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P03974

- TERA_PIG

UniProt

P03974 - TERA_PIG

Protein

Transitional endoplasmic reticulum ATPase

Gene

VCP

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Mg2+.By similarity

    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. ATP binding Source: UniProtKB-KW
    2. lipid binding Source: UniProtKB-KW
    3. nucleoside-triphosphatase activity Source: InterPro

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair, Transport, Ubl conjugation pathway

    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
    Valosin-containing protein
    Short name:
    VCP
    Gene namesi
    Name:VCP
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell
    4. site of double-strand break Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 806805Transitional endoplasmic reticulum ATPasePRO_0000084574Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei3 – 31PhosphoserineBy similarity
    Modified residuei37 – 371PhosphoserineBy similarity
    Modified residuei315 – 3151N6,N6,N6-trimethyllysine; by VCPKMTBy similarity
    Modified residuei436 – 4361PhosphothreonineBy similarity
    Modified residuei502 – 5021N6-acetyllysineBy similarity
    Modified residuei505 – 5051N6-acetyllysineBy similarity
    Modified residuei668 – 6681N6-acetyllysine; alternateBy similarity
    Modified residuei668 – 6681N6-succinyllysine; alternateBy similarity
    Modified residuei754 – 7541N6-acetyllysineBy similarity
    Modified residuei770 – 7701PhosphoserineBy similarity
    Modified residuei775 – 7751PhosphoserineBy similarity
    Modified residuei787 – 7871PhosphoserineBy similarity
    Modified residuei805 – 8051PhosphotyrosineBy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP03974.

    Interactioni

    Subunit structurei

    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 NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis By similarity. Interacts with VIMP/SELS and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Interacts with SVIP. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXD2 and RNF19A. Interacts with CASR. Interacts with UBXN6, UBE4B and YOD1. Interacts with clathrin. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). 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.By similarity

    Protein-protein interaction databases

    BioGridi1149651. 1 interaction.
    STRINGi9823.ENSSSCP00000005692.

    Structurei

    3D structure databases

    ProteinModelPortaliP03974.
    SMRiP03974. Positions 18-763.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni797 – 80610Interaction with UBXN6By similarity

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Curated

    Phylogenomic databases

    eggNOGiCOG0464.
    HOGENOMiHOG000223224.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P03974-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ    50
    LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVHLGDVI 100
    SIQPCPDVKY GKRIHVLPID 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 IPDATGRLEI LQIHTKNMKL ADDVDLEQVA 400
    NETHGHVGAD LAALCSEAAL QAIRKKMDLI DLEDETIDAE VMNSLAVTMD 450
    DFRWALSQSN PSALRETVVE VPQVTWEDIG GLEDVKRELQ DLVQYPVEHP 500
    DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI SIKGPELLTM 550
    WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 600
    INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE 650
    KSRVAILKAN LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR 700
    ESIESEIRRE RERQTNPSAM EVEEDDPVPE IRRDHFEEAM RFARRSVSDN 750
    DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG AGPSQGSGGG TGGSVYTEDN 800
    DDDLYG 806
    Length:806
    Mass (Da):89,289
    Last modified:January 23, 2007 - v5
    Checksum:i83B36B03DB7D9B35
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30143 mRNA. Translation: AAA31142.1.
    PIRiA26360. VPPG.
    RefSeqiNP_999445.1. NM_214280.1.
    UniGeneiSsc.856.

    Genome annotation databases

    GeneIDi397524.
    KEGGissc:397524.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30143 mRNA. Translation: AAA31142.1 .
    PIRi A26360. VPPG.
    RefSeqi NP_999445.1. NM_214280.1.
    UniGenei Ssc.856.

    3D structure databases

    ProteinModelPortali P03974.
    SMRi P03974. Positions 18-763.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1149651. 1 interaction.
    STRINGi 9823.ENSSSCP00000005692.

    Proteomic databases

    PaxDbi P03974.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397524.
    KEGGi ssc:397524.

    Organism-specific databases

    CTDi 7415.

    Phylogenomic databases

    eggNOGi COG0464.
    HOGENOMi HOG000223224.
    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. "Use of a cDNA clone to identify a supposed precursor protein containing valosin."
      Koller K.J., Brownstein M.J.
      Nature 325:542-545(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Valosin: isolation and characterization of a novel peptide from porcine intestine."
      Schmidt W.E., Mutt V., Carlquist M., Kratzin H., Conlon J.M., Creutzfeldt W.
      FEBS Lett. 191:264-268(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 493-517.
    3. "The generation of valosin-like peptides from a precursor protein in vitro as an extraction artifact."
      Gill J.S., Ghatei M.A., Domin J., Bloom S.R.
      Life Sci. 44:483-491(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: SHOWS THAT VALOSIN IS A PURIFICATION ARTIFACT.

    Entry informationi

    Entry nameiTERA_PIG
    AccessioniPrimary (citable) accession number: P03974
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Valosin is an artifact of purification procedure, generated in vitro by cleavage of the whole protein upon acid extraction of tissues.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3