LITAF_RAT
ID LITAF_RAT Reviewed; 161 AA.
AC P0C0T0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog;
DE Short=LPS-induced TNF-alpha factor homolog;
DE AltName: Full=Estrogen-enhanced transcript protein 1;
DE Short=Eet-1;
GN Name=Litaf;
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], INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=9275072; DOI=10.1210/endo.138.9.5384;
RA Everett L.M., Li A., Devaraju G., Caperell-Grant A., Bigsby R.M.;
RT "A novel estrogen-enhanced transcript identified in the rat uterus by
RT differential display.";
RL Endocrinology 138:3836-3841(1997).
CC -!- FUNCTION: Plays a role in endosomal protein trafficking and in
CC targeting proteins for lysosomal degradation. Plays a role in targeting
CC endocytosed EGFR and ERGG3 for lysosomal degradation, and thereby helps
CC down-regulate downstream signaling cascades. Helps recruit the ESCRT
CC complex components TSG101, HGS and STAM to cytoplasmic membranes.
CC Probably plays a role in regulating protein degradation via its
CC interaction with NEDD4. May also contribute to the regulation of gene
CC expression in the nucleus. Binds DNA (in vitro) and may play a
CC synergistic role with STAT6 in the nucleus in regulating the expression
CC of various cytokines. May regulate the expression of numerous
CC cytokines, such as TNF, CCL2, CCL5, CXCL1, IL1A and IL10.
CC {ECO:0000250|UniProtKB:Q99732}.
CC -!- SUBUNIT: Monomer. Interacts with NEDD4. Interacts (via PSAP motif) with
CC TSG101, a component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I). Interacts with WWOX. Interacts with STAM, a
CC component of the ESCRT-0 complex; the interaction is direct. Identified
CC in a complex with STAM and HGS; within this complex, interacts directly
CC with STAM, but not with HGS. Interacts with STAT6.
CC {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 -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9275072}.
CC -!- INDUCTION: By estrogen in vagina, cervix, uterus and kidney.
CC {ECO:0000269|PubMed:9275072}.
CC -!- DOMAIN: The PPxY motif mediates interaction with WWOX and NEDD4.
CC {ECO:0000250|UniProtKB:Q99732}.
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. It interacts specifically with
CC phosphatidylethanolamine lipid headgroups, but not with
CC phosphoglycerol, phosphocholine, phosphoserine or
CC inositolhexakisphosphate. {ECO:0000250|UniProtKB:Q99732}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to EGF.
CC {ECO:0000250|UniProtKB:Q99732}.
CC -!- SIMILARITY: Belongs to the CDIP1/LITAF family. {ECO:0000305}.
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DR EMBL; U53184; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001099205.1; NM_001105735.2.
DR AlphaFoldDB; P0C0T0; -.
DR STRING; 10116.ENSRNOP00000003412; -.
DR PaxDb; P0C0T0; -.
DR Ensembl; ENSRNOT00000108567; ENSRNOP00000085735; ENSRNOG00000002520.
DR GeneID; 65161; -.
DR KEGG; rno:65161; -.
DR UCSC; RGD:69294; rat.
DR CTD; 9516; -.
DR RGD; 69294; Litaf.
DR eggNOG; ENOG502S2GM; Eukaryota.
DR GeneTree; ENSGT00940000155366; -.
DR HOGENOM; CLU_095549_3_0_1; -.
DR InParanoid; P0C0T0; -.
DR OMA; SCMDVHH; -.
DR OrthoDB; 1564782at2759; -.
DR PhylomeDB; P0C0T0; -.
DR TreeFam; TF313294; -.
DR PRO; PR:P0C0T0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002520; Expressed in jejunum and 19 other tissues.
DR ExpressionAtlas; P0C0T0; baseline and differential.
DR Genevisible; P0C0T0; RN.
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:0005576; C:extracellular region; TAS:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0050699; F:WW domain binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0001817; P:regulation of cytokine production; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
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..161
FT /note="Lipopolysaccharide-induced tumor necrosis factor-
FT alpha factor homolog"
FT /id="PRO_0000084442"
FT DOMAIN 76..160
FT /note="LITAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT REGION 111..134
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000305"
FT MOTIF 20..23
FT /note="PPxY motif"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
SQ SEQUENCE 161 AA; 17030 MW; 81DD842A4374F1FC CRC64;
MSAPGPYQAA AGPSVMPTAP PTYEETVGVN SYYPTPPAPQ PGPATGLITG PDGKGMNPPS
YYTQPVPVPN ANAIAVQTVY VQQPISFYDR PIQMCCPSCN KMIVTQLSYN AGALTWLSCG
SLCLLGCVAG CCFIPFCVDA LQDVDHYCPN CKALLGTYKR L
