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CYTH2

From Wikipedia, the free encyclopedia

CYTH2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCYTH2, ARNO, CTS18, CTS18.1, PSCD2, PSCD2L, SEC7L, Sec7p-L, Sec7p-like, cytohesin 2, cytohesin-2
External IDsOMIM: 602488; MGI: 1334255; HomoloGene: 32116; GeneCards: CYTH2; OMA:CYTH2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004228
NM_017457

NM_001112701
NM_011181

RefSeq (protein)

NP_004219
NP_059431

NP_001106171
NP_035311

Location (UCSC)Chr 19: 48.47 – 48.48 MbChr 7: 45.46 – 45.46 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cytohesin-2 is a protein that in humans is encoded by the CYTH2 gene.[5][6][7]

Function

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Cytohesin-2 (CYTH2), formerly known as Pleckstrin homology, Sec7 and coiled/coil domains 2 (PSCD2), 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. CYTH2 exhibits GEP activity in vitro with ARF1, ARF3, and ARF6. CYTH2 protein is 83% homologous to CYTH1. Two transcript variants encoding different isoforms have been found for this gene.[7]

Interactions

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CYTH2 has been shown to interact with Arrestin beta 2[8] and Arrestin beta 1. [8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105443Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003269Ensembl, 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. ^ Kolanus W, Nagel W, Schiller B, Zeitlmann L, Godar S, Stockinger H, Seed B (Sep 1996). "Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule". Cell. 86 (2): 233–42. doi:10.1016/S0092-8674(00)80095-1. PMID 8706128. S2CID 18390795.
  6. ^ Chardin P, Paris S, Antonny B, Robineau S, Béraud-Dufour S, Jackson CL, Chabre M (1996). "A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains". Nature. 384 (6608): 481–4. Bibcode:1996Natur.384..481C. doi:10.1038/384481a0. PMID 8945478. S2CID 4361989.
  7. ^ a b "Entrez Gene: PSCD2 pleckstrin homology, Sec7 and coiled-coil domains 2 (cytohesin-2)".
  8. ^ a b Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ (Nov 2001). "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45): 42509–13. doi:10.1074/jbc.M108399200. PMID 11533043.

Further reading

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