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P23787

- TERA_XENLA

UniProt

P23787 - TERA_XENLA

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Protein

Transitional endoplasmic reticulum ATPase

Gene
vcp
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

ATP + H2O = ADP + phosphate.1 Publication

Enzyme regulationi

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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei348 – 3481ATP By similarity
Binding sitei384 – 3841ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi247 – 2537ATP By similarity

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. lipid binding Source: UniProtKB-KW
  4. protein complex binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. double-strand break repair Source: UniProtKB
  4. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  5. protein hexamerization Source: UniProtKB
  6. protein N-linked glycosylation via asparagine Source: UniProtKB
  7. protein ubiquitination Source: UniProtKB
  8. translesion synthesis Source: UniProtKB
  9. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Transport

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transitional endoplasmic reticulum ATPase (EC:3.6.4.6)
Short name:
TER ATPase
Alternative name(s):
15S Mg(2+)-ATPase p97 subunit
Short name:
p97
Valosin-containing protein
Short name:
VCP
Gene namesi
Name:vcp
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-969578. vcp.

Subcellular locationi

Cytoplasmcytosol. Nucleus
Note: Following DNA double-strand breaks, recruited to the sites of damage By similarity.2 Publications

GO - Cellular componenti

  1. chromatin Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB
  5. site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 805805Transitional endoplasmic reticulum ATPasePRO_0000084576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Phosphoserine By similarity

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP23787.

Expressioni

Tissue specificityi

Expressed in at least oocytes, liver and kidney (at protein level).1 Publication

Interactioni

Subunit structurei

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/duf140.2 Publications

Protein-protein interaction databases

DIPiDIP-60369N.

Structurei

3D structure databases

ProteinModelPortaliP23787.
SMRiP23787. Positions 21-763.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.

Phylogenomic databases

HOVERGENiHBG001226.
KOiK13525.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. 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]
PfamiPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
TIGRFAMsiTIGR01243. CDC48. 1 hit.
PROSITEiPS00674. AAA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23787-1 [UniParc]FASTAAdd to Basket

« Hide

MASGSDTKSD DLSTAILKQK SRPNRLIVDE SINEDNSMVS LSQAKMDELQ    50
LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI 100
SIQPCPDVKY GKRVHVLPID DTVEGITGNL FEVYLKPYFL EAYRPIRKGD 150
IFLVRGGMRA VEFKVVETDP SPYCIVAPDT VIHCEGEPIK REDEEESLNE 200
VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG ILLYGPPGTG 250
KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI 300
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP 350
NSIDPALRRF GRFDREVDIG IPDSTGRLEI LQIHTKNMKL SDDVDLEQVA 400
NETHGHVGAD LAALCSEAAL QAIRKKMDLI DLEDETIDAE VMNSLAVTMD 450
DFRWALSQSN PSALRETVVE VPQVTWEDIG GLEDVKRELQ ELVQYPVEHP 500
DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI SIKGPELLTM 550
WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 600
INQILTEMDG MSIKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE 650
KSRMAILKAN LRKSPVAKDV DVDFLAKMTN GFSGADLTEI CQRACKLAIR 700
ESIENEIRRE RDRQTNPSAM EVEEDDPVPE IRRDHFEEAM RFARRSVSDN 750
DIRKYEMFAQ TLQQSRGFGS FRFPAGGQSG AGPSPGAGGG SGGGHFTEED 800
DDLYG 805
Length:805
Mass (Da):89,212
Last modified:September 1, 2009 - v3
Checksum:i157D03B5BDB0F464
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381M → V in CAA38146. 1 Publication
Sequence conflicti45 – 451K → E AA sequence 1 Publication
Sequence conflicti455 – 4551A → G in CAA38146. 1 Publication
Sequence conflicti742 – 7421F → L in CAA38146. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54240 mRNA. Translation: CAA38146.1.
BC046949 mRNA. Translation: AAH46949.1.
PIRiS19738.
RefSeqiNP_001095217.1. NM_001101747.1.
UniGeneiXl.8775.

Genome annotation databases

GeneIDi380491.
KEGGixla:380491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54240 mRNA. Translation: CAA38146.1 .
BC046949 mRNA. Translation: AAH46949.1 .
PIRi S19738.
RefSeqi NP_001095217.1. NM_001101747.1.
UniGenei Xl.8775.

3D structure databases

ProteinModelPortali P23787.
SMRi P23787. Positions 21-763.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60369N.

Proteomic databases

PRIDEi P23787.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 380491.
KEGGi xla:380491.

Organism-specific databases

CTDi 7415.
Xenbasei XB-GENE-969578. vcp.

Phylogenomic databases

HOVERGENi HBG001226.
KOi K13525.

Family and domain databases

Gene3Di 3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR003593. 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 ]
Pfami PF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
TIGRFAMsi TIGR01243. CDC48. 1 hit.
PROSITEi PS00674. AAA. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTERA_XENLA
AccessioniPrimary (citable) accession number: P23787
Secondary accession number(s): Q7ZWL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: September 1, 2009
Last modified: June 11, 2014
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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