TRI33_XENLA
ID TRI33_XENLA Reviewed; 1091 AA.
AC Q56R14;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM33;
DE EC=2.3.2.27;
DE AltName: Full=Ectodermin;
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=ecto;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE,
RP INTERACTION WITH SMAD4, MUTAGENESIS OF CYS-97 AND CYS-100, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15820681; DOI=10.1016/j.cell.2005.01.033;
RA Dupont S., Zacchigna L., Cordenonsi M., Soligo S., Adorno M., Rugge M.,
RA Piccolo S.;
RT "Germ-layer specification and control of cell growth by Ectodermin, a Smad4
RT ubiquitin ligase.";
RL Cell 121:87-99(2005).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase for smad4. Promotes
CC ectoderm embryonic development at the expense of other germ layers.
CC Inhibits mesodermal differentiation. Promotes neural development of the
CC ectoderm. Promotes smad4 alpha degradation via the ubiquitin proteasome
CC pathway. May act as a transcriptional repressor (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15820681}.
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: May interact with smad4.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15820681}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the animal pole of unfertilized eggs
CC and throughout cleavage stages in the prospective ectoderm germ layer.
CC Expressed at the animal pole and extending up to the marginal zone at
CC blastula stage. At the onset of gastrulation remains asymmetrically
CC enriched in the dorsal side of the early gastrula. Its expression
CC progressively diminishes as gastrulation proceeds (at protein level).
CC {ECO:0000269|PubMed:15820681}.
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DR EMBL; AY781409; AAX10105.1; -; mRNA.
DR RefSeq; NP_001089077.1; NM_001095608.1.
DR AlphaFoldDB; Q56R14; -.
DR SMR; Q56R14; -.
DR BioGRID; 591680; 2.
DR IntAct; Q56R14; 3.
DR GeneID; 733198; -.
DR KEGG; xla:733198; -.
DR CTD; 733198; -.
DR Xenbase; XB-GENE-1216172; trim33.L.
DR OrthoDB; 756911at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 733198; Expressed in blastula and 19 other tissues.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR027370; Znf-RING_LisH.
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 Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 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 1: Evidence at protein level;
KW Bromodomain; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1091
FT /note="E3 ubiquitin-protein ligase TRIM33"
FT /id="PRO_0000287228"
FT DOMAIN 937..1009
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 97..154
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 180..227
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 240..281
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 850..897
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 269..361
FT /evidence="ECO:0000255"
FT COMPBIAS 15..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1070
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MUTAGEN 97
FT /note="C->A: Abolishes E3 activity but does not affect
FT interaction with smad4; when associated with A-100."
FT /evidence="ECO:0000269|PubMed:15820681"
FT MUTAGEN 100
FT /note="C->A: Abolishes E3 activity but does not affect
FT interaction with smad4; when associated with A-97."
FT /evidence="ECO:0000269|PubMed:15820681"
SQ SEQUENCE 1091 AA; 120159 MW; 27E80F67B13DDAA0 CRC64;
MADNKGGGGG GGETEGDASS NNNNNSNGAG ETGSPGETES QAVEEPESAE KAPVAAVPTD
TPAEENPAPS SSSVASSSAT PASSSSSPLV VNLLDTCAVC KLSLQSRDTE PKLLPCLHSF
CRRCLPEPER QLSVPGGTNG DIQQVGVIRC LVCRQECRQI DLVDNYFVKD ASEAPNTDEK
SEQVCTSCED NASAVGFCVE CGEWLCKTCI EAHQRVKFTK DHIITNKEDV SSESVGASGQ
RPVFCPVHKQ EQLKLFCETC DRLTCRDCQL LEHKEHRYQF LEEAFQNQKG AIENLLAKLL
EKKNYVHFAA TQVQNRIKEV NETNKRVEQE IKVAIFTLIN EINKKGKSLL QQLESVTKER
QIKLVQQQND ITGLSRQIKH VMTFTNWAIA SGSSTALLYS KRLITFQLRH ILKARCDPVP
AANGAIRFHC DPTFWAKNVV NLGNLVIENK PTTGFTPNVV VGQVPQGANH VNKPPAQINL
AQLRLQHMQQ QVYAQKQQQL QMRMAQPPGQ HQRPSAPQVM HQQPPRLISM QSMPRNNMNC
GPFQAHQMRM AQNAAQNAAR MSGVPRHNGM QYSMMQPHLQ RQHSNPGHAG PFPVVSVHNN
TINPTSPTTA TMANANRGPT SPSVTSIELI PSVTNPENLP SLPDIPPIQL EDAGSSNLDN
LLSRYISLGH QLPQPTSNMN PSPAPSAMSP GSTGLSNSHT PVRPPSTSST GSRGSCGSSS
RTVERNSSFK SDPVKVKQEP GTEEEVCSFS GPVKQEKAED GRRSACMLSS PESSLTPPLT
TNVHLETDLE SLAALENNVK TEPNNTSQSC RQSSHVSLVN GKSAVRNSMH RPPRGGGGGD
GSNKDDDPNE DWCAVCQNGG DLLCCEKCPK VFHLTCHVPT LLSFPSGEWI CTFCRDLNKP
EVEYDCDNSQ HSKKGKTVQG LSPVDQMKCE RLLLYLYCHE LSIEFQEPVP ATIPNYYKII
KKPMDLSTVK KKLQKKHSQH YQTPEDFVAD VRLIFKNCER FNEMMKVVQA YADTQEINLQ
NDSEVAQAGK AVVLYFEEKL PAIYPDRTFQ PLPEFEAEDD DGDVTDDSDD DDFVQPRRKR
LKSEERPVHI K
