호모사피엔스 종의 단백질 코딩 유전자
GIPC1 식별자 별칭 GIPC1 , C19orf3, GIPC, GLUT1CBP, Hs.6454, IIP-1, NIP, RGS19IP1, SEMCAP, SYNECTIIN, SYNECTIN, TIP-2, GIPC PDZ domain containing family member 1, OPDM2외부 ID OMIM : 605072 MGI : 1926252 호몰로진 : 21167 GeneCard : GIPC1 직교체 종 인간 마우스 엔트레스 앙상블 유니프로트 RefSeq(mRNA) RefSeq(단백질) 위치(UCSC) Cr 19: 14.48 – 14.5Mb Chr 8: 84.38 – 84.39Mb PubMed 검색[3] [4] 위키다타
가족, 멤버 1 (GIPC1 )을 포함하는 GIPC PDZ 도메인 은 인간에서 GIPC1 유전자 에 의해 인코딩 되는 단백질이다.[5] [6] [7] GIPC는 원래 G단백질신호 조절에 관여하는 단백질인 RGS-GAIP의 C단말기에 특별히 결합하는 것으로 확인되었다.[5] GIPC는 "GAIP Interactiving 단백질 C-terminus"의 약자다. RGS 단백질은 'G단백신호 조절기'이고, RGS-GAIP는 'Gαi/Gαq용 GTPase 활성제 단백질'로, Gα 단백질의 두 가지 주요 아종이다. 인간 GIPC1 분자는 분자 크기의 아미노산 333개 또는 약 36kDa이며, 특정 단백질-단백질 상호작용을 매개하는 콤팩트 단백질 모듈인 중앙 PDZ 영역 으로 구성되어 있다. RGS-GAIP 단백질은 이 영역과 상호작용을 하며 많은 다른 단백질은 여기 또는 GIPC1 분자의 다른 부분에서 상호작용을 한다. 그 결과 GIPC1은 여러 다른 그룹에 의해 독립적으로 발견되었으며, 시넥틴, C19orf3, RGS19IP1 등을 포함한 다양한 대체 이름을 가지고 있다. 세 개의 멤버로 구성된 포유류에서 GIPC1 유전자 계열이 형성되어 있어 최초 발견되는 유전자 계열은 현재 일반적으로 GIPC1이라고 불리고 있으며, 나머지 두 종은 GIPC2와 GIPC3로 명명되었다.[8] 3개의 인간 단백질은 단백질 순서에서 약 60%가 동일하다. 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. 그러므로 GIPC 계열 단백질의 일반적인 기능은 G 단백질 신호 전달과 막 번역에 관여하는 단백질 사이의 특정한 상호작용을 매개하는 것으로 보인다.
상호작용 GIPC1은 다음과 상호 작용하는 것으로 나타났다.
액티닌, [9] 알파1 , ADRB1 ,[10] 글루트1 ,[9] ITGA5 ,[11] ITGA6 ,[11] KIF1B ,[9] LRP1 ,[12] LRP2 ,[12] [13] [14] LHCGR ,[15] MYO6 ,[16] [17] RGS19 ,[18] TPBG [19] 및 TYRP1 .[20] 참고 항목 패밀리가 포함된 GIPC PDZ 도메인, 멤버 2, GIPC2
패밀리가 포함된 GIPC PDZ 도메인, 멤버 3, GIPC3
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PMID 17353931 . ^ 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 . ^ 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 . ^ 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 . ^ 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. 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"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 . 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. 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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 .