GIPC1

GIPC1
Identifiers
Aliases	GIPC1 , C19orf3, GIPC, GLUT1CBP, Hs.6454, IIP-1, NIP, RGS19IP1, SEMCAP, SYNECTIIN, SYNECTIN, TIP-2, GIPC PDZ domain containing family member 1, OPDM2
External IDs	OMIM: 605072; MGI: 1926252; HomoloGene: 21167; GeneCards: GIPC1; OMA:GIPC1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) [1] Band 19p13.12 Start 14,477,760 bp [1] End 14,496,149 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8|8 C2 Start 84,379,306 bp [2] End 84,391,323 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon skin of leg skin of abdomen C1 segment mucosa of pharynx apex of heart putamen minor salivary glands right frontal lobe nucleus accumbens Top expressed in lip corneal stroma superior surface of tongue ventricular zone lens neural tube perirhinal cortex superior frontal gyrus yolk sac entorhinal cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding PDZ domain binding signaling receptor binding protein homodimerization activity myosin binding actin binding cadherin binding Cellular component cell cortex brush border endocytic vesicle extracellular exosome cytoplasm cytosol membrane synaptic vesicle vesicle membrane dendritic spine dendritic shaft cytoplasmic vesicle Schaffer collateral - CA1 synapse presynapse postsynapse glutamatergic synapse Biological process G protein-coupled receptor signaling pathway positive regulation of cytokinesis protein targeting positive regulation of transforming growth factor beta receptor signaling pathway regulation of protein stability regulation of synaptic plasticity glutamate secretion negative regulation of proteasomal ubiquitin-dependent protein catabolic process endothelial cell migration chemical synaptic transmission positive regulation of melanin biosynthetic process cellular response to interleukin-7 regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10755 67903 Ensembl ENSG00000123159 ENSMUSG00000019433 UniProt O14908 Q9Z0G0 RefSeq (mRNA) NM_005716 NM_202467 NM_202468 NM_202469 NM_202470 NM_202494 NM_018771 RefSeq (protein) NP_005707 NP_974197 NP_974198 NP_974199 NP_974223 NP_061241 Location (UCSC) Chr 19: 14.48 – 14.5 Mb Chr 8: 84.38 – 84.39 Mb PubMed search [3] [4]
Wikidata
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GIPC PDZ domain containing family, member 1 (GIPC1) is a protein that in humans is encoded by the GIPC1 gene. ^{[5] [6] [7]} GIPC was originally identified as it binds specifically to the C terminus of RGS-GAIP, a protein involved in the regulation of G protein signaling. ^[5] GIPC is an acronym for "GAIP Interacting Protein C-terminus". RGS proteins are "Regulators of G protein Signaling" and RGS-GAIP is a "GTPase Activator protein for Gαi/Gαq", which are two major subtypes of Gα proteins. The human GIPC1 molecule is 333 amino acids or about 36 kDa in molecular size and consists of a central PDZ domain, a compact protein module which mediates specific protein-protein interactions. The RGS-GAIP protein interacts with this domain and many other proteins interact here or at other parts of the GIPC1 molecule. As a result, GIPC1 was independently discovered by several other groups and has a variety of alternate names, including synectin, C19orf3, RGS19IP1 and others. The GIPC1 gene family in mammals consisting of three members, so the first discovered, originally named GIPC, is now generally called GIPC1, with the other two being named GIPC2 and GIPC3. ^[8] The three human proteins are about 60% identical in protein sequence. GIPC1 has been shown to interact with a variety of other receptor and cytoskeletal proteins including the GLUT1 receptor, ACTN1, KIF1B, MYO6, PLEKHG5, SDC4/syndecan-4, SEMA4C/semaphorin-4 and HTLV-I Tax. The general function of GIPC family proteins therefore appears to be mediating specific interactions between proteins involved in G protein signaling and membrane translocation.

Interactions

GIPC1 has been shown to interact with:

• Actinin, alpha 1, ^[9]
• ADRB1, ^[10]
• GLUT1, ^[9]
• ITGA5, ^[11]
• ITGA6, ^[11]
• KIF1B, ^[9]
• LRP1, ^[12]
• LRP2, ^{[12] [13] [14]}
• LHCGR, ^[15]
• MYO6, ^{[16] [17]}
• RGS19, ^[18]
• TPBG, ^[19] and
• TYRP1. ^[20]

See also

GIPC PDZ domain containing family, member 2, GIPC2

GIPC PDZ domain containing family, member 3, GIPC3

References

1. GRCh38: Ensembl release 89: ENSG00000123159 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000019433 – 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. De Vries L, Lou X, Zhao G, Zheng B, Farquhar MG (November 1998). "GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12340–5. Bibcode:1998PNAS...9512340D. doi: 10.1073/pnas.95.21.12340 . PMC   22833 . PMID   9770488.
6. Rousset R, Fabre S, Desbois C, Bantignies F, Jalinot P (March 1998). "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins". Oncogene. 16 (5): 643–54. doi: 10.1038/sj.onc.1201567 . PMID   9482110.
7. "Entrez Gene: GIPC1 GIPC PDZ domain containing family, member 1".
8. Katoh M (2002). "GIPC gene family (Review)". Int. J. Mol. Med. 9 (6): 585–9. doi:10.3892/ijmm.9.6.585. PMID   12011974.
9. Bunn RC, Jensen MA, Reed BC (April 1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell. 10 (4): 819–32. doi:10.1091/mbc.10.4.819. PMC   25204 . PMID   10198040.
10. Hu LA, Chen W, Martin NP, Whalen EJ, Premont RT, Lefkowitz RJ (July 2003). "GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation". J. Biol. Chem. 278 (28): 26295–301. doi: 10.1074/jbc.M212352200 . PMID   12724327.
11. Tani TT, Mercurio AM (September 2001). "PDZ interaction sites in integrin alpha subunits. T14853, TIP/GIPC binds to a type I recognition sequence in alpha 6A/alpha 5 and a novel sequence in alpha 6B". J. Biol. Chem. 276 (39): 36535–42. doi: 10.1074/jbc.M105785200 . PMID   11479315.
12. Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (August 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi: 10.1074/jbc.M000955200 . PMID   10827173.
13. Petersen HH, Hilpert J, Militz D, Zandler V, Jacobsen C, Roebroek AJ, Willnow TE (February 2003). "Functional interaction of megalin with the megalinbinding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule". J. Cell Sci. 116 (Pt 3): 453–61. doi: 10.1242/jcs.00243 . PMID   12508107.
14. Lou X, McQuistan T, Orlando RA, Farquhar MG (April 2002). "GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function". J. Am. Soc. Nephrol. 13 (4): 918–27. doi: 10.1681/ASN.V134918 . PMID   11912251.
15. Hirakawa T, Galet C, Kishi M, Ascoli M (December 2003). "GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR". J. Biol. Chem. 278 (49): 49348–57. doi: 10.1074/jbc.M306557200 . PMID   14507927.
16. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.
17. Aschenbrenner L, Lee T, Hasson T (July 2003). "Myo6 facilitates the translocation of endocytic vesicles from cell peripheries". Mol. Biol. Cell. 14 (7): 2728–43. doi:10.1091/mbc.E02-11-0767. PMC   165672 . PMID   12857860.
18. Lou X, Yano H, Lee F, Chao MV, Farquhar MG (March 2001). "GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways". Mol. Biol. Cell. 12 (3): 615–27. doi:10.1091/mbc.12.3.615. PMC   30968 . PMID   11251075.
19. Awan A, Lucic MR, Shaw DM, Sheppard F, Westwater C, Lyons SA, Stern PL (January 2002). "5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis". Biochem. Biophys. Res. Commun. 290 (3): 1030–6. doi:10.1006/bbrc.2001.6288. PMID   11798178.
20. Liu TF, Kandala G, Setaluri V (September 2001). "PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1)". J. Biol. Chem. 276 (38): 35768–77. doi: 10.1074/jbc.M103585200 . PMID   11441007.

Further reading

• Katoh M (2002). "GIPC gene family (Review)". Int. J. Mol. Med. 9 (6): 585–9. doi:10.3892/ijmm.9.6.585. PMID   12011974.
• Hasson T (2003). "Myosin VI: two distinct roles in endocytosis". J. Cell Sci. 116 (Pt 17): 3453–61. doi: 10.1242/jcs.00669 . PMID   12893809.
• Gress TM, Müller-Pillasch F, Geng M, Zimmerhackl F, Zehetner G, Friess H, Büchler M, Adler G, Lehrach H (1996). "A pancreatic cancer-specific expression profile". Oncogene. 13 (8): 1819–30. PMID   8895530.
• De Vries L, Elenko E, Hubler L, Jones TL, Farquhar MG (1996). "GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits". Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15203–8. Bibcode:1996PNAS...9315203D. doi: 10.1073/pnas.93.26.15203 . PMC   26381 . PMID   8986788.
• Bunn RC, Jensen MA, Reed BC (1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell. 10 (4): 819–32. doi:10.1091/mbc.10.4.819. PMC   25204 . PMID   10198040.
• Wang LH, Kalb RG, Strittmatter SM (1999). "A PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemF". J. Biol. Chem. 274 (20): 14137–46. doi: 10.1074/jbc.274.20.14137 . PMID   10318831.
• Cai H, Reed RR (1999). "Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1". J. Neurosci. 19 (15): 6519–27. doi: 10.1523/JNEUROSCI.19-15-06519.1999 . PMC   6782790 . PMID   10414980.
• Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi: 10.1074/jbc.M000955200 . PMID   10827173.
• Gao Y, Li M, Chen W, Simons M (2000). "Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration". J. Cell. Physiol. 184 (3): 373–9. doi:10.1002/1097-4652(200009)184:3<373::AID-JCP12>3.0.CO;2-I. PMID   10911369. S2CID   20829740.
• Von Kap-Herr C, Kandala G, Mann SS, Hart TC, Pettenati MJ, Setaluri V (2000). "Assignment of PDZ domain-containing protein GIPC gene (C19orf3) to human chromosome band 19p13.1 by in situ hybridization and radiation hybrid mapping". Cytogenet. Cell Genet. 89 (3–4): 234–5. doi:10.1159/000015621. PMID   10965131. S2CID   85292825.
• Lou X, Yano H, Lee F, Chao MV, Farquhar MG (2001). "GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways". Mol. Biol. Cell. 12 (3): 615–27. doi:10.1091/mbc.12.3.615. PMC   30968 . PMID   11251075.
• Liu TF, Kandala G, Setaluri V (2001). "PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1)". J. Biol. Chem. 276 (38): 35768–77. doi: 10.1074/jbc.M103585200 . PMID   11441007.
• Ligensa T, Krauss S, Demuth D, Schumacher R, Camonis J, Jaques G, Weidner KM (2001). "A PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptor". J. Biol. Chem. 276 (36): 33419–27. doi: 10.1074/jbc.M104509200 . PMID   11445579.
• Tani TT, Mercurio AM (2001). "PDZ interaction sites in integrin alpha subunits. T14853, TIP/GIPC binds to a type I recognition sequence in alpha 6A/alpha 5 and a novel sequence in alpha 6B". J. Biol. Chem. 276 (39): 36535–42. doi: 10.1074/jbc.M105785200 . PMID   11479315.
• Blobe GC, Liu X, Fang SJ, How T, Lodish HF (2001). "A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC". J. Biol. Chem. 276 (43): 39608–17. doi: 10.1074/jbc.M106831200 . PMID   11546783.
• Awan A, Lucic MR, Shaw DM, Sheppard F, Westwater C, Lyons SA, Stern PL (2002). "5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis". Biochem. Biophys. Res. Commun. 290 (3): 1030–6. doi:10.1006/bbrc.2001.6288. PMID   11798178.
• El Mourabit H, Poinat P, Koster J, Sondermann H, Wixler V, Wegener E, Laplantine E, Geerts D, Georges-Labouesse E, Sonnenberg A, Aumailley M (2002). "The PDZ domain of TIP-2/GIPC interacts with the C-terminus of the integrin alpha5 and alpha6 subunits". Matrix Biol. 21 (2): 207–14. doi:10.1016/S0945-053X(01)00198-6. PMID   11852236.
• Lou X, McQuistan T, Orlando RA, Farquhar MG (2002). "GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function". J. Am. Soc. Nephrol. 13 (4): 918–27. doi: 10.1681/ASN.V134918 . PMID   11912251.