CYTH4

Cytohesin-4 is a protein that in humans is encoded by the CYTH4 gene.^[5][6]

CYTH4
Identifiers
Aliases	CYTH4, CYT4, DJ63G5.1, PSCD4, cytohesin 4, cytohesin-4
External IDs	OMIM: 606514; MGI: 2441702; HomoloGene: 22750; GeneCards: CYTH4; OMA:CYTH4 - orthologs
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q13.1 Start 37,282,027 bp[1] End 37,315,341 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 E1 Start 78,597,047 bp[2] End 78,622,019 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte monocyte blood spleen appendix lymph node periodontal fiber bone marrow cells gallbladder right coronary artery Top expressed in granulocyte mesenteric lymph nodes stroma of bone marrow spleen subcutaneous adipose tissue blood superior frontal gyrus thymus dentate gyrus of hippocampal formation granule cell body of femur More reference expression data BioGPS More reference expression data
Gene ontology Molecular function guanyl-nucleotide exchange factor activity lipid binding Cellular component plasma membrane membrane Golgi membrane cytosol Biological process regulation of ARF protein signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27128 72318 Ensembl ENSG00000100055 ENSMUSG00000018008 UniProt Q9UIA0 Q80YW0 RefSeq (mRNA) NM_013385 NM_001318024 NM_028195 RefSeq (protein) NP_001304953 NP_037517 NP_082471 Location (UCSC) Chr 22: 37.28 – 37.32 Mb Chr 15: 78.6 – 78.62 Mb PubMed search [3] [4]
Wikidata
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This gene encodes a member of the cytohesin (CYTH) family, formerly known as the PSCD (pleckstrin homology, Sec7 and coiled-coil domains) 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. CYTH4 exhibits GEP activity in vitro with both ARF1 and ARF5 but is inactive with ARF6. The CYTH4 and CYTH1 gene structures are very similar.^[6]