Q3ZBT1 (TERA_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified November 13, 2013. Version 83. History...
Names and origin
|Protein names||Recommended name:|
Transitional endoplasmic reticulum ATPase
Short name=TER ATPase
15S Mg(2+)-ATPase p97 subunit
|Organism||Bos taurus (Bovine) [Reference proteome]|
|Taxonomic identifier||9913 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos|
|Sequence length||806 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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.
ATP + H2O = ADP + phosphate.
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 VIMP/SELS and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with SVIP. Directly interacts with UBXD2 and RNF19A. Interacts with CASR. Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis. Interacts with UBXN6, UBE4B and YOD1. Interacts with clathrin By similarity. Interacts with RNF103 By similarity. Interacts with TRIM13 and TRIM21. Interacts with RHBDD1 (via C-terminus domain). Interacts with SPRTN; leading to recruitment to stalled replication forks By similarity.
Cytoplasm › cytosol 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.
Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation.
ISGylated By similarity.
Methylation at Lys-315 catalyzed by METTL21D is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity By similarity.
Belongs to the AAA ATPase family.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 806||805||Transitional endoplasmic reticulum ATPase||PRO_0000280706|
|Nucleotide binding||247 – 253||7||ATP By similarity|
|Region||797 – 806||10||Interaction with UBXN6 By similarity|
|Binding site||348||1||ATP By similarity|
|Binding site||384||1||ATP By similarity|
Amino acid modifications
|Modified residue||2||1||N-acetylalanine By similarity|
|Modified residue||3||1||Phosphoserine By similarity|
|Modified residue||37||1||Phosphoserine By similarity|
|Modified residue||315||1||N6,N6,N6-trimethyllysine; by METTL21D By similarity|
|Modified residue||436||1||Phosphothreonine By similarity|
|Modified residue||770||1||Phosphoserine By similarity|
|Modified residue||775||1||Phosphoserine By similarity|
|Modified residue||787||1||Phosphoserine By similarity|
|Modified residue||805||1||Phosphotyrosine By similarity|
|BC103125 mRNA. Translation: AAI03126.1.|
|RefSeq||NP_001029466.1. NM_001034294.2. |
3D structure databases
|SMR||Q3ZBT1. Positions 18-763. |
Protein-protein interaction databases
|IntAct||Q3ZBT1. 1 interaction.|
Protocols and materials databases
Genome annotation databases
Enzyme and pathway databases
Family and domain databases
|InterPro||IPR003593. AAA+_ATPase. |
|Pfam||PF00004. AAA. 2 hits. |
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
|SMART||SM00382. AAA. 2 hits. |
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
|SUPFAM||SSF50692. SSF50692. 1 hit. |
SSF52540. SSF52540. 2 hits.
|TIGRFAMs||TIGR01243. CDC48. 1 hit. |
|PROSITE||PS00674. AAA. 2 hits. |
|Accession||Primary (citable) accession number: Q3ZBT1|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families