ID   TRI44_RAT               Reviewed;         344 AA.
AC   Q6QA27;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Tripartite motif-containing protein 44;
DE   AltName: Full=Protein DIPB;
GN   Name=Trim44; Synonyms=Dipb;
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 [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Midbrain;
RA   Ju S.K.;
RT   "Cloning and sequencing of cDNA encoding DIPB from rat.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AY551091; AAS58454.1; -; mRNA.
DR   RefSeq; NP_001013221.1; NM_001013203.1.
DR   AlphaFoldDB; Q6QA27; -.
DR   SMR; Q6QA27; -.
DR   STRING; 10116.ENSRNOP00000007018; -.
DR   PaxDb; Q6QA27; -.
DR   Ensembl; ENSRNOT00000007018; ENSRNOP00000007018; ENSRNOG00000005191.
DR   GeneID; 362172; -.
DR   KEGG; rno:362172; -.
DR   UCSC; RGD:1304877; rat.
DR   CTD; 54765; -.
DR   RGD; 1304877; Trim44.
DR   eggNOG; ENOG502RHR7; Eukaryota.
DR   InParanoid; Q6QA27; -.
DR   OrthoDB; 869824at2759; -.
DR   PhylomeDB; Q6QA27; -.
DR   TreeFam; TF333911; -.
DR   PRO; PR:Q6QA27; -.
DR   Proteomes; UP000002494; Chromosome 3.
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:RGD.
DR   GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:RGD.
DR   GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
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   2: Evidence at transcript level;
KW   Coiled coil; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..344
FT                   /note="Tripartite motif-containing protein 44"
FT                   /id="PRO_0000220374"
FT   ZN_FING         174..215
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          69..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          290..325
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        91..165
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXA7"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXA7"
SQ   SEQUENCE   344 AA;  38086 MW;  FAC0A10A08800EF3 CRC64;
     MASGVGAACE ELPPDGTCDE CEPDEAPGAE EVCRDCGFCY CRRHADAHRQ KFLSHRLAAY
     VHGAQAWTPP ASGDDALPED VEAKGEAEGE VESEVGEEES ESEVDSESEE ESETEEDSED
     ESDEESEEDS EEEMEDEQES EAEEDNQEGE SEAEGETEAE SEFDPEIEME AERVAKRKCP
     DHGLDLSTYC QEDRQLICVL CPVIGAHRGH QLSTLDEAFE ELRSKDSGGL KAAMIELVER
     LKFKSSDPKV TRDQMKVFIQ QEFKKVQKVI ADEEQKALHL VDIQEAMATA HVTEILADIQ
     SHMDRLMTQM AQAKEQLDTS NESAEPKAEG DEEGPSGASE EEDT