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P03974

- TERA_PIG

UniProt

P03974 - TERA_PIG

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Protein

Transitional endoplasmic reticulum ATPase

Gene
VCP
Organism
Sus scrofa (Pig)
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 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.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+ By similarity.

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. 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
Complete GO annotation...

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.

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
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 ATPasePRO_0000084574Add
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.
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

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.

Protein-protein interaction databases

BioGridi1149651. 1 interaction.
STRINGi9823.ENSSSCP00000005692.

Structurei

3D structure databases

ProteinModelPortaliP03974.
SMRiP03974. 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.
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

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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: June 11, 2014
This is version 137 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.

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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