LITAF_CHICK
ID LITAF_CHICK Reviewed; 148 AA.
AC Q8QGW7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog;
DE Short=LPS-induced TNF-alpha factor homolog;
DE AltName: Full=Small integral membrane protein of lysosome/late endosome;
GN Name=LITAF; Synonyms=SIMPLE;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Thymus;
RA Moriwaki Y., Begum N.A., Kobayashi M., Matsumoto M., Seya T.;
RT "Molecular cloning and functional characterization of chicken SIMPLE, a
RT human SIMPLE ortholog.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lillehoj H.S., Min W., Ashwell C.M., Matukumalli L.K., van Tassel C.,
RA Han J.Y.;
RT "Gallus gallus TNF-alpha factor.";
RL Submitted (SEP-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; AB058634; BAB85678.1; -; mRNA.
DR EMBL; AB061737; BAC58022.1; -; Genomic_DNA.
DR EMBL; AY765397; AAU95774.1; -; mRNA.
DR RefSeq; NP_989598.1; NM_204267.1.
DR RefSeq; XP_015149605.1; XM_015294119.1.
DR RefSeq; XP_015149606.1; XM_015294120.1.
DR RefSeq; XP_015149607.1; XM_015294121.1.
DR RefSeq; XP_015149610.1; XM_015294124.1.
DR AlphaFoldDB; Q8QGW7; -.
DR STRING; 9031.ENSGALP00000005086; -.
DR PaxDb; Q8QGW7; -.
DR GeneID; 374125; -.
DR KEGG; gga:374125; -.
DR CTD; 9516; -.
DR VEuPathDB; HostDB:geneid_374125; -.
DR eggNOG; ENOG502S2GM; Eukaryota.
DR InParanoid; Q8QGW7; -.
DR OrthoDB; 1564782at2759; -.
DR PhylomeDB; Q8QGW7; -.
DR PRO; PR:Q8QGW7; -.
DR Proteomes; UP000000539; Unplaced.
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:0005765; C:lysosomal membrane; TAS:AgBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; NAS:AgBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0001816; P:cytokine production; TAS:AgBase.
DR GO; GO:0019953; P:sexual reproduction; TAS:AgBase.
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_0000084443"
FT DOMAIN 62..147
FT /note="LITAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01181"
FT REGION 35..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..123
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000305"
FT MOTIF 13..16
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; 16013 MW; BA4A52B60B7A59E8 CRC64;
MSAPSGFPAP SAPPSYEETV GINVNYPHPY PVPQPGLRPD GKGMNPPQYS GQPMPTSTPV
TVQTVYVQQP VVLFYDRPVQ MSCPSCNQMI VTRLCYESGA LTWLSCGGLF LLGCIAGCCL
IPFCVDALKD VEHFCPNCNA HVGSYKRL
