ID   TRI44_BOVIN             Reviewed;         338 AA.
AC   A6QQX5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Tripartite motif-containing protein 44;
GN   Name=TRIM44;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal brain;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC150032; AAI50033.1; -; mRNA.
DR   RefSeq; NP_001098484.1; NM_001105014.2.
DR   AlphaFoldDB; A6QQX5; -.
DR   SMR; A6QQX5; -.
DR   STRING; 9913.ENSBTAP00000051946; -.
DR   PaxDb; A6QQX5; -.
DR   PRIDE; A6QQX5; -.
DR   Ensembl; ENSBTAT00000052439; ENSBTAP00000051946; ENSBTAG00000037389.
DR   GeneID; 782816; -.
DR   KEGG; bta:782816; -.
DR   CTD; 54765; -.
DR   VEuPathDB; HostDB:ENSBTAG00000037389; -.
DR   VGNC; VGNC:36336; TRIM44.
DR   eggNOG; ENOG502RHR7; Eukaryota.
DR   GeneTree; ENSGT00440000034605; -.
DR   HOGENOM; CLU_070347_0_0_1; -.
DR   InParanoid; A6QQX5; -.
DR   OMA; LREAYMW; -.
DR   OrthoDB; 869824at2759; -.
DR   TreeFam; TF333911; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000037389; Expressed in choroid plexus and 107 other tissues.
DR   ExpressionAtlas; A6QQX5; baseline.
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; IEA:Ensembl.
DR   GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..338
FT                   /note="Tripartite motif-containing protein 44"
FT                   /id="PRO_0000324097"
FT   ZN_FING         171..212
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          109..153
FT                   /evidence="ECO:0000255"
FT   COILED          257..322
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        83..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..162
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..338
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ   SEQUENCE   338 AA;  37512 MW;  9717AEB3D5AACCA3 CRC64;
     MASGGGAAFE ELPHDGTCDE CEPDEAPGAE EVCRECGFCY CRHHAEAHGQ KFPRHHLAEY
     VHCAAQAWTP GARGDGAGEE AVEAPVENEK ALENEAGEGI ESEEDSEPEE ESETEEESED
     ESEEDSEEEM EDEQESEAEE DNQEEGESEA EGETEAESEF DPEIEMEAER VAKRKCPDHG
     LDLSTYCQED KQLICVLCPV IGAHHGHHLS TLDEAFEELR SKDSGGLKAA MIELVERLKF
     KSSDPKVTRD QMKMFIQQEF KKVQKVIADE EQKALHLVDI QEAMATAHVT EILADIQSHM
     DRLMTQMAQA KEQLDTSNES AEPKAEGDEE EPGGTDED