ID TRI33_DANRE Reviewed; 1163 AA.
AC Q6E2N3; Q29RE2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM33;
DE EC=2.3.2.27;
DE AltName: Full=Ectodermin homolog;
DE AltName: Full=Protein moonshine;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM33 {ECO:0000305};
DE AltName: Full=Transcription intermediary factor 1-gamma;
DE Short=TIF1-gamma;
DE AltName: Full=Tripartite motif-containing protein 33;
GN Name=trim33; Synonyms=mon;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Kidney marrow;
RX PubMed=15314655; DOI=10.1371/journal.pbio.0020237;
RA Ransom D.G., Bahary N., Niss K., Traver D., Burns C., Trede N.S.,
RA Paffett-Lugassy N., Saganic W.J., Lim C.A., Hersey C., Zhou Y., Barut B.A.,
RA Lin S., Kingsley P.D., Palis J., Orkin S.H., Zon L.I.;
RT "The zebrafish moonshine gene encodes transcriptional intermediary factor 1
RT gamma, an essential regulator of hematopoiesis.";
RL PLoS Biol. 2:1188-1196(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as an E3 ubiquitin-protein ligase and a
CC transcriptional repressor (By similarity). Involved in the regulation
CC of embryonic and adult hematopoiesis. Required for normal development
CC and survival of both committed erythroid progenitor cells and posterior
CC mesenchymal cells. {ECO:0000250, ECO:0000269|PubMed:15314655}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15314655}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6E2N3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6E2N3-2; Sequence=VSP_025397;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and throughout the
CC embryo during blastula stage. During gastrulation and epiboly stages,
CC strongly expressed in the mesendoderm of the germ ring. Expressed at
CC the tail bud and in early somite stages in a horseshoeshaped population
CC of ventral/lateral mesoderm cells that will give rise to blood.
CC Detected in ventral-lateral mesoderm between the one- to three-somite
CC stages and increases through early development. Expressed in lateral
CC stripes of mesoderm at five somites. Expressed broadly in the brain,
CC spinal cord, trunk, and tail mesenchyme, but is at much higher levels
CC in hematopoietic cells of the blood island at 24-72 hours post-
CC fertilization (hpf). {ECO:0000269|PubMed:15314655}.
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DR EMBL; AY598453; AAT70732.1; -; mRNA.
DR EMBL; BC114245; AAI14246.1; -; mRNA.
DR AlphaFoldDB; Q6E2N3; -.
DR SMR; Q6E2N3; -.
DR STRING; 7955.ENSDARP00000025140; -.
DR PaxDb; 7955-ENSDARP00000025140; -.
DR AGR; ZFIN:ZDB-GENE-030131-2773; -.
DR ZFIN; ZDB-GENE-030131-2773; trim33.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q6E2N3; -.
DR PhylomeDB; Q6E2N3; -.
DR Reactome; R-DRE-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6E2N3; -.
DR Proteomes; UP000000437; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048066; P:developmental pigmentation; IMP:ZFIN.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:ZFIN.
DR GO; GO:0033333; P:fin development; IMP:ZFIN.
DR GO; GO:0048246; P:macrophage chemotaxis; IMP:ZFIN.
DR GO; GO:1905517; P:macrophage migration; IMP:ZFIN.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:ZFIN.
DR GO; GO:1990266; P:neutrophil migration; IMP:ZFIN.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; IMP:ZFIN.
DR GO; GO:0060215; P:primitive hemopoiesis; IMP:ZFIN.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0034243; P:regulation of transcription elongation by RNA polymerase II; IGI:ZFIN.
DR CDD; cd19847; Bbox1_TIF1g_C-VI; 1.
DR CDD; cd19830; Bbox2_TIF1g_C-VI; 1.
DR CDD; cd05502; Bromo_tif1_like; 1.
DR CDD; cd15541; PHD_TIF1_like; 1.
DR CDD; cd16766; RING-HC_TIF1gamma; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45915:SF3; E3 UBIQUITIN-PROTEIN LIGASE TRIM33; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Bromodomain; Coiled coil; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1163
FT /note="E3 ubiquitin-protein ligase TRIM33"
FT /id="PRO_0000287227"
FT DOMAIN 1008..1080
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 129..188
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 215..268
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 275..316
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 921..968
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 345..369
FT /evidence="ECO:0000255"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025397"
FT CONFLICT 544..545
FT /note="Missing (in Ref. 2; AAI14246)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="S -> T (in Ref. 2; AAI14246)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="A -> T (in Ref. 2; AAI14246)"
FT /evidence="ECO:0000305"
FT CONFLICT 1084
FT /note="E -> G (in Ref. 2; AAI14246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1163 AA; 128198 MW; A7DBA0C625323F5D CRC64;
MEVEASGTED NGDGGAKEPE AVVSIDTETK EAADEAKSQE TVPQTPTTSS DSSSSGGGGE
ATDGTPNAES ADPPPPPPPP PPPPPSTPAD STAAAASPAV LTEMSPPPPA STSSSSSTPA
APINLLDTCA VCKQSLQNRD CEPKLLPCLH SFCLKCIPQP DRKITMPVQG PHGQDTRIVN
VMRCTVCHQD YKQIDMVDNY FVKDTSEATN TSVENSTQVC TSCEDNASAI GFCVECGEWL
CKTCIEAHQR VKFTKDHKIR KKEEVSPESV GTSGQRPVFC PVHKQEALKL FCETCDTLTC
RDCQLLEHKE HRYQFLDEAC QNQKGIIATF MTKLQEKRGL VEYSASEVQK RLKEVAETHK
KVEHEIKIAV FTLINEINKK GKSLLQQLES VTKDRSMKLL SQQRDISVLA QQIIHVLNFT
NWAITNGSST ALLYSKRLIT YQLRLIMKAR VDAVPPANGA VRFFCDPTFW AKNVVNLGNL
VIEKVAPTAP PSNMMVNQQI SPGHNHPGKH SGQINLAQLR LQHMQQAAIA QKHQQQHQHH
QQQQHQHQHQ QQQQQQQQQQ QQQQQQQQQQ QHQQQIQQQM RIASQMSQHP RQGAPQMIQQ
PPPRLISMQA LHRGGVNGSS HMFPPHHLRM VSAQNRMPSA QPRLNGQPYP MMQPQLQRQH
SNPGHAGPFP VASLHNISAA NPTSPTSASM ANAHMHRGPS SPVITPIELI PSVTNPENLP
CLPDIPPIQL EDAGSSTLDN ILSRYISANA YPTVGPTNPS PGPSTHSPGS SGLSNSHTPA
RPSSTSSTGS RGSSGTTVDQ VKVKQEPGVE EECSYSGANV KTERTKDGRR SACMMSSPEG
SLTPPLPILG SVSTGSVQDI LRTLGENVKS EPQSDNLSSC TNPNSRATLT NGTSGSNGGQ
RGGATNANSQ TTAGKEDDPN EDWCAVCQNG GELLCCDHCP KVFHITCHIP TLKSSPSGDW
MCTFCRNLAN PEIEYNCDDD PPRNKEKNEM AMSPEEQRRC ERLLLHVFCH ELSTEFQEPV
PTSVPNYYKI IKHPMDLTLV KRKLQRKHPL HYKSPKEFVS DVRLVFSNCA KYNEMSRIIQ
VYDEEKQSNV QADSEVAEAG KAVSLYFEER LLEIFPEQTF PVVMEKETQI EAEKEDSDDS
DDDIIQPKRK RLKVDTEMLL HIK
//
