RN123_MOUSE
ID RN123_MOUSE Reviewed; 1314 AA.
AC Q5XPI3; Q6PGE0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=E3 ubiquitin-protein ligase RNF123;
DE EC=2.3.2.27;
DE AltName: Full=Kip1 ubiquitination-promoting complex protein 1;
DE AltName: Full=RING finger protein 123;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF123 {ECO:0000305};
GN Name=Rnf123; Synonyms=Kpc1;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=15531880; DOI=10.1038/ncb1194;
RA Kamura T., Hara T., Matsumoto M., Ishida N., Okumura F., Hatakeyama S.,
RA Yoshida M., Nakayama K., Nakayama K.;
RT "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1
RT phase.";
RL Nat. Cell Biol. 6:1229-1235(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC 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 [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-683, 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: Catalytic subunit of the KPC complex that acts as E3
CC ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-
CC mediated degradation of CDKN1B which is the cyclin-dependent kinase
CC inhibitor at the G0-G1 transition of the cell cycle. Functions also as
CC an inhibitor of innate antiviral signaling mediated by DDX58 and IFIH1
CC independently of its E3 ligase activity. Interacts with the N-terminal
CC CARD domains of DDX58 and IFIH1 and competes with the downstream
CC adapter MAVS. {ECO:0000250|UniProtKB:Q5XPI4}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the KPC complex composed of RNF123/KPC1 and
CC UBAC1/KPC2. Interacts with UBAC1 and CDKN1B via its N-terminal domain.
CC Interacts with DDX58 (via N-terminus) and IFIH1 (via N-terminus).
CC {ECO:0000250|UniProtKB:Q5XPI4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5XPI4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XPI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XPI3-2; Sequence=VSP_020651;
CC -!- PTM: Ubiquitinated, leading to its degradation. Deubiquitinated by
CC USP19, thereby stimulating CDKN1B ubiquitin-dependent degradation.
CC {ECO:0000250|UniProtKB:D3ZXK7}.
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DR EMBL; AY744153; AAU93471.1; -; mRNA.
DR EMBL; BC057082; AAH57082.1; -; mRNA.
DR CCDS; CCDS52922.1; -. [Q5XPI3-1]
DR CCDS; CCDS81072.1; -. [Q5XPI3-2]
DR RefSeq; NP_001298081.1; NM_001311152.1. [Q5XPI3-2]
DR RefSeq; NP_115932.1; NM_032543.2. [Q5XPI3-1]
DR RefSeq; XP_006511940.1; XM_006511877.3. [Q5XPI3-2]
DR RefSeq; XP_006511941.1; XM_006511878.2. [Q5XPI3-2]
DR RefSeq; XP_006511942.1; XM_006511879.3. [Q5XPI3-2]
DR RefSeq; XP_017169196.1; XM_017313707.1. [Q5XPI3-1]
DR AlphaFoldDB; Q5XPI3; -.
DR SMR; Q5XPI3; -.
DR BioGRID; 220011; 16.
DR STRING; 10090.ENSMUSP00000125745; -.
DR iPTMnet; Q5XPI3; -.
DR PhosphoSitePlus; Q5XPI3; -.
DR EPD; Q5XPI3; -.
DR MaxQB; Q5XPI3; -.
DR PaxDb; Q5XPI3; -.
DR PRIDE; Q5XPI3; -.
DR ProteomicsDB; 300531; -. [Q5XPI3-1]
DR ProteomicsDB; 300532; -. [Q5XPI3-2]
DR Antibodypedia; 30603; 111 antibodies from 19 providers.
DR DNASU; 84585; -.
DR Ensembl; ENSMUST00000047746; ENSMUSP00000040803; ENSMUSG00000041528. [Q5XPI3-2]
DR Ensembl; ENSMUST00000160249; ENSMUSP00000124548; ENSMUSG00000041528. [Q5XPI3-1]
DR Ensembl; ENSMUST00000162355; ENSMUSP00000125745; ENSMUSG00000041528. [Q5XPI3-2]
DR Ensembl; ENSMUST00000178267; ENSMUSP00000136953; ENSMUSG00000041528. [Q5XPI3-1]
DR GeneID; 84585; -.
DR KEGG; mmu:84585; -.
DR UCSC; uc009roi.3; mouse. [Q5XPI3-2]
DR UCSC; uc033jmw.1; mouse. [Q5XPI3-1]
DR CTD; 63891; -.
DR MGI; MGI:2148796; Rnf123.
DR VEuPathDB; HostDB:ENSMUSG00000041528; -.
DR eggNOG; KOG2242; Eukaryota.
DR eggNOG; KOG4692; Eukaryota.
DR GeneTree; ENSGT00940000155781; -.
DR HOGENOM; CLU_006687_2_0_1; -.
DR InParanoid; Q5XPI3; -.
DR OMA; NHQHVMG; -.
DR OrthoDB; 54386at2759; -.
DR PhylomeDB; Q5XPI3; -.
DR TreeFam; TF313546; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 84585; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rnf123; mouse.
DR PRO; PR:Q5XPI3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q5XPI3; protein.
DR Bgee; ENSMUSG00000041528; Expressed in retinal neural layer and 247 other tissues.
DR ExpressionAtlas; Q5XPI3; baseline and differential.
DR Genevisible; Q5XPI3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd12882; SPRY_RNF123; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035773; SPRY_RNF123.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363; PTHR13363; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5XPI4"
FT CHAIN 2..1314
FT /note="E3 ubiquitin-protein ligase RNF123"
FT /id="PRO_0000250448"
FT DOMAIN 74..254
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 1254..1292
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 460..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5XPI4"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZXK7"
FT MOD_RES 683
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 653
FT /note="Q -> QVWQEGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020651"
SQ SEQUENCE 1314 AA; 148652 MW; 6DB1F01109FFFD28 CRC64;
MASKGTGMSF SRKSYRLTSD AEKSRVTGIV QEKLLSDYLY RIFSPPDRGP AAATSRKPLN
FHNLPEHVDQ LLQVDSEDNE SQGQVEGRLG PSTVVLDHTG GFEGLLLVDD DLLGVIGHSN
FGTIRSTTCV YKGKWVYEVL ISSQGLMQIG WCTINCRFNQ EEGVGDTHNS YAYDGNRVRK
WNVTTTNYGK AWAAGDIVSC LIDLDDGTLS FCLNGVSLGT AFENLSRGLG MAYFPAISLS
FKESVAFNFG SRPLRYPVAG FRPLQDPPFA DLVRAQRLLG CFQAVLSVEL DPVEGRLVET
ESSEWQLQGQ PTVLLTLAHI FHHFAPLLRK VYLVEAVLMS FLLGVVEKGT PEQAQSVVHQ
ILDLLWLFME DYEVQDCLKQ LMMSLLRLYR FSPIVPDLGL QIHYLRLTMS ILRHEKSRKF
LLSNVLFDML RSVVFFYIKS PLRVEEAGLK ELIPTTWWPH RSSRESRDGK EAREETTEER
QRRRAYERGC QRLKKRIEVV EELQVQILKL LLDNKDDNGG EASRYIFLTK FRKFLQENAS
GRGNTPVLCP PEYMVCFLHR LVSALRFYWD EYKASNPRAS FSEEAYIPPQ IFYNGKVDYF
DLQRLGGLLS HLRKTLKDDL ASKANIVIDP LELQAATMDD LDEDEEPAPS AAQRPMQALA
IGGALPLPRP GWLSSPTLGR ANRFLSTAAV SLMTPRRLLS TMEKVKVRSL NVEQRTREDI
EGSHWNEGLL LGRPPEEPEQ PLTENSLLEV LDGTVMMYNL SVHQQLGKMV GVSDDVNEYA
MALRDTEDKL RRCPKRRKDI LAELTKSQKV FSEKLDHLSR RLAWVHATVY SQEKMLDIYW
LLRVCLRTIE HGDRTGSLFA FMPEFYLSVA INSYSALKNY FGPVHSMEEL PGYEETLTRL
AAILAKHFAD PRIVGTDIRD SLMQALASYV CYPHSLRAVE RIPEEQRIAM VRNLLAPYEQ
RPWAQTNWIL VRLWRGCGFG YRYTRLPHLL KTKPEDANLP SLQKPCPSTL LQQHMADLLR
QGSDVAPSFL NSVLNQLNWA FSEFIGMIQE IQQAAERLER NFVDSRQLKV CATCFDLSVS
LLRVLEMTIT LVPEIFLDWS RPTSEMLLRR LAQLLNQVLN RVTAERNLFD RVVTLRLPGL
ESVDHYPILV AVTGILVRLL VHGPTSETEQ ATSVLLADPC FQLRSICYLL GQPEPLAPGT
TLPAPDRKRF SLQSYTDYIS AEELAQVEQM LAHLTAASAQ AAAASLPTNE EDLCPICYAH
PISAVFQPCG HKSCKACINQ HLMNNKDCFF CKATIVSVED WDKAANTSAM SSAA
