STARD8 (original) (raw)

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Protein-coding gene in the species Homo sapiens

STARD8
Identifiers
Aliases STARD8, ARHGAP38, DLC3, STARTGAP3, StAR related lipid transfer domain containing 8
External IDs OMIM: 300689; MGI: 2448556; HomoloGene: 22837; GeneCards: STARD8; OMA:STARD8 - orthologs
Gene location (Human)X chromosome (human)Chr.X chromosome (human)[1]X chromosome (human)Genomic location for STARD8Genomic location for STARD8BandXq13.1Start68,647,666 bp[1]End68,725,842 bp[1]
Gene location (Mouse)X chromosome (mouse)Chr.X chromosome (mouse)[2]X chromosome (mouse)Genomic location for STARD8Genomic location for STARD8BandX|X C3Start98,046,854 bp[2]End98,118,334 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inright lungupper lobe of left lungapex of heartolfactory bulbhuman kidneytesticleleft ventricleright lobe of thyroid glandleft uterine tubeleft lobe of thyroid glandTop expressed instroma of bone marrowyolk sacright lung lobesciatic nerveleft lungextraocular muscledermisleft lung lobemyocardium of ventriclehuman kidneyMore reference expression dataBioGPSn/a
Gene ontologyMolecular function lipid binding GTPase activator activity Cellular component cytosol cell junction focal adhesion Biological process positive regulation of GTPase activity regulation of small GTPase mediated signal transduction signal transduction Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez9754236920EnsemblENSG00000130052ENSMUSG00000031216UniProtQ92502Q8K031RefSeq (mRNA)NM_001142503NM_001142504NM_014725NM_199018RefSeq (protein)NP_001135975NP_001135976NP_055540NP_950183Location (UCSC)Chr X: 68.65 – 68.73 MbChr X: 98.05 – 98.12 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

StAR-related lipid transfer domain protein 8 (STARD8) also known as deleted in liver cancer 3 protein (DLC-3) is a protein that in humans is encoded by the STARD8 gene[5][6] and is a member of the DLC family.

Structure and function

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The protein is 1103 amino acids long, which like other DLC proteins consists of a sterile alpha motif (SAM), RhoGAP and a StAR-related lipid-transfer (START) domains.[7]

The protein is a Rho GTPase-activating protein (GAP), a type of protein that regulates members of the Rho family of GTPases. STARD8 is characterized as activating Rho GTPases. Its expression inhibits the growth of human breast and prostate cancer cells in culture.[7]

Tissue distribution and pathology

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The protein is expressed in tissues throughout the body, but is absent or reduced in many kinds of tumor cells.[7]

While there are no known disorders caused by STARD8, partial loss of the STARD8 gene occurs in cases of craniofrontonasal syndrome where the EFNB1 gene (which causes the syndrome) is completely deleted.[8][9]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000130052 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031216 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: StAR-related lipid transfer (START) domain containing 8".
  6. ^ Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N (Feb 1996). "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 3 (1): 17–24. doi:10.1093/dnares/3.1.17. PMID 8724849.
  7. ^ a b c Durkin ME, Ullmannova V, Guan M, Popescu NC (Jul 2007). "Deleted in liver cancer 3 (DLC-3), a novel Rho GTPase-activating protein, is downregulated in cancer and inhibits tumor cell growth". Oncogene. 26 (31): 4580–9. doi:10.1038/sj.onc.1210244. PMID 17297465. S2CID 5867743.
  8. ^ Twigg SR, Matsumoto K, Kidd AM, Goriely A, Taylor IB, Fisher RB, Hoogeboom AJ, Mathijssen IM, Lourenco MT, Morton JE, Sweeney E, Wilson LC, Brunner HG, Mulliken JB, Wall SA, Wilkie AO (Jun 2006). "The origin of EFNB1 mutations in craniofrontonasal syndrome: frequent somatic mosaicism and explanation of the paucity of carrier males". American Journal of Human Genetics. 78 (6): 999–1010. doi:10.1086/504440. PMC 1474108. PMID 16685650.
  9. ^ Wieland I, Weidner C, Ciccone R, Lapi E, McDonald-McGinn D, Kress W, Jakubiczka S, Collmann H, Zuffardi O, Zackai E, Wieacker P (Dec 2007). "Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome". Clinical Genetics. 72 (6): 506–16. doi:10.1111/j.1399-0004.2007.00905.x. PMID 17941886. S2CID 33823266.