Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23787

- TERA_XENLA

UniProt

P23787 - TERA_XENLA

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 3 (01 Sep 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.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 – 3481ATPBy similarity
    Binding sitei384 – 3841ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi247 – 2537ATPBy 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

    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

    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

    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 – 31PhosphoserineBy 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/duf140.1 Publication

    Protein-protein interaction databases

    DIPiDIP-60369N.

    Structurei

    3D structure databases

    ProteinModelPortaliP23787.
    SMRiP23787. Positions 21-763.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381M → V in CAA38146. 1 PublicationCurated
    Sequence conflicti45 – 451K → E AA sequence (PubMed:10682845)Curated
    Sequence conflicti455 – 4551A → G in CAA38146. 1 PublicationCurated
    Sequence conflicti742 – 7421F → L in CAA38146. 1 PublicationCurated

    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

    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: October 1, 2014
    This is version 102 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