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TRANSPORTERS FROM HUMANS:
Transporter Information:
Name: solute carrier family 30 (zinc transporter), member 9
Symbol: SLC30A9
Locations: 4p12-p13
Aliases: HUEL, ZNT9
GenBank: AF006621
Accession Number: NM_006345
Old Name: chromosome 4 open reading frame 1
LocusLink10463
OMIM604604
PubMed (10409434): Sim DL, Chow VT. The novel human HUEL (C4orf1) gene maps to chromosome 4p12-p13 and encodes anuclear protein containing the nuclear receptor interaction motif.Genomics. 1999 Jul 15;59(2):224-33. PMID: 10409434 [PubMed - indexed for MEDLINE]

A 3250-bp novel human cDNA sequence was isolated from the MRC-5 human embryonic lung cell line by the rapid amplification of cDNA ends technique. This gene was designated HUEL and given the symbol C4orf1 by the HUGO Nomenclature Committee. Within HUEL was identified a continuous ORF of 1704 bp encoding a predicted hydrophilic protein of 568 amino acids with a calculated molecular mass of 63,410 Da. The putative protein contains the LXXLL signature motif considered necessary and sufficient for binding of certain coactivators to liganded nuclear receptors, as well as nuclear localization signals, a nuclear export-like signal, a zinc finger-like motif, an acidic region, and two leucine zipper-like domains. Northern blot analysis of human fetal tissues revealed 3. 4-kb transcripts, while RT-PCR demonstrated HUEL expression in a wide range of human adult tissues and cancer cell lines. In the SiHa, HT-1080, and G-401 cancer lines was detected an alternative transcript in which a 166-bp segment was excluded by exon skipping, which is predicted to culminate in a protein with a modified and truncated C-terminus. HUEL was localized to chromosome region 4p12-p13 by fluorescence in situ hybridization. In Western blots, affinity-purified antibodies raised against a HUEL-specific synthetic peptide could recognize a distinct protein band of approximately 70 kDa. Immunoblotting of subcellular fractions and indirect immunofluorescence of human embryonic lung cells demonstrated the distribution of HUEL predominantly in the cytoplasm, with an apparently cytoskeletal association. However, in smaller or dividing PLC/PRF/5 and TONG liver carcinoma cells, there was a translocation of HUEL from the cytoplasm to the nucleus. Taken together, these data suggest that HUEL plays a role in transcriptional regulation.

PubMed (11906820): Sim del LC, Yeo WM, Chow VT. The novel human HUEL (C4orf1) protein shares homology with the DNA-bindingdomain of the XPA DNA repair protein and displays nuclear translocation in acell cycle-dependent manner.Int J Biochem Cell Biol. 2002 May;34(5):487-504. PMID: 11906820 [PubMed - indexed for MEDLINE]

We have previously isolated and characterized a novel human gene HUEL (C4orf1) that is ubiquitously expressed in a wide range of human fetal, adult tissues and cancer cell lines. HUEL maps to region 4p12-p13 within the short arm of chromosome 4 whose deletion is frequently associated with bladder and other carcinomas. Here we present the genomic organization, sizes and boundaries of exons and introns of HUEL. The GC-rich upstream genomic region and 5' untranslated region (UTR) together constitute a CpG island, a hallmark of housekeeping genes. The 3250 bp HUEL cDNA incorporates a 1704 bp ORF that translates into a hydrophilic protein of 568-amino acids (aa), detected as a band of approximately 70 kDa by Western blotting. We have isolated the murine homolog of HUEL which exhibits 89% nucleotide and 94% amino acid identity to its human counterpart. The HUEL protein shares significant homology with the minimal DNA-binding domain (DNA-BD) of the DNA repair protein encoded by the xeroderma pigmentosum group A (XPA) gene. Other notable features within HUEL include the putative nuclear receptor interaction motif, nuclear localization and export signals, zinc finger, leucine zipper and acidic domains. Mimosine-mediated cell cycle synchronization of PLC/PRF/5 liver cancer cells clearly portrayed translocation of HUEL into the nucleus specifically during the S phase of the cell cycle. Yeast two-hybrid experiments revealed interactions of HUEL with two partner proteins (designated HIPC and HIPB) bearing similarity to a mitotically phosphorylated protein and to reverse transcriptase. Co-immunoprecipitation assays validated the interaction between HUEL and HIPC proteins in mammalian cells. HUEL is likely to be an evolutionarily conserved, housekeeping gene that plays a role intimately linked with cellular replication, DNA synthesis and/or transcriptional regulation.