DCST1_MOUSE
ID DCST1_MOUSE Reviewed; 732 AA.
AC Q059Y8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=E3 ubiquitin-protein ligase DCST1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q5T197};
DE AltName: Full=DC-STAMP domain-containing protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000305};
GN Name=Dcst1;
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].
RC 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: E3 ubiquitin-protein ligase which mediates 'Lys-48'-linked
CC ubiquitination of STAT2 and induces its proteosomal degradation thereby
CC negatively regulating type-I-interferon signaling.
CC {ECO:0000250|UniProtKB:Q5T197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q5T197};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q5T197}.
CC -!- SUBUNIT: Interacts with STAT2; the interaction results in STAT2 'Lys-
CC 48'-linked ubiquitination leading to its proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q5T197}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T197};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q5T197}.
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DR EMBL; BC125478; AAI25479.1; -; mRNA.
DR EMBL; BC125480; AAI25481.1; -; mRNA.
DR CCDS; CCDS38490.1; -.
DR RefSeq; NP_084250.1; NM_029974.2.
DR AlphaFoldDB; Q059Y8; -.
DR BioGRID; 218909; 3.
DR STRING; 10090.ENSMUSP00000065502; -.
DR GlyGen; Q059Y8; 5 sites.
DR iPTMnet; Q059Y8; -.
DR PhosphoSitePlus; Q059Y8; -.
DR PaxDb; Q059Y8; -.
DR PRIDE; Q059Y8; -.
DR ProteomicsDB; 279840; -.
DR Antibodypedia; 20409; 86 antibodies from 20 providers.
DR Ensembl; ENSMUST00000070820; ENSMUSP00000065502; ENSMUSG00000042672.
DR GeneID; 77772; -.
DR KEGG; mmu:77772; -.
DR UCSC; uc008pyy.1; mouse.
DR CTD; 149095; -.
DR MGI; MGI:1925022; Dcst1.
DR VEuPathDB; HostDB:ENSMUSG00000042672; -.
DR eggNOG; KOG3726; Eukaryota.
DR GeneTree; ENSGT00940000153269; -.
DR HOGENOM; CLU_015030_1_1_1; -.
DR InParanoid; Q059Y8; -.
DR OMA; MAKPFTN; -.
DR OrthoDB; 572860at2759; -.
DR PhylomeDB; Q059Y8; -.
DR TreeFam; TF318254; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 77772; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Dcst1; mouse.
DR PRO; PR:Q059Y8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q059Y8; protein.
DR Bgee; ENSMUSG00000042672; Expressed in spermatid and 45 other tissues.
DR Genevisible; Q059Y8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR InterPro; IPR012858; DC_STAMP-like.
DR Pfam; PF07782; DC_STAMP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Immunity; Innate immunity; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..732
FT /note="E3 ubiquitin-protein ligase DCST1"
FT /id="PRO_0000278825"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 672..711
FT /note="RING-type; degenerate"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 732 AA; 84332 MW; 22AB2CD98AC17CD9 CRC64;
MAFLSSTLHS LGIFEKISRI KEVLKNRLLD LTKRRDQARE QQRKRPHTII QGLLLWSLPV
SWIRFLWRQP GEFPVTAFLL GAGTGGLLAI GLFQLLVNPM NIYEEQKVVA LYCLASLGAI
GWGTSPHIRC ASLLLVPKML GKEGRLFVMG YALAAIYSGP AANLRSNINE VIASLGCTVE
LQINNTRSAW RVSTAPLRAV FKGMVGSKDS LNKEIQNVST SFEEMDEQVK SDAGYSSEDW
DKNRESTEMF GTSRVRPYLS TQMVYELRTR LRCIHVVNKA ILSCYRWFDK KHKNCMRRIH
LPLFNNMICV PMKFKFLCNI AKVIEIWCYK RIPVEGNFGQ TYDSVNQSIH GLSGEFSANI
NLKEEKQSSM VGLNTTNWEH MGTEVRDYVR QQETYLQWAM GLLHVLLSCT FLLVFHSAFS
YMDHYNWDIR FDNIYISTYF CQIDARRKKL GKQSLLPLRK AERKTVIFPF KATIQAWEMR
YVIRELLETL PIVLLLLVLC AIDWALYSVF DTIRQHSFVQ YSFRSSHKLE IKVEGDSILA
KLLRKTIGAL NTSSSTDVET NNMPCLPQPI SLNARDYFKA SLPTLLLVCL CLAQAFGYRL
RRVIAAFYFP KREKKRALFF YNEFLKKRSA FTKLRRAAIV RRANQQKAPP HYLVEALYRR
CPLLHRFMRQ RCVVCQAMET PDSYVCPTPD CKALYCRSCW DDMQRLCPVC TPREELSSSA
HSDSNDDAVY GD
