CYTH1

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CYTH1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCYTH1, B2-1, CYTOHESIN-1, D17S811E, PSCD1, SEC7, cytohesin 1
External IDsOMIM: 182115 MGI: 1334257 HomoloGene: 31262 GeneCards: CYTH1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)Chr 17: 78.67 – 78.78 MbChr 11: 118.02 – 118.14 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cytohesin-1 formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 1 (PSCD1) is a protein that in humans is encoded by the CYTH1 gene.[5][6][7]

Function

Cytohesin-1 (CYTH1) is a member of the cytohesin family. Members of this family have identical structural organization that consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain. The coiled-coil motif is involved in homodimerization, the Sec7 domain contains guanine-nucleotide exchange protein (GEP) activity, and the PH domain interacts with phospholipids and is responsible for association of CYTHs with membranes. Members of this family appear to mediate the regulation of protein sorting and membrane trafficking. The CYTH1 is highly expressed in natural killer and peripheral T cells, and regulates the adhesiveness of integrins at the plasma membrane of lymphocytes. CYTH1 protein is 83% homologous to CYTH2.[7]

Interactions

CYTH1 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108669 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017132 - 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. ^ Liu L, Pohajdak B (September 1992). "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7". Biochim. Biophys. Acta. 1132 (1): 75–8. doi:10.1016/0167-4781(92)90055-5. PMID 1511013.
  6. ^ Dixon B, Mansour M, Pohajdak B (April 1993). "Assignment of human B2-1 gene (D17S811E) to chromosome 17qter by PCR analysis of somatic cell hybrids and fluorescence in situ hybridization". Cytogenet. Cell Genet. 63 (1): 42–4. doi:10.1159/000133498. PMID 8449036.
  7. ^ a b "Entrez Gene: PSCD1 pleckstrin homology, Sec7 and coiled-coil domains 1(cytohesin 1)".
  8. ^ Schürmann A, Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S, Massmann S, Schilf C, Subauste MC, Voss M, Jakobs KH, Joost HG (April 1999). "The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D". J. Biol. Chem. 274 (14): 9744–51. doi:10.1074/jbc.274.14.9744. PMID 10092663.
  9. ^ Rietzler M, Bittner M, Kolanus W, Schuster A, Holzmann B (October 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". J. Biol. Chem. 273 (42): 27459–66. doi:10.1074/jbc.273.42.27459. PMID 9765275.
  10. ^ Geiger C, Nagel W, Boehm T, van Kooyk Y, Figdor CG, Kremmer E, Hogg N, Zeitlmann L, Dierks H, Weber KS, Kolanus W (June 2000). "Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1". EMBO J. 19 (11): 2525–36. doi:10.1093/emboj/19.11.2525. PMC 212768. PMID 10835351.
  11. ^ Vitale N, Pacheco-Rodriguez G, Ferrans VJ, Riemenschneider W, Moss J, Vaughan M (July 2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem. 275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID 10748148.

Further reading