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P46462 (TERA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transitional endoplasmic reticulum ATPase

Short name=TER ATPase
EC=3.6.4.6
Alternative name(s):
15S Mg(2+)-ATPase p97 subunit
Valosin-containing protein
Short name=VCP
Gene names
Name:Vcp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage By similarity. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Ref.6 Ref.8

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis. Interacts with RHBDD1 (via C-terminal domain) By similarity. Interacts with VIMP/SELS and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Interacts with SVIP. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXD2 and RNF19A. Interacts with CASR. Interacts with UBXN6, UBE4B and YOD1. Interacts with clathrin. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with SPRTN; leading to recruitment to stalled replication forks By similarity. 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. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP. Interacts with KIAA0196 By similarity. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasmcytosol. Nucleus. Endoplasmic reticulum By similarity. Note: Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMFR/gp78. Following DNA double-strand breaks, recruited to the sites of damage. Recruited to stalled replication forks via interaction with SPRTN By similarity. Ref.5

Post-translational modification

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. Phosphorylated in mitotic cells. Ref.10

ISGylated By similarity.

Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity By similarity.

Sequence similarities

Belongs to the AAA ATPase family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transport
   Cellular componentCytoplasm
Endoplasmic reticulum
Nucleus
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.1. Source: GOC

ER to Golgi vesicle-mediated transport

Inferred from mutant phenotype Ref.1. Source: RGD

ER-associated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

aggresome assembly

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 16103111. Source: RGD

positive regulation of protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein N-linked glycosylation via asparagine

Inferred from sequence or structural similarity. Source: UniProtKB

protein hexamerization

Inferred from direct assay PubMed 18332143. Source: RGD

protein homooligomerization

Inferred from direct assay Ref.1. Source: RGD

protein ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

retrograde protein transport, ER to cytosol

Inferred from electronic annotation. Source: Ensembl

translesion synthesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay PubMed 23444373. Source: MGI

endoplasmic reticulum

Inferred from direct assay Ref.1. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay Ref.1. Source: RGD

lipid particle

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome complex

Inferred from electronic annotation. Source: Ensembl

site of double-strand break

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionADP binding

Inferred from mutant phenotype PubMed 18332143. Source: RGD

ATP binding

Inferred from direct assay Ref.1. Source: BHF-UCL

ATPase activity

Inferred from direct assay Ref.1. Source: RGD

identical protein binding

Inferred from direct assay Ref.1. Source: BHF-UCL

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16601695PubMed 20691684PubMed 9214505. Source: IntAct

protein complex binding

Inferred from physical interaction Ref.5. Source: RGD

receptor binding

Inferred from direct assay PubMed 16103111. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Nsfl1cO3598710EBI-399011,EBI-1993760

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 806805Transitional endoplasmic reticulum ATPase
PRO_0000084575

Regions

Nucleotide binding247 – 2537ATP By similarity
Region797 – 80610Interaction with UBXN6 By similarity

Sites

Binding site3481ATP By similarity
Binding site3841ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue31Phosphoserine By similarity
Modified residue371Phosphoserine By similarity
Modified residue3151N6,N6,N6-trimethyllysine; by VCPKMT By similarity
Modified residue4361Phosphothreonine By similarity
Modified residue5021N6-acetyllysine By similarity
Modified residue5051N6-acetyllysine By similarity
Modified residue6681N6-acetyllysine; alternate By similarity
Modified residue6681N6-succinyllysine; alternate By similarity
Modified residue7541N6-acetyllysine By similarity
Modified residue7701Phosphoserine By similarity
Modified residue7751Phosphoserine By similarity
Modified residue7871Phosphoserine By similarity
Modified residue8051Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P46462 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 501B721D205EBA8A

FASTA80689,349
        10         20         30         40         50         60 
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK 

        70         80         90        100        110        120 
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID 

       130        140        150        160        170        180 
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT 

       190        200        210        220        230        240 
VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG 

       250        260        270        280        290        300 
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI 

       310        320        330        340        350        360 
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF 

       370        380        390        400        410        420 
GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL 

       430        440        450        460        470        480 
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG 

       490        500        510        520        530        540 
GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI 

       550        560        570        580        590        600 
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 

       610        620        630        640        650        660 
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRVAILKAN 

       670        680        690        700        710        720 
LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM 

       730        740        750        760        770        780 
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG 

       790        800 
AGPSQGSGGG TGGNVYTEDN DDDLYG 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver."
Zhang L., Ashendel C.L., Becker G.W., Morre D.J.
J. Cell Biol. 127:1871-1883(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]Lubec G., Diao W.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 46-53; 149-155; 192-210; 218-225; 240-251; 296-312; 366-386; 454-465; 616-638; 669-677 AND 701-709, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]"Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro."
Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G.
Cell 92:603-610(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STX5A.
[5]"A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways."
Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.
EMBO J. 19:2181-2192(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPLOC4; UFD1L; NSFL1C AND UBE4B, SUBCELLULAR LOCATION.
[6]"Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic reticulum."
Roy L., Bergeron J.J.M., Lavoie C., Hendriks R., Gushue J., Fazel A., Pelletier A., Morre D.J., Subramaniam V.N., Hong W., Paiement J.
Mol. Biol. Cell 11:2529-2542(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Phospholipid species act as modulators in p97/p47-mediated fusion of Golgi membranes."
Pecheur E.-I., Martin I., Maier O., Bakowsky U., Ruysschaert J.-M., Hoekstra D.
Biochemistry 41:9813-9823(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEMBRANES.
[8]"Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4."
Meyer H.H., Wang Y., Warren G.
EMBO J. 21:5645-5652(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NSFL1C; NAP1L4 AND UFD1L.
[9]"VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo."
Uchiyama K., Jokitalo E., Kano F., Murata M., Zhang X., Canas B., Newman R., Rabouille C., Pappin D., Freemont P., Kondo H.
J. Cell Biol. 159:855-866(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VCIP135.
[10]"The localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycle."
Uchiyama K., Jokitalo E., Lindman M., Jackman M., Kano F., Murata M., Zhang X., Kondo H.
J. Cell Biol. 161:1067-1079(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U11760 mRNA. Translation: AAC52154.1.
BC060518 mRNA. Translation: AAH60518.1.
PIRA55190.
RefSeqNP_446316.1. NM_053864.2.
UniGeneRn.98891.

3D structure databases

ProteinModelPortalP46462.
SMRP46462. Positions 18-763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250528. 19 interactions.
IntActP46462. 7 interactions.
MINTMINT-1954391.
STRING10116.ENSRNOP00000040121.

PTM databases

PhosphoSiteP46462.

2D gel databases

World-2DPAGE0004:P46462.

Proteomic databases

PaxDbP46462.
PRIDEP46462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000046102; ENSRNOP00000040121; ENSRNOG00000034242.
GeneID116643.
KEGGrno:116643.
UCSCRGD:621595. rat.

Organism-specific databases

CTD7415.
RGD621595. Vcp.

Phylogenomic databases

eggNOGCOG0464.
GeneTreeENSGT00740000115575.
HOGENOMHOG000223224.
HOVERGENHBG001226.
InParanoidP46462.
KOK13525.
OMAHKKVNLT.
OrthoDBEOG7H4DSW.
PhylomeDBP46462.
TreeFamTF300542.

Gene expression databases

GenevestigatorP46462.

Family and domain databases

Gene3D3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR005938. AAA_ATPase_CDC48.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
TIGRFAMsTIGR01243. CDC48. 1 hit.
PROSITEPS00674. AAA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio619375.
PROP46462.

Entry information

Entry nameTERA_RAT
AccessionPrimary (citable) accession number: P46462
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families