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DCAF1_CAEEL
ID   DCAF1_CAEEL             Reviewed;        1701 AA.
AC   Q21106; Q23436;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 5.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=DDB1- and CUL4-associated factor homolog 1;
GN   Name=dcaf-1; ORFNames=ZK1251.9;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Component of the cul4-rbx1-ddb1-dcaf1 E3 ubiquitin-protein
CC       ligase complex, dcaf1 may function as the substrate recognition module
CC       within this complex. {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the cul4-rbx1-ddb1-dcaf1 E3 ubiquitin-protein
CC       ligase complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The DWD boxes are required for interaction with ddb1.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPRBP/DCAF1 family. {ECO:0000305}.
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DR   EMBL; Z68222; CAA92505.3; -; Genomic_DNA.
DR   EMBL; Z68218; CAA92505.3; JOINED; Genomic_DNA.
DR   PIR; B88789; B88789.
DR   PIR; T23210; T23210.
DR   RefSeq; NP_501725.2; NM_069324.5.
DR   AlphaFoldDB; Q21106; -.
DR   SMR; Q21106; -.
DR   BioGRID; 42908; 2.
DR   STRING; 6239.ZK1251.9; -.
DR   EPD; Q21106; -.
DR   PaxDb; Q21106; -.
DR   PeptideAtlas; Q21106; -.
DR   EnsemblMetazoa; ZK1251.9a.1; ZK1251.9a.1; WBGene00014243.
DR   GeneID; 177804; -.
DR   KEGG; cel:CELE_ZK1251.9; -.
DR   UCSC; ZK1251.9; c. elegans.
DR   CTD; 177804; -.
DR   WormBase; ZK1251.9a; CE33014; WBGene00014243; dcaf-1.
DR   eggNOG; KOG1832; Eukaryota.
DR   GeneTree; ENSGT00390000005874; -.
DR   HOGENOM; CLU_001785_1_0_1; -.
DR   InParanoid; Q21106; -.
DR   OMA; ECSQDQA; -.
DR   OrthoDB; 105679at2759; -.
DR   PhylomeDB; Q21106; -.
DR   Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q21106; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00014243; Expressed in adult organism and 4 other tissues.
DR   ExpressionAtlas; Q21106; baseline and differential.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR033270; VPRBP/DCAF1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13129; PTHR13129; 1.
DR   SMART; SM00667; LisH; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..1701
FT                   /note="DDB1- and CUL4-associated factor homolog 1"
FT                   /id="PRO_0000287475"
FT   DOMAIN          851..883
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REPEAT          1086..1125
FT                   /note="WD 1"
FT   REPEAT          1128..1169
FT                   /note="WD 2"
FT   REPEAT          1171..1210
FT                   /note="WD 3"
FT   REPEAT          1215..1252
FT                   /note="WD 4"
FT   REGION          224..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          883..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1384..1559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1566..1585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1641..1701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1237..1245
FT                   /note="DWD box 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1275..1282
FT                   /note="DWD box 2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        224..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1390..1425
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1490..1539
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1643..1657
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1701 AA;  192897 MW;  DF1345ADB9CA9411 CRC64;
     MTSKEIYPLR STGTMMMISD QDLKLSTQLM LRIAELLLEF DANHEQSSFD PIPILKRISE
     LLEQATDIFI KNDPDPLDDR HPHRTHPDSA LGNILKIIFK NDDFMTKLVV SYILARDNVE
     LNIQGSRLLL ACIPGLDSKV VFSEPDDFIP RLYTWAGSEG TNETLQGYAM GLLAAALENT
     ENASKYRNEN ALLVPFGLRR LHELQGRSLE EQKKIGQTDF SQLHAEQSTS NGTSIPSIKI
     TSVDGSTKEN EKTFVQSTDP PPPKKRRTEP CLTSLLRTEI TQRVPSFHNL RNLDDSNSKW
     DILQPFLIGD QQVYPLSLAT YQRFILQYLA ACGEYQDLLL QTFEGNALEI LFDYIDLEKS
     KDVRLTFDAL KYLTSLLVHR KFALEFVNKG GIPALLKVPK TSLASVGVVT CLYYIAYSND
     VMEILCQMSD EIVDETVQYV LWCLEHSHES GMASACMFFS QGLFYKAILR RFDQYDGPRK
     LHNYIATLTL MQNNEDVELT EEQIHTSTQC TRGVCTTFRS YLTAHIFIKV ENYKKLYGNN
     LPTGMRFPEL VQGDCPDYKS MKPYEEVCWQ CEAIVTEMLR FTGSSFREAE NLRKLGMVRM
     FLAVRVLSRD WENISPSLRT EMCVHALETL CMMFCLPSIQ TELITQHSYN HSNYDGFTIL
     LQTSLGRYDE DPSLRMAALG CIQRCVYVEP ECWKAIIQRV KSSEEKSSSA SKRQSKYEII
     MNHLERMWTE VRKTDGIMAL VNLINCKIPL TEADSIRKTA TNTLTGLARH PEVRQILAKL
     PLIAHNGLQN LMREPVCSDK RDIHAAFCKE AVQLLQVIYG RKIHDQQGKE IQSSEKSHRQ
     WVIENTQVSF NQAELLQLIH DHLLKSKLDS VAAMLKSEAK LPDRPASRSI NTPILNKPLP
     SSGNNFSKIN DTYPTLAPRT LESEIGGISA RRPSNAASLS SPAMATRSHS TDDDVFATPT
     LPRRYTTSGA FPKKLMISPA RQKLRPLTPG ESSSGYRPIK DLNSIVTDYF RNQHSTCKNP
     VTTCPPFSLF YQHKCPELSY QTNVVRNISL RTLDQELLRP HERVYSQWTN ERTIFSRFRN
     WKTIHDHDES YTKATFSVDD EHLIVGLFNG EVHWINVDTG LDEGHTNCHG SALTNIEPSK
     DGSMMLTSSA FSRPLSALWR LGEALQRVHT YREDSCVKFA NTTMQRIVGT CRDKATVYDT
     ETNHVLDTYL SGIDGLQYEK NYASFSPDDK LIFNDGLLWD VRKKNSAIHV FDRLSKITLF
     GTFHPHGTQI VINSEVYDIR TFRMLHHVPE LNRCQVSFNS TGNIMYATEV TDVHCPDYDE
     KIFSSFRTFE TRDYSALTTF EGRRPVIDLC ASHQDQKMCV IEKVRPQMSD YMIQASTQLK
     IVEIGRLKDN EDENDEEEDE QREDHDEDED SDESGDGDDD EEIGGNSSDR ESVFRTLGRL
     GDESDSGSSV DDNDTLDDLD FENAQNRIIR RQAQRRRQRL NSSENDAELP GSDEGSDEDG
     DDDEDGEGDP DFDMGAAIDD LVDAVDEEVD EDELGTDGDD DDSGSWRTTN SIDSEDINLD
     DLDEEEARVV ENEGNNERPA RPVDPIEAAA AARRAILGRG LRDLRMGIRG GNRRRNGGGL
     EQAEMLNARA EEQRVSFMEA LVRGAEAERR EEEGGDDGES SSSSSSDTDE YQSEEEEINS
     VSTTALNPAL RRRNRRPDDE A
 
 
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