DCA15_MOUSE
ID DCA15_MOUSE Reviewed; 600 AA.
AC Q6PFH3; Q3U305; Q8BMB2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DDB1- and CUL4-associated factor 15 {ECO:0000305};
GN Name=Dcaf15 {ECO:0000312|MGI:MGI:2684420};
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 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Wolffian duct;
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Substrate-recognition component of the DCX(DCAF15) complex, a
CC cullin-4-RING E3 ubiquitin-protein ligase complex that mediates
CC ubiquitination and degradation of target proteins. The DCX(DCAF15)
CC complex acts as a regulator of the natural killer (NK) cells effector
CC functions, possibly by mediating ubiquitination and degradation of
CC cohesin subunits SMC1A and SMC3. May play a role in the activation of
CC antigen-presenting cells (APC) and their interaction with NK cells.
CC {ECO:0000250|UniProtKB:Q66K64}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q66K64}.
CC -!- SUBUNIT: Component of the DCX(DCAF15) complex, also named CLR4(DCAF15)
CC complex, composed of DCAF15, DDB1, cullin-4 (CUL4A or CUL4B), DDA1 and
CC RBX1. {ECO:0000250|UniProtKB:Q66K64}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PFH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PFH3-2; Sequence=VSP_030290;
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DR EMBL; BC057552; AAH57552.1; -; mRNA.
DR EMBL; AK032982; BAC28110.1; -; mRNA.
DR EMBL; AK153305; BAE31886.1; -; mRNA.
DR EMBL; AK155000; BAE32985.1; -; mRNA.
DR CCDS; CCDS40406.1; -. [Q6PFH3-2]
DR CCDS; CCDS90424.1; -. [Q6PFH3-1]
DR RefSeq; NP_766090.2; NM_172502.3. [Q6PFH3-2]
DR RefSeq; XP_006530871.1; XM_006530808.1.
DR AlphaFoldDB; Q6PFH3; -.
DR SMR; Q6PFH3; -.
DR BioGRID; 229292; 1.
DR STRING; 10090.ENSMUSP00000038568; -.
DR iPTMnet; Q6PFH3; -.
DR PhosphoSitePlus; Q6PFH3; -.
DR EPD; Q6PFH3; -.
DR MaxQB; Q6PFH3; -.
DR PeptideAtlas; Q6PFH3; -.
DR PRIDE; Q6PFH3; -.
DR ProteomicsDB; 279280; -. [Q6PFH3-1]
DR ProteomicsDB; 279281; -. [Q6PFH3-2]
DR Antibodypedia; 77450; 2 antibodies from 2 providers.
DR Ensembl; ENSMUST00000041367; ENSMUSP00000038568; ENSMUSG00000037103. [Q6PFH3-2]
DR Ensembl; ENSMUST00000210279; ENSMUSP00000147690; ENSMUSG00000037103. [Q6PFH3-1]
DR GeneID; 212123; -.
DR KEGG; mmu:212123; -.
DR UCSC; uc009mlw.1; mouse. [Q6PFH3-2]
DR UCSC; uc009mlx.1; mouse. [Q6PFH3-1]
DR CTD; 90379; -.
DR MGI; MGI:2684420; Dcaf15.
DR VEuPathDB; HostDB:ENSMUSG00000037103; -.
DR eggNOG; ENOG502QQCQ; Eukaryota.
DR GeneTree; ENSGT00390000011987; -.
DR HOGENOM; CLU_031970_0_0_1; -.
DR InParanoid; Q6PFH3; -.
DR OMA; QILYTKG; -.
DR OrthoDB; 471103at2759; -.
DR PhylomeDB; Q6PFH3; -.
DR TreeFam; TF329680; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 212123; 2 hits in 40 CRISPR screens.
DR PRO; PR:Q6PFH3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6PFH3; protein.
DR Bgee; ENSMUSG00000037103; Expressed in ear vesicle and 242 other tissues.
DR ExpressionAtlas; Q6PFH3; baseline and differential.
DR Genevisible; Q6PFH3; MM.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036094; F:small molecule binding; ISO:MGI.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0032814; P:regulation of natural killer cell activation; ISS:UniProtKB.
DR InterPro; IPR038914; DCAF15.
DR InterPro; IPR032734; DCAF15_WD40.
DR PANTHER; PTHR28541; PTHR28541; 1.
DR Pfam; PF14939; DCAF15_WD40; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Immunity; Metal-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..600
FT /note="DDB1- and CUL4-associated factor 15"
FT /id="PRO_0000314486"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT VAR_SEQ 583
FT /note="G -> GRKCPSWAGHLILPWIPGMLDVRSVLGSEWHPAMAGEAG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030290"
FT CONFLICT 203
FT /note="H -> N (in Ref. 1; BAC28110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 66643 MW; EB45516DD355C7A8 CRC64;
MAPSSKSERN SGAGSAGGGP GGTGGKRAVG RRREHVLKQL ERVKISGQLS PRLFRKLPPR
VCVSLKNIVD EDFLYAGHIF LGFSKCGRYV LSYTSSSGDD DFSFYIYHLY WWEFNVHSKL
KLVRQVRLFQ DEEIYSDLYL TVCEWPSDAS KVIVFGFNTR SANGMLMNMM MMSDENHRDI
YISTVAVPPR GRCAACQDAS RAHPGDPSAQ CLRHGFMLHT KYQVVYPFPT FQPAFQLKKD
QVVLLNTSYS LVACAVSVHS AGDSSFCQIL YDHTALPPAP PSSPGPWSPE AAPAFPSLGV
EVVPAQPSGA PEPSPAIAKA KEFVADIFRR AKEAKGSPLE ETRLPSSLGP SSSRCRPSLE
PQAPSGEVVP RDSPPAAETT APEPGYINYT KLHYVLQSGE GTEPEDEFED DKISLPFVVT
DLRGRNLRPM RERTDMQGQY LTVEQLTLDF EYVINEVIRH DATWGHQFCS FSDYDIVILE
VCPETNQVLI NIGLLLLAFP APTEEGQLRP KTYHTSLKVA WDLNTGIFET VSVGDLTEVK
GQTSGSVWSS YRKSCVDMVM KWLVPESSGR YVNRMTNEAL HKGCSLKVLA DSERYTWIVL
