CYTH3

Protein-coding gene in the species Homo sapiens
CYTH3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4KAX

Identifiers
AliasesCYTH3, ARNO3, GRP1, PSCD3, cytohesin 3, cytohesin-3
External IDsOMIM: 605081; MGI: 1335107; HomoloGene: 3116; GeneCards: CYTH3; OMA:CYTH3 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for CYTH3
Genomic location for CYTH3
Band7p22.1Start6,161,776 bp[1]
End6,272,644 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for CYTH3
Genomic location for CYTH3
Band5 G2|5 82.36 cMStart143,608,202 bp[2]
End143,696,005 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • visceral pleura

  • parietal pleura

  • middle temporal gyrus

  • Brodmann area 23

  • spinal ganglia

  • trigeminal ganglion

  • saphenous vein

  • tendon of biceps brachii

  • tibia
Top expressed in
  • superior cervical ganglion

  • right lung

  • carotid body

  • right lung lobe

  • barrel cortex

  • iris

  • left lung

  • ciliary body

  • endothelial cell of lymphatic vessel

  • fetal liver hematopoietic progenitor cell
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • phosphatidylinositol-3,4,5-trisphosphate binding
  • guanyl-nucleotide exchange factor activity
  • lipid binding
Cellular component
  • cytoplasm
  • ruffle
  • extrinsic component of cytoplasmic side of plasma membrane
  • plasma membrane
  • membrane
  • Golgi membrane
  • cytosol
  • nucleoplasm
  • adherens junction
  • bicellular tight junction
  • cell junction
Biological process
  • regulation of ARF protein signal transduction
  • Golgi vesicle transport
  • positive regulation of cell adhesion
  • establishment of epithelial cell polarity
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9265

19159

Ensembl

ENSG00000008256

ENSMUSG00000018001

UniProt

O43739

O08967

RefSeq (mRNA)

NM_004227

NM_001163548
NM_011182

RefSeq (protein)

NP_004218
NP_001354509
NP_001354510
NP_001354511

NP_001157020
NP_035312

Location (UCSC)Chr 7: 6.16 – 6.27 MbChr 5: 143.61 – 143.7 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cytohesin-3 is a protein that in humans is encoded by the CYTH3 gene.[5][6]

This gene encodes a member of the cytohesin (CYTH) family, formerly known as the PSCD (pleckstrin homology, Sec7 and coiled-coil domains) family. Cytohesin family members 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. This encoded protein is involved in the control of Golgi structure and function, and it may have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000008256 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018001 – 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. ^ Klarlund JK, Guilherme A, Holik JJ, Virbasius JV, Chawla A, Czech MP (Apr 1997). "Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains". Science. 275 (5308): 1927–30. doi:10.1126/science.275.5308.1927. PMID 9072969. S2CID 40523716.
  6. ^ a b "Entrez Gene: PSCD3 pleckstrin homology, Sec7 and coiled-coil domains 3".

Further reading

  • Franco M, Boretto J, Robineau S, et al. (1998). "ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP ribosylation factor 1, is involved in the control of Golgi structure and function". Proc. Natl. Acad. Sci. U.S.A. 95 (17): 9926–31. Bibcode:1998PNAS...95.9926F. doi:10.1073/pnas.95.17.9926. PMC 21438. PMID 9707577.
  • Venkateswarlu K, Gunn-Moore F, Oatey PB, et al. (1998). "Nerve growth factor- and epidermal growth factor-stimulated translocation of the ADP-ribosylation factor-exchange factor GRP1 to the plasma membrane of PC12 cells requires activation of phosphatidylinositol 3-kinase and the GRP1 pleckstrin homology domain". Biochem. J. 335 ( Pt 1) (Pt 1): 139–46. doi:10.1042/bj3350139. PMC 1219762. PMID 9742223.
  • Ogasawara M, Kim SC, Adamik R, et al. (2000). "Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors". J. Biol. Chem. 275 (5): 3221–30. doi:10.1074/jbc.275.5.3221. PMID 10652308.
  • Nevrivy DJ, Peterson VJ, Avram D, et al. (2000). "Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors". J. Biol. Chem. 275 (22): 16827–36. doi:10.1074/jbc.275.22.16827. PMID 10828067.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human Chromosome 7: DNA Sequence and Biology". Science. 300 (5620): 767–72. Bibcode:2003Sci...300..767S. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205.
  • Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Poirier MB, Hamann G, Domingue ME, et al. (2005). "General receptor for phosphoinositides 1, a novel repressor of thyroid hormone receptor action that prevents deoxyribonucleic acid binding". Mol. Endocrinol. 19 (8): 1991–2005. doi:10.1210/me.2004-0449. PMID 15878955.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • v
  • t
  • e
  • 1bc9: CYTOHESIN-1/B2-1 SEC7 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
    1bc9: CYTOHESIN-1/B2-1 SEC7 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
  • 1fgy: GRP1 PH DOMAIN WITH INS(1,3,4,5)P4
    1fgy: GRP1 PH DOMAIN WITH INS(1,3,4,5)P4
  • 1fgz: GRP1 PH DOMAIN (UNLIGANDED)
    1fgz: GRP1 PH DOMAIN (UNLIGANDED)
  • 1fhw: Structure of the pleckstrin homology domain from GRP1 in complex with inositol(1,3,4,5,6)pentakisphosphate
    1fhw: Structure of the pleckstrin homology domain from GRP1 in complex with inositol(1,3,4,5,6)pentakisphosphate
  • 1fhx: Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate
    1fhx: Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate
  • 1u2b: Triglycine variant of the Grp1 Pleckstrin Homology Domain unliganded
    1u2b: Triglycine variant of the Grp1 Pleckstrin Homology Domain unliganded


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