| General information | | DisProt: | DP00435 | | Name: | Transitional endoplasmic reticulum ATPase | | Synonym(s): | TERA_MOUSE
TER ATPase
15S Mg(2+)-ATPase p97 subunit
Valosin-containing protein
VCP
| | First appeared in release: | Release 3.5 (12/22/2006) | | UniProt: | Q01853 | | UniGene: | Mm.245976 | | SwissProt: | TERA_MOUSE | | TrEMBL: | | | NCBI (GI): | 146291078 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 806 | | Percent disordered: | 3% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK - 60
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID - 120
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT - 180
VIHCEGEPIK REDEEESLNE VGYDDVGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG - 240
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI - 300
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF - 360
GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL - 420
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG - 480
GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI - 540
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV - 600
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRVAILKAN - 660
LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM - 720
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG - 780
AGPSQGSGGG TGGSVYTEDN DDDLYG
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| Functional narrative |
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.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | D1D2 linker | | Location: | 469 - 482 | | Length: | 14 | | Region sequence: |
VEVPQVTWEDIGGL | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises via an order to disorder transition
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (294 K; pH: 5; NaH2PO4 0.75 M; NH4F 50 mM; PEG 400 (w/v) 6 %; sodium citrate (buffer) 100 mM)
| References:
- DeLaBarre B, Brunger AT. "Nucleotide dependent motion and mechanism of action of p97/VCP." J Mol Biol. 2005; 347(2): 437-52. PubMed: 15740751
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 588 - 597 | | Length: | 10 | | Region sequence: |
GNIGDGGGAA | | Modification type: | | | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (294 K; pH: 5; NaH2PO4 0.75 M; NH4F 50 mM; PEG 400 (w/v) 6 %; sodium citrate (buffer) 100 mM)
| References:
- DeLaBarre B, Brunger AT. "Nucleotide dependent motion and mechanism of action of p97/VCP." J Mol Biol. 2005; 347(2): 437-52. PubMed: 15740751
| Comments:
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| References |
- Egerton M, Ashe OR, Chen D, Druker BJ, Burgess WH, Samelson LE. "VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation." EMBO J. 1992; 11(10): 3533-40. PubMed: 1382975
- Watts GD, Wymer J, Kovach MJ, Mehta SG, Mumm S, Darvish D, Pestronk A, Whyte MP, Kimonis VE. "Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein." Nat Genet. 2004; 36(4): 377-81. PubMed: 15034582
- 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. "Structure of the AAA ATPase p97." Mol Cell. 2000; 6(6): 1473-84. PubMed: 11163219
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| Comments |
D1/D2 domains allow the N-terminal domain to change conformational shape without a deleterious effect on its structure. Mutations with VCP (valosin-containing protein), which bind to the D1/D2 domains can give rise to Paget Disease or Frontotemporal dementia. Mutations in VCP negatively affect the conformational stability of the N-terminal domain and as a result give rise to improper ubiquitin binding (i.e., protein quality control) and affect similar proteins and their pathways (e.g., Huntington, Alzheimer, Creutzfeldt-Jakob, and Parkinson disease).
Additional UniGene ID: Mm.262053
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