LITAF_DANRE
ID LITAF_DANRE Reviewed; 163 AA.
AC Q6GMG8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog;
DE Short=LPS-induced TNF-alpha factor homolog;
GN Name=litaf; ORFNames=zgc:91882;
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 [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in endosomal protein trafficking and in
CC targeting proteins for lysosomal degradation. May also contribute to
CC the regulation of gene expression in the nucleus. Binds DNA (in vitro)
CC and may play a synergistic role in the nucleus in regulating the
CC expression of numerous cytokines. {ECO:0000250|UniProtKB:Q99732}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99732}. Nucleus
CC {ECO:0000250|UniProtKB:Q99732}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q99732}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q99732}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q99732}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q99732}. Cell membrane
CC {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q99732}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q99732}. Note=Associated with membranes of
CC lysosomes, early and late endosomes. Can translocate from the cytoplasm
CC into the nucleus (By similarity). Detected at Schmidt-Lanterman
CC incisures and in nodal regions of myelinating Schwann cells (By
CC similarity). {ECO:0000250|UniProtKB:Q99732,
CC ECO:0000250|UniProtKB:Q9JLJ0}.
CC -!- DOMAIN: The LITAF domain is stabilized by a bound zinc ion. The LITAF
CC domain contains an amphipathic helix that mediates interaction with
CC lipid membranes. {ECO:0000250|UniProtKB:Q99732}.
CC -!- SIMILARITY: Belongs to the CDIP1/LITAF family. {ECO:0000305}.
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DR EMBL; BC074085; AAH74085.1; -; mRNA.
DR RefSeq; NP_001002184.1; NM_001002184.1.
DR AlphaFoldDB; Q6GMG8; -.
DR STRING; 7955.ENSDARP00000069049; -.
DR PaxDb; Q6GMG8; -.
DR Ensembl; ENSDART00000157619; ENSDARP00000130720; ENSDARG00000103483.
DR GeneID; 431731; -.
DR KEGG; dre:431731; -.
DR CTD; 9516; -.
DR ZFIN; ZDB-GENE-040704-23; litaf.
DR eggNOG; ENOG502S2GM; Eukaryota.
DR GeneTree; ENSGT00940000155366; -.
DR HOGENOM; CLU_095549_3_0_1; -.
DR InParanoid; Q6GMG8; -.
DR OMA; SCMDVHH; -.
DR OrthoDB; 1564782at2759; -.
DR PhylomeDB; Q6GMG8; -.
DR TreeFam; TF313294; -.
DR PRO; PR:Q6GMG8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000103483; Expressed in spleen and 30 other tissues.
DR ExpressionAtlas; Q6GMG8; baseline and differential.
DR GO; GO:0098559; C:cytoplasmic side of early endosome membrane; ISS:UniProtKB.
DR GO; GO:0098560; C:cytoplasmic side of late endosome membrane; ISS:UniProtKB.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR InterPro; IPR006629; LITAF.
DR InterPro; IPR037519; LITAF_fam.
DR PANTHER; PTHR23292; PTHR23292; 1.
DR Pfam; PF10601; zf-LITAF-like; 1.
DR SMART; SM00714; LITAF; 1.
DR PROSITE; PS51837; LITAF; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; DNA-binding; Endosome; Golgi apparatus; Lysosome;
KW Membrane; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..163
FT /note="Lipopolysaccharide-induced tumor necrosis factor-
FT alpha factor homolog"
FT /id="PRO_0000084444"
FT DOMAIN 78..162
FT /note="LITAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..136
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000305"
FT MOTIF 22..25
FT /note="PPxY motif"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
SQ SEQUENCE 163 AA; 17450 MW; 8854B5A40DE4BC29 CRC64;
MAMPMPTAPP MENTTLVGHP PPPSYDEISG ANPYYPAGPY PPADMKASGP PPYPTQEYNQ
MYPPTAQGQP VTSPVVAVQT VYVQPGLVFG NVPVQAHCPV CSQSVITRLE YSSGPLVWLS
CAGLAVFGCI YGCCLIPFCI EDLKDVTHHC PNCSSVLGVH KRF
