeneID; 100172900; -.
DR KEGG; pon:100172900; -.
DR CTD; 55827; -.
DR eggNOG; KOG1334; Eukaryota.
DR InParanoid; Q5R9B8; -.
DR OrthoDB; 1270484at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR045151; DCAF8.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15574; PTHR15574; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..860
FT /note="DDB1- and CUL4-associated factor 6"
FT /id="PRO_0000304403"
FT REPEAT 49..88
FT /note="WD 1"
FT REPEAT 92..133
FT /note="WD 2"
FT REPEAT 139..179
FT /note="WD 3"
FT REPEAT 189..229
FT /note="WD 4"
FT REPEAT 251..290
FT /note="WD 5"
FT DOMAIN 676..705
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REPEAT 718..756
FT /note="WD 6"
FT REPEAT 759..798
FT /note="WD 7"
FT REGION 288..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q58WW2"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q58WW2"
FT MOD_RES 654
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q58WW2"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q58WW2"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC22"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC22"
FT VAR_SEQ 460..469
FT /note="DNNNEKLSPK -> VRLFLRLYIK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028022"
FT VAR_SEQ 470..860
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028023"
FT CONFLICT 125
FT /note="V -> I (in Ref. 1; CAH90642)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="T -> I (in Ref. 1; CAH92757)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="E -> A (in Ref. 1; CAH92757)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="P -> Q (in Ref. 1; CAH91642)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="S -> P (in Ref. 1; CAH91642)"
FT /evidence="ECO:0000305"
FT CONFLICT 499..500
FT /note="RS -> WG (in Ref. 1; CAH92757)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="T -> I (in Ref. 1; CAH92757)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="E -> G (in Ref. 1; CAH92757)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="G -> E (in Ref. 1; CAH92757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 860 AA; 96138 MW; 30446705E0391E2E CRC64;
MSRGGSCPHL LWDVRKRSLG LEDPSRLRSR YLGRREFIQR LKLEATLNVH DGCVNTICWN
DTGEYILSGS DDTKLVISNP YSRKVLTTIR SGHRANIFSA KFLPCTNDKQ IVSCSGDGVI
FYTNVEQDAE TNRQCQFTCH YGTTYEIMTV PNDPYTFLSC GEDGTVRWFD TRIKTSCTKE
DCKDDILINC RRAATSVAIC PPIPYYLAVG CSDSSVRIYD RRMLGTRATG NYAGRGTTGM
VARFIPSHLN NKSCRVTSLC YSEDGQEILV SYSSDYIYLF DPKDDTAREL KTPSAEERRE
ELRQPPVKRL RLRGDWSDTG PRARPESERE RDGEQSPNVS LMQRMSDMLS RWFEEASEVA
QSNRGRGRSR PRGGTSQSDI STLPTVPSSP DLEVSETAME VDTPAEQFLQ PSTSSTMSAQ
AHSTSSPTES PHSTPLLSSP DSEQRQSVEA SGHHTHHQSD NNNEKLSPKP GTGEPVLSLH
YSTEGTTTST IKLNFTDERS SIASSSRGIG SHCKSEGQEE SLVPQSSMQP PEGDSETKAP
EESSEDVTKY QEGVSAENPV ENHTNITQSD KFTAKPLDSN SGERNDLNLD SSCGVPEESA
SPEKAKEPET SDHTSTESAT NENNTNPEPQ FQTEATGPSA HEETSTRDSA LQDTDDSDDD
PVLIPGARYR AGPGDRRSAV ARIQEFFRRR KERKEMEELD TLNIRRPLVK MVYKGHRNSR
TMIKEANFWG ANFVMSGSDC GHIFIWDRHT AEHLMLLEAD NHVVNCLQPH PFDPILASSG
IDYDIKIWSP LEESRIFNRK LADEVITRNE LMLEETRNTI TVPASFMLRM LASLNHIRAD
RLEGDRSEGS GQENENEDEE