LITAF_XENTR
ID LITAF_XENTR Reviewed; 148 AA.
AC Q6P828; Q28IB0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog;
DE Short=LPS-induced TNF-alpha factor homolog;
GN Name=litaf; ORFNames=TEgg087j16.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) 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; CR760500; CAJ81689.1; -; mRNA.
DR EMBL; BC061403; AAH61403.1; -; mRNA.
DR RefSeq; NP_988970.1; NM_203639.1.
DR AlphaFoldDB; Q6P828; -.
DR STRING; 8364.ENSXETP00000053520; -.
DR PaxDb; Q6P828; -.
DR DNASU; 394567; -.
DR GeneID; 394567; -.
DR KEGG; xtr:394567; -.
DR CTD; 9516; -.
DR Xenbase; XB-GENE-1017030; litaf.
DR eggNOG; ENOG502S2GM; Eukaryota.
DR HOGENOM; CLU_095549_3_0_1; -.
DR InParanoid; Q6P828; -.
DR OMA; IAMQTVY; -.
DR OrthoDB; 1564782at2759; -.
DR PhylomeDB; Q6P828; -.
DR TreeFam; TF313294; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000024896; Expressed in egg cell and 17 other tissues.
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 GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
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..148
FT /note="Lipopolysaccharide-induced tumor necrosis factor-
FT alpha factor homolog"
FT /id="PRO_0000084445"
FT DOMAIN 63..147
FT /note="LITAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT REGION 101..123
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 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q99732"
SQ SEQUENCE 148 AA; 16273 MW; 9546452ACB4C6E19 CRC64;
MQTSGNYQPV PIGFTVPSAP PSYEEATFHH PPYPPLHQGM DAKNMSNPPY IVQPVPMQPP
VTVQTVYVQQ AMTLYDRPVQ MCCRSCNSMI TTRLEYSSGA LAWLSCGGLC LLGCIGGCCL
IPFCIDSLKD VDHYCPNCHA LLGSYKRI
