TRI23_RAT
ID TRI23_RAT Reviewed; 573 AA.
AC P36407; D3ZT39;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 153.
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=Ard-1, Ard1, Arfd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-573 (ISOFORM 1).
RX PubMed=8473324; DOI=10.1016/s0021-9258(18)52945-8;
RA Mishima K., Tsuchiya M., Nightingale M.S., Moss J., Vaughan M.;
RT "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-
RT terminal ADP-ribosylation factor domain.";
RL J. Biol. Chem. 268:8801-8807(1993).
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=2;
CC Name=1;
CC IsoId=P36407-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36407-2; Sequence=VSP_039562;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L04760; AAA41301.1; -; mRNA.
DR RefSeq; NP_001094107.1; NM_001100637.1.
DR AlphaFoldDB; P36407; -.
DR SMR; P36407; -.
DR BioGRID; 249495; 1.
DR STRING; 10116.ENSRNOP00000016647; -.
DR jPOST; P36407; -.
DR PaxDb; P36407; -.
DR PRIDE; P36407; -.
DR GeneID; 81002; -.
DR KEGG; rno:81002; -.
DR UCSC; RGD:621587; rat. [P36407-1]
DR CTD; 373; -.
DR RGD; 621587; Trim23.
DR eggNOG; KOG0070; Eukaryota.
DR eggNOG; KOG4185; Eukaryota.
DR InParanoid; P36407; -.
DR PhylomeDB; P36407; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P36407; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; ISS:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; IDA:RGD.
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..573
FT /note="E3 ubiquitin-protein ligase TRIM23"
FT /id="PRO_0000207485"
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..573
FT /note="ARF-like"
FT COILED 351..378
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 216..276
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039562"
FT CONFLICT 61
FT /note="T -> S (in Ref. 1; AAA41301)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="C -> CE (in Ref. 1; AAA41301)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="H -> Y (in Ref. 1; AAA41301)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="G -> E (in Ref. 1; AAA41301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 63892 MW; 62263E1DE6C2C909 CRC64;
MAALAVNKPG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL
TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGHIGQY GAAEEALGIS
GESIIRCDED EAHVASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCCQ
HQVHAIEFVC LEEACQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF
TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCVRA YFSDLHETLC
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSQVSTACL HCKTLQQDDC RVVLAKQEIT
RLLETLQKQQ QQFTEVADHI QLDASIPVTF TKDNRVYHGP KMEIRVVTLG LDGAGKTTIL
FKLKQDEFMQ PIPTIGFNVE TVEYKNLKFT IWDVGGKHKL RPLWKHYYLN TQAVVFVVDS
SHRDRISEAH SELAKLLTEK ELRDALLLIF ANKQDVAGAL SVEEITELLS LHKLCCGRSW
YIQGCDARSG MGLYEGLDWL SRQLVAAGVL DVA
