DCA10_MOUSE
ID DCA10_MOUSE Reviewed; 566 AA.
AC A2AKB9; A2AKV8; Q3TNI7; Q5U4G6; Q8BHQ2; Q8BHS1; Q8BHX4; Q8K3A5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DDB1- and CUL4-associated factor 10;
DE AltName: Full=WD repeat-containing protein 32;
GN Name=Dcaf10; Synonyms=Wdr32;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 112-566 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57; SER-96 AND
RP SER-100, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-141, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DDB1. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2AKB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AKB9-2; Sequence=VSP_028516;
CC Name=3;
CC IsoId=A2AKB9-3; Sequence=VSP_028514;
CC Name=4;
CC IsoId=A2AKB9-4; Sequence=VSP_028515;
CC -!- SIMILARITY: Belongs to the WD repeat DCAF10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27317.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH85101.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM20443.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK045241; BAC32276.1; -; mRNA.
DR EMBL; AK076417; BAC36330.1; -; mRNA.
DR EMBL; AK083428; BAC38912.1; ALT_INIT; mRNA.
DR EMBL; AK165246; BAE38101.1; -; mRNA.
DR EMBL; AL772376; CAM20447.1; -; Genomic_DNA.
DR EMBL; AL772285; CAM20447.1; JOINED; Genomic_DNA.
DR EMBL; AL772285; CAM26867.1; -; Genomic_DNA.
DR EMBL; AL772376; CAM26867.1; JOINED; Genomic_DNA.
DR EMBL; AL772376; CAM20443.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC027317; AAH27317.1; ALT_INIT; mRNA.
DR EMBL; BC085101; AAH85101.1; ALT_INIT; mRNA.
DR CCDS; CCDS38754.1; -. [A2AKB9-1]
DR RefSeq; NP_694807.2; NM_153167.2. [A2AKB9-1]
DR AlphaFoldDB; A2AKB9; -.
DR SMR; A2AKB9; -.
DR BioGRID; 232403; 1.
DR STRING; 10090.ENSMUSP00000117082; -.
DR iPTMnet; A2AKB9; -.
DR PhosphoSitePlus; A2AKB9; -.
DR EPD; A2AKB9; -.
DR MaxQB; A2AKB9; -.
DR PaxDb; A2AKB9; -.
DR PeptideAtlas; A2AKB9; -.
DR PRIDE; A2AKB9; -.
DR ProteomicsDB; 277954; -. [A2AKB9-1]
DR ProteomicsDB; 277955; -. [A2AKB9-2]
DR ProteomicsDB; 277956; -. [A2AKB9-3]
DR ProteomicsDB; 277957; -. [A2AKB9-4]
DR Antibodypedia; 12056; 97 antibodies from 20 providers.
DR Ensembl; ENSMUST00000155551; ENSMUSP00000117082; ENSMUSG00000035572. [A2AKB9-1]
DR GeneID; 242418; -.
DR KEGG; mmu:242418; -.
DR UCSC; uc008ssm.1; mouse. [A2AKB9-4]
DR UCSC; uc008ssn.1; mouse. [A2AKB9-1]
DR CTD; 79269; -.
DR MGI; MGI:2140179; Dcaf10.
DR VEuPathDB; HostDB:ENSMUSG00000035572; -.
DR eggNOG; KOG0266; Eukaryota.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00390000012666; -.
DR HOGENOM; CLU_028919_2_0_1; -.
DR InParanoid; A2AKB9; -.
DR OMA; EFQEGTP; -.
DR OrthoDB; 1068414at2759; -.
DR PhylomeDB; A2AKB9; -.
DR TreeFam; TF323434; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 242418; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Dcaf10; mouse.
DR PRO; PR:A2AKB9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AKB9; protein.
DR Bgee; ENSMUSG00000035572; Expressed in humerus cartilage element and 220 other tissues.
DR ExpressionAtlas; A2AKB9; baseline and differential.
DR Genevisible; A2AKB9; MM.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR039085; DCA10.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR14588; PTHR14588; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methylation; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..566
FT /note="DDB1- and CUL4-associated factor 10"
FT /id="PRO_0000306834"
FT REPEAT 173..212
FT /note="WD 1"
FT REPEAT 216..254
FT /note="WD 2"
FT REPEAT 258..297
FT /note="WD 3"
FT REPEAT 303..342
FT /note="WD 4"
FT REPEAT 415..455
FT /note="WD 5"
FT REPEAT 477..515
FT /note="WD 6"
FT REPEAT 533..566
FT /note="WD 7"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QP82"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QP82"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QP82"
FT VAR_SEQ 1..308
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028514"
FT VAR_SEQ 226..566
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028515"
FT VAR_SEQ 359..395
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028516"
FT CONFLICT 202
FT /note="F -> L (in Ref. 1; BAE38101)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="C -> S (in Ref. 3; AAH27317)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="S -> P (in Ref. 1; BAC38912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 61558 MW; 4923778CDA90E6F8 CRC64;
MFPFGPHSPG GDETAGAEEP PPLGGPAAAS RPPSPAPRPA SPQRGADAAS PPPVAGSPRL
PGGPAVSPAE RAGEFAAPGA LELSAATASA SQAKLSPSSS PRRRSRPDWR AGGRSRQGLG
AGLGGPGARL FGWLRERSLG RGLFVDPARD NFRTMTNLYG SIHPADSVYL STRTHGAVFN
LEYSPDGSVL TVACEQTEVL LFDPISSKHI KTLSEAHEDC VNNIRFLDNR LFATCSDDTT
IALWDLRKLN TKVCTLHGHT SWVKNIEYDT NTRLLVTSGF DGNVIIWDTN RCTEDGCPHK
KFFHTRFLMR MRLTPDCSKM LISTSSGYLL ILHELDLTKS LEVGSYPILR ARRTTSSSDL
TTTSSSSGSR VSGSPCHHND SNSTEKHMSR ASQREGVSPR NSLEVLTPEV PGERDRGNCI
TSLQLHPKGW ATLLRCSSNT DDQEWTCVYE FQEGAPVRPV SPRCSLRLTH YIEEANVGRG
YIKELCFSPD GRMISSPHGY GIRLLGFDKQ CSELVDCLPK EASPLRVIRS LYSHNDVVLT
TKFSPTHCQI ASGCLSGRVS LYQPKF
