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Vcp |
Protein FULL name:
valosin containing protein [Mus musculus].
Vcp (Mus musculus) is product of expression of Vcp gene.
FUNCTION: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A (By similarity).
SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Part of a ternary complex containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer. The complex binds to membranes enriched in phosphatidylethanolamine-containing lipids and promotes Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1L, binding to this heterodimer inhibits Golgi- membrane fusion. Interaction with VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP. Part of a ternary complex containing NPLOC4, UFD1L and VCP (By similarity). Interacts with SELS/VIMP and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Interacts with SVIP (By similarity). Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXD2. Interacts with CASR (By similarity). Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis. Interacts with UBXN6, UBE4B and YOD1. Interacts with clathrin (By similarity). Interacts with RNF103 (By similarity). Interacts with TRIM13 (By similarity).
INTERACTION: Q9CVD2:Atxn3; NbExp=1; IntAct=EBI-80597, EBI-1784669; Q9BQE4:SELS (xeno); NbExp=3; IntAct=EBI-80597, EBI-398970; Q9ES00:Ube4b; NbExp=1; IntAct=EBI-80597, EBI-80579;
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
DOMAIN: The N-terminal domain shows evolutionary conservation with that of PEX1, and is able to bind phospholipids with a preference for phosphatidylinositol mono- and biphosphates.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity). Phosphorylated by tyrosine kinases in response to T- cell antigen receptor activation.
SIMILARITY: Belongs to the AAA ATPase family.
| NCBI GenPept GI number(s): |
30023842 |
| Species: | Mus musculus |
Links to other databases:
| Database | ID | Link |
| Uniprot | Q01853 |
Q01853 |
| PFAM: | - |
Q01853 (Link - using uniprot id) |
| InterPro: | - |
Q01853 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQ LFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVI SIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGD IFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNE VGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTG KTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAI IFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRP NSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVA NETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMD DFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHP DKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTM WFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRV INQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDE KSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSVADLTEICQRACKLAIR ESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDN DIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDN DDDLYG |
Vcp (Mus musculus) is able to recognize following damages:
Vcp (Mus musculus) belongs to following protein families:
References:
| Title | Authors | Journal |
| VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. | Egerton M, Ashe OR, Chen D, Druker BJ, Burgess WH, Samelson LE | EMBO J Oct. 1, 1992 |
| Structure of the AAA ATPase p97. | Zhang X, Shaw A, Bates PA, Newman RH, Gowen B, Orlova E, Gorman MA, Kondo H, Dokurno P, Lally J, Leonard G, Meyer H, van Heel M, Freemont PS | Mol Cell Dec. 1, 2000 |
| Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. | DeLaBarre B, Brunger AT | Nat Struct Biol Oct. 1, 2003 |
| The crystal structure of murine p97/VCP at 3.6A. | Huyton T, Pye VE, Briggs LC, Flynn TC, Beuron F, Kondo H, Ma J, Zhang X, Freemont PS | J Struct Biol Dec. 1, 2003 |
| Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47. | Dreveny I, Kondo H, Uchiyama K, Shaw A, Zhang X, Freemont PS | EMBO J March 10, 2004 |
| The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). | Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J | Genome Res Oct. 1, 2004 |
| Physical and functional interaction between Dorfin and Valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders. | Ishigaki S, Hishikawa N, Niwa J, Iemura S, Natsume T, Hori S, Kakizuka A, Tanaka K, Sobue G | J Biol Chem Dec. 3, 2004 |
| Nucleotide dependent motion and mechanism of action of p97/VCP. | DeLaBarre B, Brunger AT | J Mol Biol March 25, 2005 |
| The transcriptional landscape of the mammalian genome. | Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, Hirokawa N, Hill D, Huminiecki L, Iacono M, Ikeo K, Iwama A, Ishikawa T, Jakt M, Kanapin A, Katoh M, Kawasawa Y, Kelso J, Kitamura H, Kitano H, Kollias G, Krishnan SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, Lazarevic D, Lipovich L, Liu J, Liuni S, McWilliam S, Madan Babu M, Madera M, Marchionni L, Matsuda H, Matsuzawa S, Miki H, Mignone F, Miyake S, Morris K, Mottagui-Tabar S, Mulder N, Nakano N, Nakauchi H, Ng P, Nilsson R, Nishiguchi S, Nishikawa S, Nori F, Ohara O, Okazaki Y, Orlando V, Pang KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schonbach C, Sekiguchi K, Semple CA, Seno S, Sessa L, Sheng Y, Shibata Y, Shimada H, Shimada K, Silva D, Sinclair B, Sperling S, Stupka E, Sugiura K, Sultana R, Takenaka Y, Taki K, Tammoja K, Tan SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, Kai C, Sasaki D, Tomaru Y, Fukuda S, Kanamori-Katayama M, Suzuki M, Aoki J, Arakawa T, Iida J, Imamura K, Itoh M, Kato T, Kawaji H, Kawagashira N, Kawashima T, Kojima M, Kondo S, Konno H, Nakano K, Ninomiya N, Nishio T, Okada M, Plessy C, Shibata K, Shiraki T, Suzuki S, Tagami M, Waki K, Watahiki A, Okamura-Oho Y, Suzuki H, Kawai J, Hayashizaki Y | Science Sept. 2, 2005 |
| Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome. | Li G, Zhou X, Zhao G, Schindelin H, Lennarz WJ | Proc Natl Acad Sci U S A Nov. 1, 2005 |
| The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor. | Li G, Zhao G, Zhou X, Schindelin H, Lennarz WJ | Proc Natl Acad Sci U S A May 1, 2006 |
| The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97. | Shiozawa K, Goda N, Shimizu T, Mizuguchi K, Kondo N, Shimozawa N, Shirakawa M, Hiroaki H | FEBS J Nov. 1, 2006 |
| p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase and at the end of mitosis. | Uchiyama K, Totsukawa G, Puhka M, Kaneko Y, Jokitalo E, Dreveny I, Beuron F, Zhang X, Freemont P, Kondo H | Dev Cell Dec. 1, 2006 |
| Large-scale phosphorylation analysis of mouse liver. | Villen J, Beausoleil SA, Gerber SA, Gygi SP | Proc Natl Acad Sci U S A Feb. 1, 2007 |
| Lineage-specific biology revealed by a finished genome assembly of the mouse. | Church DM, Goodstadt L, Hillier LW, Zody MC, Goldstein S, She X, Bult CJ, Agarwala R, Cherry JL, DiCuccio M, Hlavina W, Kapustin Y, Meric P, Maglott D, Birtle Z, Marques AC, Graves T, Zhou S, Teague B, Potamousis K, Churas C, Place M, Herschleb J, Runnheim R, Forrest D, Amos-Landgraf J, Schwartz DC, Cheng Z, Lindblad-Toh K, Eichler EE, Ponting CP | PLoS Biol May 5, 2009 |
Last modification of this entry: Oct. 6, 2010.
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