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Q7ZU99 (TERA_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. 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):
Protein CDC48
Valosin-containing protein
Short name=VCP
Gene names
Name:vcp
Synonyms:cdc48
ORF Names:si:ch211-113n10.2
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length806 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 By similarity. Enhances cell cycle progression and inhibits apoptosis at low temperatures. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites and promotes the recruitment of tp53bp1 at DNA damage sites. Ref.1 UniProtKB P46462

Catalytic activity

ATP + H2O = ADP + phosphate. UniProtKB P23787

Subunit structure

Homohexamer By similarity. UniProtKB P23787

Subcellular location

Cytoplasmcytosol By similarity. Nucleus By similarity. Note: Following DNA double-strand breaks, recruited to the sites of damage By similarity. UniProtKB P23787

Induction

By cold. Ref.1

Sequence similarities

Belongs to the AAA ATPase family.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA repair
Transport
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

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

embryo development

Inferred from mutant phenotype PubMed 22549779. Source: ZFIN

protein N-linked glycosylation via asparagine

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 22549779. Source: ZFIN

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

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

Chain1 – 806806Transitional endoplasmic reticulum ATPase
PRO_0000382233

Regions

Nucleotide binding247 – 2537ATP By similarity

Sites

Binding site3481ATP By similarity
Binding site3841ATP By similarity

Amino acid modifications

Modified residue31Phosphoserine Ref.5

Experimental info

Mutagenesis8051Y → A: Inhibits cell-proliferation and enhances apoptosis at low temperatures. Ref.1
Sequence conflict641 – 6433QLI → HIM in BAC87740. Ref.1
Sequence conflict7091R → L in BAC87740. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7ZU99 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E126C61DFD7EE174

FASTA80689,424
        10         20         30         40         50         60 
MASGGESKND DLSTAILKQK NRPNRLIVDE SINEDNSVVS LSQAKMDELQ LFRGDTVLLK 

        70         80         90        100        110        120 
GKKRRETVCI VLSDDTCSDE KVRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID 

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

       190        200        210        220        230        240 
VIHCEGEPIK REDEEESLNE VGYDDIGGVR 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 VPNITWEDIG 

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

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

       610        620        630        640        650        660 
INQILTEMDG MSSKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRIAILKAN 

       670        680        690        700        710        720 
LRKSPISKDV DLDFLAKMTN GFSGADLTEI CQRACKLAIR ESIENEIRRE RERQTNPSAM 

       730        740        750        760        770        780 
EVEEDDPVPE IRKDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSSNQGG 

       790        800 
SGPSQGSSGG GGGNVFNEDN DDDLYG 

« Hide

References

« Hide 'large scale' references
[1]"Cold-inducible expression of the cell division cycle gene CDC48 and its promotion of cell proliferation during cold acclimation in zebrafish cells."
Imamura S., Ojima N., Yamashita M.
FEBS Lett. 549:14-20(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, MUTAGENESIS OF TYR-805.
Tissue: Embryo.
[2]"Hematopoietic gene expression profile in zebrafish kidney marrow."
Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y., Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X., Look A.T., Chen Z.
Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney marrow.
[3]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[4]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: AB.
Tissue: Kidney.
[5]"Online automated in vivo zebrafish phosphoproteomics: from large-scale analysis down to a single embryo."
Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J., Slijper M., Heck A.J.R.
J. Proteome Res. 7:1555-1564(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB093594 mRNA. Translation: BAC87740.1.
AY576993 mRNA. Translation: AAS92631.1.
CR318632 Genomic DNA. Translation: CAM13143.1.
BC050488 mRNA. Translation: AAH50488.1.
BC067384 mRNA. Translation: AAH67384.1.
RefSeqNP_958889.1. NM_201481.1.
UniGeneDr.75122.

3D structure databases

ProteinModelPortalQ7ZU99.
SMRQ7ZU99. Positions 18-763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ7ZU99. 1 interaction.
MINTMINT-8283632.
STRING7955.ENSDARP00000012048.

Proteomic databases

PRIDEQ7ZU99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000023779; ENSDARP00000012048; ENSDARG00000020008.
GeneID327197.
KEGGdre:327197.

Organism-specific databases

CTD7415.
ZFINZDB-GENE-030131-5408. vcp.

Phylogenomic databases

eggNOGCOG0464.
GeneTreeENSGT00740000115575.
HOGENOMHOG000223224.
InParanoidQ76KA4.
KOK13525.
OMADKFLKYG.
OrthoDBEOG7H4DSW.
PhylomeDBQ7ZU99.
TreeFamTF300542.

Gene expression databases

BgeeQ7ZU99.

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...

Other

NextBio20809924.
PROQ7ZU99.

Entry information

Entry nameTERA_DANRE
AccessionPrimary (citable) accession number: Q7ZU99
Secondary accession number(s): Q76KA4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 103 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