TRI44_MOUSE
ID TRI44_MOUSE Reviewed; 346 AA.
AC Q9QXA7; Q80SV9; Q9JHR8;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Tripartite motif-containing protein 44;
DE AltName: Full=Protein DIPB;
DE AltName: Full=Protein Mc7;
GN Name=Trim44; Synonyms=Dipb;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=11165382; DOI=10.1016/s0169-328x(00)00281-3;
RA Boutou E., Matsas R., Mamalaki A.;
RT "Isolation of a mouse brain cDNA expressed in developing neuroblasts and
RT mature neurons.";
RL Brain Res. Mol. Brain Res. 86:153-167(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Castello A., Chafey P., Lambert M., Collod-Beroud G.;
RT "Identification of a novel brain potential partner of dystrophin and
RT utrophin C-terminal end.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-346.
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=19358823; DOI=10.1016/j.bbrc.2009.04.010;
RA Urano T., Usui T., Takeda S., Ikeda K., Okada A., Ishida Y., Iwayanagi T.,
RA Otomo J., Ouchi Y., Inoue S.;
RT "TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase.";
RL Biochem. Biophys. Res. Commun. 383:263-268(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 AND SER-341, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in the process of differentiation and
CC maturation of neuronal cells (By similarity). May regulate the activity
CC of TRIM17 (By similarity). Is a negative regulator of PAX6 expression
CC (By similarity). {ECO:0000250|UniProtKB:Q96DX7}.
CC -!- SUBUNIT: Interacts (via coiled coil) with TRIM17 (via coiled coil).
CC {ECO:0000250|UniProtKB:Q96DX7}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in brain with high level in
CC cerebral hemispheres and cerebellum. Lower expression in kidney, lung
CC and spleen. In brain is detected in the hippocampus, thalamic and
CC pretectal nuclei, substantia nigra, the dorsal part of the medulla, the
CC cerebellum, in the olfactory nucleus, other cortical areas apart from
CC hippocampus and the striatum. Indeed expression is confined in neuronal
CC somata namely in the CA3 region and dentate gyrus of the hippocampus,
CC caudate-putamen, parabranchial nucleus, olfactory nucleus, cortex, deep
CC cerebellar nuclei and thalamus. Also highly expressed in the spleen.
CC thymus and testis. {ECO:0000269|PubMed:19358823}.
CC -!- DEVELOPMENTAL STAGE: Expression was detected in brain at 14 dpc and 18
CC dpc. At P5 expression in cerebellum is detected in both the dividing
CC neuroblasts and post-mitotic neurons of the external granular layer as
CC well as in the developing granule neurons of the internal granular
CC layer while the expression in Purkinje cells was lower. At P10 the
CC expression in external and internal granular layers remained strong
CC while at the same time the Purkinje cells also acquired significant
CC level of expression.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39979.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH45602.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ278191; CAB95697.1; -; mRNA.
DR EMBL; AJ249129; CAB65270.1; -; mRNA.
DR EMBL; BC039979; AAH39979.1; ALT_INIT; mRNA.
DR EMBL; BC045602; AAH45602.1; ALT_INIT; mRNA.
DR RefSeq; NP_064663.2; NM_020267.2.
DR AlphaFoldDB; Q9QXA7; -.
DR SMR; Q9QXA7; -.
DR IntAct; Q9QXA7; 1.
DR STRING; 10090.ENSMUSP00000099633; -.
DR iPTMnet; Q9QXA7; -.
DR PhosphoSitePlus; Q9QXA7; -.
DR EPD; Q9QXA7; -.
DR MaxQB; Q9QXA7; -.
DR PaxDb; Q9QXA7; -.
DR PRIDE; Q9QXA7; -.
DR ProteomicsDB; 259322; -.
DR DNASU; 80985; -.
DR GeneID; 80985; -.
DR KEGG; mmu:80985; -.
DR CTD; 54765; -.
DR MGI; MGI:1931835; Trim44.
DR eggNOG; ENOG502RHR7; Eukaryota.
DR InParanoid; Q9QXA7; -.
DR OrthoDB; 869824at2759; -.
DR PhylomeDB; Q9QXA7; -.
DR BioGRID-ORCS; 80985; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Trim44; mouse.
DR PRO; PR:Q9QXA7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXA7; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061944; P:negative regulation of protein K48-linked ubiquitination; ISO:MGI.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..346
FT /note="Tripartite motif-containing protein 44"
FT /id="PRO_0000220373"
FT ZN_FING 176..217
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 68..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 292..327
FT /evidence="ECO:0000255"
FT COMPBIAS 92..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 82
FT /note="A -> G (in Ref. 1; CAB95697)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Q -> R (in Ref. 2; CAB65270)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="Missing (in Ref. 1; CAB95697 and 3; AAH39979/
FT AAH45602)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="D -> H (in Ref. 2; CAB65270)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="K -> T (in Ref. 2; CAB65270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38272 MW; 8FE36AB7C1F198E1 CRC64;
MASGVGAACE ELPPDGTCDE CEPDEAPGAE EVCRDCGFCY CRRHADAHRQ KFLSHRLAAY
VHGAQAWTPP ASGGDDALPE DAEAKGEAEG EVESEVGEEE SETEVDSESE EESETEEDSE
DESDEESEED SEEEMEDEQE SEAEEDNQEE GESEAEGETE AESEFDPEIE MEAERVAKRK
CPDHGLDLST YCQEDRQLIC VLCPVIGAHR GHQLSTLDEA FEELRSKDSG GLKAAMIELV
ERLKFKSSDP KVTRDQMKIF IQQEFKKVQK VIADEEQKAL HLVDIQEAMA TAHVTEILAD
IQSHMDRLMT QMAQAKEQLD TSNESAEPKA EGDEEGPSGA SEEEDT
