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P23787 (TERA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. 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
Short name=p97
Valosin-containing protein
Short name=VCP
Gene names
Name:vcp
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length805 AA.
Sequence statusComplete.
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 nuclear envelope, and 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. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites and promotes the recruitment of tp53bp1 at DNA damage sites By similarity.

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.3

Enzyme regulation

ATPase activity is inhibited or reduced by lowering pH from 9.0 to 7.0, and by addition of Ca2+, EDTA, KNO3 or by treatment with N-ethylmaleimide (NEM). Ref.3

Subunit structure

Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Interacts with the FACT/DUF complex, which contains subunits ssrp1/duf87 and supt16h/duf140. Ref.3 Ref.4

Subcellular location

Cytoplasmcytosol. Nucleus. Note: Following DNA double-strand breaks, recruited to the sites of damage By similarity. Ref.3 Ref.4

Tissue specificity

Expressed in at least oocytes, liver and kidney (at protein level). Ref.3

Post-translational modification

Phosphorylated. Ref.3

Sequence similarities

Belongs to the AAA ATPase family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transport
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.3. Source: GOC

ER-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 hexamerization

Inferred from direct assay Ref.3. 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_componentchromatin

Inferred from direct assay Ref.4. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.4Ref.3. Source: UniProtKB

site of double-strand break

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay Ref.3. Source: UniProtKB

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein complex binding

Inferred from physical interaction Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 805805Transitional endoplasmic reticulum ATPase
PRO_0000084576

Regions

Nucleotide binding247 – 2537ATP By similarity

Sites

Binding site3481ATP By similarity
Binding site3841ATP By similarity

Amino acid modifications

Modified residue31Phosphoserine By similarity

Experimental info

Sequence conflict381M → V in CAA38146. Ref.1
Sequence conflict451K → E AA sequence Ref.4
Sequence conflict4551A → G in CAA38146. Ref.1
Sequence conflict7421F → L in CAA38146. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23787 [UniParc].

Last modified September 1, 2009. Version 3.
Checksum: 157D03B5BDB0F464

FASTA80589,212
        10         20         30         40         50         60 
MASGSDTKSD DLSTAILKQK SRPNRLIVDE SINEDNSMVS LSQAKMDELQ LFRGDTVLLK 

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

       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 IPDSTGRLEI LQIHTKNMKL SDDVDLEQVA 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 MSIKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRMAILKAN 

       670        680        690        700        710        720 
LRKSPVAKDV DVDFLAKMTN GFSGADLTEI CQRACKLAIR ESIENEIRRE RDRQTNPSAM 

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

       790        800 
AGPSPGAGGG SGGGHFTEED DDLYG 

« Hide

References

« Hide 'large scale' references
[1]Peters J.-M.
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF."
Peters J.-M., Walsh M.J., Franke W.W.
EMBO J. 9:1757-1767(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 443-805, PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ENZYME REGULATION, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
Tissue: Embryo and Oocyte.
[4]"p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication."
Yamada T., Okuhara K., Iwamatsu A., Seo H., Ohta K., Shibata T., Murofushi H.
FEBS Lett. 466:287-291(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 45-77 AND 389-405, INTERACTION WITH FACT COMPLEX, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54240 mRNA. Translation: CAA38146.1.
BC046949 mRNA. Translation: AAH46949.1.
PIRS19738.
RefSeqNP_001095217.1. NM_001101747.1.
UniGeneXl.8775.

3D structure databases

ProteinModelPortalP23787.
SMRP23787. Positions 21-763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60369N.

Proteomic databases

PRIDEP23787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID380491.
KEGGxla:380491.

Organism-specific databases

CTD7415.
XenbaseXB-GENE-969578. vcp.

Phylogenomic databases

HOVERGENHBG001226.
KOK13525.

Family and domain databases

Gene3D3.40.50.300. 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.
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.
TIGRFAMsTIGR01243. CDC48. 1 hit.
PROSITEPS00674. AAA. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTERA_XENLA
AccessionPrimary (citable) accession number: P23787
Secondary accession number(s): Q7ZWL8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 100 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