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P46462

- TERA_RAT

UniProt

P46462 - TERA_RAT

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Protein
Transitional endoplasmic reticulum ATPase
Gene
Vcp
Organism
Rattus norvegicus (Rat)
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 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. 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. 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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

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. ADP binding Source: RGD
  2. ATP binding Source: BHF-UCL
  3. ATPase activity Source: RGD
  4. identical protein binding Source: BHF-UCL
  5. lipid binding Source: UniProtKB-KW
  6. protein binding Source: IntAct
  7. protein complex binding Source: RGD
  8. receptor binding Source: RGD

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. ER to Golgi vesicle-mediated transport Source: RGD
  3. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  5. aggresome assembly Source: Ensembl
  6. cellular response to DNA damage stimulus Source: UniProtKB
  7. double-strand break repair Source: UniProtKB
  8. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: RGD
  9. positive regulation of protein complex assembly Source: Ensembl
  10. protein N-linked glycosylation via asparagine Source: UniProtKB
  11. protein hexamerization Source: RGD
  12. protein homooligomerization Source: RGD
  13. protein ubiquitination Source: UniProtKB
  14. retrograde protein transport, ER to cytosol Source: Ensembl
  15. translesion synthesis Source: UniProtKB
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
Valosin-containing protein
Short name:
VCP
Gene namesi
Name:Vcp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 5

Organism-specific databases

RGDi621595. Vcp.

Subcellular locationi

Cytoplasmcytosol. Nucleus. 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.1 Publication

GO - Cellular componenti

  1. cytosol Source: MGI
  2. endoplasmic reticulum Source: RGD
  3. intracellular membrane-bounded organelle Source: RGD
  4. lipid particle Source: Ensembl
  5. nucleus Source: UniProtKB-SubCell
  6. proteasome complex Source: Ensembl
  7. site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 806805Transitional endoplasmic reticulum ATPase
PRO_0000084575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei3 – 31Phosphoserine By similarity
Modified residuei37 – 371Phosphoserine By similarity
Modified residuei315 – 3151N6,N6,N6-trimethyllysine; by VCPKMT By similarity
Modified residuei436 – 4361Phosphothreonine By similarity
Modified residuei502 – 5021N6-acetyllysine By similarity
Modified residuei505 – 5051N6-acetyllysine By similarity
Modified residuei668 – 6681N6-acetyllysine; alternate By similarity
Modified residuei668 – 6681N6-succinyllysine; alternate By similarity
Modified residuei754 – 7541N6-acetyllysine By similarity
Modified residuei770 – 7701Phosphoserine By similarity
Modified residuei775 – 7751Phosphoserine By similarity
Modified residuei787 – 7871Phosphoserine By similarity
Modified residuei805 – 8051Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. Phosphorylated in mitotic cells.1 Publication
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.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP46462.
PRIDEiP46462.

2D gel databases

World-2DPAGE0004:P46462.

PTM databases

PhosphoSiteiP46462.

Expressioni

Gene expression databases

GenevestigatoriP46462.

Interactioni

Subunit structurei

Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis. Interacts with RHBDD1 (via C-terminal domain) 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 SPRTN; leading to recruitment to stalled replication forks By similarity. 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. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP. Interacts with KIAA0196 By similarity.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nsfl1cO3598710EBI-399011,EBI-1993760

Protein-protein interaction databases

BioGridi250528. 19 interactions.
IntActiP46462. 7 interactions.
MINTiMINT-1954391.
STRINGi10116.ENSRNOP00000040121.

Structurei

3D structure databases

ProteinModelPortaliP46462.
SMRiP46462. Positions 18-763.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni797 – 80610Interaction with UBXN6 By similarity

Sequence similaritiesi

Belongs to the AAA ATPase family.

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00740000115575.
HOGENOMiHOG000223224.
HOVERGENiHBG001226.
InParanoidiP46462.
KOiK13525.
OMAiHKKVNLT.
OrthoDBiEOG7H4DSW.
PhylomeDBiP46462.
TreeFamiTF300542.

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.

P46462-1 [UniParc]FASTAAdd to Basket

« Hide

MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ    50
LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI 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 ELVQYPVEHP 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 TGGNVYTEDN 800
DDDLYG 806
Length:806
Mass (Da):89,349
Last modified:January 23, 2007 - v3
Checksum:i501B721D205EBA8A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11760 mRNA. Translation: AAC52154.1.
BC060518 mRNA. Translation: AAH60518.1.
PIRiA55190.
RefSeqiNP_446316.1. NM_053864.2.
UniGeneiRn.98891.

Genome annotation databases

EnsembliENSRNOT00000046102; ENSRNOP00000040121; ENSRNOG00000034242.
GeneIDi116643.
KEGGirno:116643.
UCSCiRGD:621595. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11760 mRNA. Translation: AAC52154.1 .
BC060518 mRNA. Translation: AAH60518.1 .
PIRi A55190.
RefSeqi NP_446316.1. NM_053864.2.
UniGenei Rn.98891.

3D structure databases

ProteinModelPortali P46462.
SMRi P46462. Positions 18-763.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250528. 19 interactions.
IntActi P46462. 7 interactions.
MINTi MINT-1954391.
STRINGi 10116.ENSRNOP00000040121.

PTM databases

PhosphoSitei P46462.

2D gel databases

World-2DPAGE 0004:P46462.

Proteomic databases

PaxDbi P46462.
PRIDEi P46462.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000046102 ; ENSRNOP00000040121 ; ENSRNOG00000034242 .
GeneIDi 116643.
KEGGi rno:116643.
UCSCi RGD:621595. rat.

Organism-specific databases

CTDi 7415.
RGDi 621595. Vcp.

Phylogenomic databases

eggNOGi COG0464.
GeneTreei ENSGT00740000115575.
HOGENOMi HOG000223224.
HOVERGENi HBG001226.
InParanoidi P46462.
KOi K13525.
OMAi HKKVNLT.
OrthoDBi EOG7H4DSW.
PhylomeDBi P46462.
TreeFami TF300542.

Miscellaneous databases

NextBioi 619375.
PROi P46462.

Gene expression databases

Genevestigatori P46462.

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. "Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver."
    Zhang L., Ashendel C.L., Becker G.W., Morre D.J.
    J. Cell Biol. 127:1871-1883(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. Lubec G., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 46-53; 149-155; 192-210; 218-225; 240-251; 296-312; 366-386; 454-465; 616-638; 669-677 AND 701-709, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. "Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro."
    Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G.
    Cell 92:603-610(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STX5A.
  5. "A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways."
    Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.
    EMBO J. 19:2181-2192(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NPLOC4; UFD1L; NSFL1C AND UBE4B, SUBCELLULAR LOCATION.
  6. Cited for: FUNCTION.
  7. "Phospholipid species act as modulators in p97/p47-mediated fusion of Golgi membranes."
    Pecheur E.-I., Martin I., Maier O., Bakowsky U., Ruysschaert J.-M., Hoekstra D.
    Biochemistry 41:9813-9823(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEMBRANES.
  8. "Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4."
    Meyer H.H., Wang Y., Warren G.
    EMBO J. 21:5645-5652(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NSFL1C; NAP1L4 AND UFD1L.
  9. "VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo."
    Uchiyama K., Jokitalo E., Kano F., Murata M., Zhang X., Canas B., Newman R., Rabouille C., Pappin D., Freemont P., Kondo H.
    J. Cell Biol. 159:855-866(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VCIP135.
  10. "The localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycle."
    Uchiyama K., Jokitalo E., Lindman M., Jackman M., Kano F., Murata M., Zhang X., Kondo H.
    J. Cell Biol. 161:1067-1079(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.

Entry informationi

Entry nameiTERA_RAT
AccessioniPrimary (citable) accession number: P46462
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 139 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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