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   27-MAR-2024, entry version 171.
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; 10090-ENSMUSP00000069371; -.
DR   PeptideAtlas; Q8BGX0; -.
DR   ProteomicsDB; 259312; -. [Q8BGX0-1]
DR   ProteomicsDB; 259313; -. [Q8BGX0-2]
DR   ProteomicsDB; 259314; -. [Q8BGX0-3]
DR   Pumba; Q8BGX0; -.
DR   Antibodypedia; 11584; 302 antibodies from 32 providers.
DR   Ensembl; ENSMUST00000022225.12; ENSMUSP00000022225.6; ENSMUSG00000021712.16. [Q8BGX0-1]
DR   Ensembl; ENSMUST00000069174.6; ENSMUSP00000069371.6; ENSMUSG00000021712.16. [Q8BGX0-2]
DR   Ensembl; ENSMUST00000069187.12; ENSMUSP00000070767.6; ENSMUSG00000021712.16. [Q8BGX0-3]
DR   UCSC; uc007rsx.1; mouse. [Q8BGX0-1]
DR   UCSC; uc007rsy.1; mouse. [Q8BGX0-2]
DR   UCSC; uc011zeg.1; mouse. [Q8BGX0-3]
DR   AGR; MGI:1933161; -.
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; VCEEVFT; -.
DR   OrthoDB; 2939799at2759; -.
DR   PhylomeDB; Q8BGX0; -.
DR   TreeFam; TF320703; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 81003; 1 hit in 64 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 255 other cell types or tissues.
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:0061630; F:ubiquitin protein ligase activity; 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:0010508; P:positive regulation of autophagy; ISO:MGI.
DR   GO; GO:0031401; P:positive regulation of protein modification process; ISO:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:HGNC-UCL.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd04158; ARD1; 1.
DR   CDD; cd19773; Bbox2_TRIM23_C-IX_rpt1; 1.
DR   CDD; cd19774; Bbox2_TRIM23_C-IX_rpt2; 1.
DR   CDD; cd16645; mRING-HC-C3HC3D_TRIM23_C-IX; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   InterPro; IPR027370; Znf-RING_euk.
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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1.
DR   PANTHER; PTHR11711:SF163; E3 UBIQUITIN-PROTEIN LIGASE TRIM23; 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; SM00177; ARF; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 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.
DR   Genevisible; Q8BGX0; MM.
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
//