TRI23_MOUSE
ID TRI23_MOUSE Reviewed; 574 AA.
AC Q8BGX0; Q8C2B6; Q8CDA4; Q8CDA7;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM23;
DE EC=2.3.2.27;
DE AltName: Full=ADP-ribosylation factor domain-containing protein 1;
DE AltName: Full=GTP-binding protein ARD-1;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM23 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 23;
GN Name=Trim23; Synonyms=Arfd1;
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; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and Thymus;
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: Acts as an E3 ubiquitin-protein ligase. Plays an essential
CC role in autophagy activation during viral infection. Mechanistically,
CC activates TANK-binding kinase 1/TBK1 by facilitating its dimerization
CC and ability to phosphorylate the selective autophagy receptor SQSTM1.
CC In order to achieve this function, TRIM23 mediates 'Lys-27'-linked
CC auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to
CC induce its GTPase activity and its recruitment to autophagosomes.
CC {ECO:0000250|UniProtKB:P36406}.
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:P36406};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Interacts with PSCD1. Interacts with UBE2D2.
CC Interacts with TBK1 (via N-terminal kinase domain) and p62/SQSTM1.
CC {ECO:0000250|UniProtKB:P36406}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36406}.
CC Endomembrane system {ECO:0000250|UniProtKB:P36406}. Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:P36406}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P36406}. Note=Membrane-associated with the Golgi
CC complex and lysosomal structures. {ECO:0000250|UniProtKB:P36406}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BGX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGX0-2; Sequence=VSP_010814;
CC Name=3;
CC IsoId=Q8BGX0-3; Sequence=VSP_010815;
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity. {ECO:0000250|UniProtKB:P36406}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the small GTPase
CC superfamily. Arf family. {ECO:0000305}.
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DR EMBL; AK030843; BAC27156.1; -; mRNA.
DR EMBL; AK030862; BAC27160.1; -; mRNA.
DR EMBL; AK039280; BAC30304.1; -; mRNA.
DR EMBL; AK042070; BAC31152.1; -; mRNA.
DR EMBL; AK088922; BAC40654.1; -; mRNA.
DR EMBL; BC056390; AAH56390.1; -; mRNA.
DR EMBL; BC059017; AAH59017.1; -; mRNA.
DR CCDS; CCDS88515.1; -. [Q8BGX0-1]
DR CCDS; CCDS88516.1; -. [Q8BGX0-3]
DR RefSeq; NP_109656.1; NM_030731.3.
DR AlphaFoldDB; Q8BGX0; -.
DR SMR; Q8BGX0; -.
DR BioGRID; 219862; 2.
DR STRING; 10090.ENSMUSP00000069371; -.
DR iPTMnet; Q8BGX0; -.
DR PhosphoSitePlus; Q8BGX0; -.
DR EPD; Q8BGX0; -.
DR jPOST; Q8BGX0; -.
DR MaxQB; Q8BGX0; -.
DR PaxDb; Q8BGX0; -.
DR PeptideAtlas; Q8BGX0; -.
DR PRIDE; Q8BGX0; -.
DR ProteomicsDB; 259312; -. [Q8BGX0-1]
DR ProteomicsDB; 259313; -. [Q8BGX0-2]
DR ProteomicsDB; 259314; -. [Q8BGX0-3]
DR Antibodypedia; 11584; 266 antibodies from 32 providers.
DR Ensembl; ENSMUST00000022225; ENSMUSP00000022225; ENSMUSG00000021712. [Q8BGX0-1]
DR Ensembl; ENSMUST00000069174; ENSMUSP00000069371; ENSMUSG00000021712. [Q8BGX0-2]
DR Ensembl; ENSMUST00000069187; ENSMUSP00000070767; ENSMUSG00000021712. [Q8BGX0-3]
DR UCSC; uc007rsx.1; mouse. [Q8BGX0-1]
DR UCSC; uc007rsy.1; mouse. [Q8BGX0-2]
DR UCSC; uc011zeg.1; mouse. [Q8BGX0-3]
DR MGI; MGI:1933161; Trim23.
DR VEuPathDB; HostDB:ENSMUSG00000021712; -.
DR eggNOG; KOG0070; Eukaryota.
DR eggNOG; KOG4185; Eukaryota.
DR GeneTree; ENSGT00940000158562; -.
DR HOGENOM; CLU_033905_0_0_1; -.
DR InParanoid; Q8BGX0; -.
DR OMA; WHIQGSS; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; Q8BGX0; -.
DR TreeFam; TF320703; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 81003; 1 hit in 61 CRISPR screens.
DR ChiTaRS; Trim23; mouse.
DR PRO; PR:Q8BGX0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BGX0; protein.
DR Bgee; ENSMUSG00000021712; Expressed in spermatocyte and 252 other tissues.
DR Genevisible; Q8BGX0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:HGNC-UCL.
DR GO; GO:0005765; C:lysosomal membrane; ISS:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISS:HGNC-UCL.
DR GO; GO:0005525; F:GTP binding; ISS:HGNC-UCL.
DR GO; GO:0003924; F:GTPase activity; ISS:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:HGNC-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:HGNC-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; Golgi apparatus; GTP-binding;
KW Lysosome; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..574
FT /note="E3 ubiquitin-protein ligase TRIM23"
FT /id="PRO_0000207484"
FT ZN_FING 31..76
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 122..168
FT /note="B box-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 390..574
FT /note="ARF-like"
FT COILED 352..379
FT /evidence="ECO:0000255"
FT BINDING 411..418
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 454..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 513..516
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..27
FT /note="MAALAVNKPGAGVDSGRQGSRGTAVVK -> MFLFYIQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010814"
FT VAR_SEQ 216..276
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010815"
FT CONFLICT 371
FT /note="Q -> K (in Ref. 1; BAC27156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 63931 MW; 678D7BDA937E16F2 CRC64;
MAALAVNKPG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL
TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGHIGQY GAAEEAIGTS
GESIIRCDED EAHVASVYCT VCATHLCSDC SQVTHSTKTL AKHRRVPLAD KPHEKTMCCQ
HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF
TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCVRA YFSDLHETLC
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSQVSTACL HCEKTLQQDD CRVVLAKQEI
TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI
LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD
SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS
WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA
