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TRI33_DANRE
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   03-AUG-2022, entry version 104.
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; Q6E2N3; -.
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   Proteomes; UP000814640; Unplaced.
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 from RNA polymerase II promoter; IGI:ZFIN.
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; 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; 2.
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   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
 
 
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