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Q3ZBT1 (TERA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. 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·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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

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

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. 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. Interacts with VIMP/SELS and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with SVIP. Directly interacts with UBXD2 and RNF19A. Interacts with CASR. 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 and TRIM21. Interacts with RHBDD1 (via C-terminal domain). Interacts with SPRTN; leading to recruitment to stalled replication forks By similarity. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP By similarity. Interacts with KIAA0196 By similarity.

Subcellular location

Cytoplasmcytosol By similarity. Nucleus By similarity. 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.

Post-translational modification

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation.

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
Ubl conjugation pathway
   Cellular componentCytoplasm
Endoplasmic reticulum
Nucleus
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

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

protein N-linked glycosylation via asparagine

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

translesion synthesis

Inferred from sequence or structural similarity. Source: UniProtKB

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

site of double-strand break

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 806805Transitional endoplasmic reticulum ATPase
PRO_0000280706

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
Q3ZBT1 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 1D366BF671119B70

FASTA80689,330
        10         20         30         40         50         60 
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK 

        70         80         90        100        110        120 
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVHLGDVI 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

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC103125 mRNA. Translation: AAI03126.1.
RefSeqNP_001029466.1. NM_001034294.2.
UniGeneBt.49331.

3D structure databases

ProteinModelPortalQ3ZBT1.
SMRQ3ZBT1. Positions 18-763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ3ZBT1. 1 interaction.
STRING9913.ENSBTAP00000019970.

Proteomic databases

PaxDbQ3ZBT1.
PRIDEQ3ZBT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID507345.
KEGGbta:507345.

Organism-specific databases

CTD7415.

Phylogenomic databases

eggNOGCOG0464.
HOGENOMHOG000223224.
HOVERGENHBG001226.
InParanoidQ3ZBT1.
KOK13525.

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

NextBio20868019.

Entry information

Entry nameTERA_BOVIN
AccessionPrimary (citable) accession number: Q3ZBT1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: September 27, 2005
Last modified: June 11, 2014
This is version 89 of the entry and version 1 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