Transitional endoplasmic reticulum ATPase - Xenopus laevis (African clawed frog)

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P23787 (TERA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transitional endoplasmic reticulum ATPase
Short name=TER ATPase
EC=3.6.4.6

Alternative name(s):
15S Mg(2+)-ATPase p97 subunit
Short name=p97
Valosin-containing protein
Short name=VCP

Gene names

Name:

vcp

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	805 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	ATP + H₂O = ADP + phosphate. Ref.3
Enzyme regulation	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). Ref.3
Subunit structure	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. Ref.3 Ref.4
Subcellular location	Cytoplasm › cytosol. Nucleus. Note: Following DNA double-strand breaks, recruited to the sites of damage By similarity. Ref.3 Ref.4
Tissue specificity	Expressed in at least oocytes, liver and kidney (at protein level). Ref.3
Post-translational modification	Phosphorylated. Ref.3
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transport
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Lipid-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB protein N-linked glycosylation via asparagine Inferred from sequence or structural similarity. Source: UniProtKB protein hexamerization Inferred from direct assay Ref.3. Source: UniProtKB protein ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB translesion synthesis Inferred from sequence or structural similarity. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromatin Inferred from direct assay Ref.4. Source: UniProtKB cytoplasm Inferred from direct assay Ref.3. Source: UniProtKB cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.4 Ref.3. Source: UniProtKB site of double-strand break Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from direct assay Ref.3. Source: UniProtKB lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 805

805

Transitional endoplasmic reticulum ATPase

PRO_0000084576

Regions

Nucleotide binding

247 – 253

ATP By similarity

Sites

Binding site

348

ATP By similarity

Binding site

384

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Experimental info

Sequence conflict

M → V in CAA38146. Ref.1

Sequence conflict

K → E AA sequence Ref.4

Sequence conflict

455

A → G in CAA38146. Ref.1

Sequence conflict

742

F → L in CAA38146. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P23787 [UniParc].

Last modified September 1, 2009. Version 3.
Checksum: 157D03B5BDB0F464
Show »

FASTA

805

89,212

        10         20         30         40         50         60 
MASGSDTKSD DLSTAILKQK SRPNRLIVDE SINEDNSMVS LSQAKMDELQ LFRGDTVLLK 

        70         80         90        100        110        120 
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRVHVLPID 

       130        140        150        160        170        180 
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT 

       190        200        210        220        230        240 
VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG 

       250        260        270        280        290        300 
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI 

       310        320        330        340        350        360 
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF 

       370        380        390        400        410        420 
GRFDREVDIG IPDSTGRLEI LQIHTKNMKL SDDVDLEQVA NETHGHVGAD LAALCSEAAL 

       430        440        450        460        470        480 
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG 

       490        500        510        520        530        540 
GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI 

       550        560        570        580        590        600 
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 

       610        620        630        640        650        660 
INQILTEMDG MSIKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRMAILKAN 

       670        680        690        700        710        720 
LRKSPVAKDV DVDFLAKMTN GFSGADLTEI CQRACKLAIR ESIENEIRRE RDRQTNPSAM 

       730        740        750        760        770        780 
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPAGGQSG 

       790        800 
AGPSPGAGGG SGGGHFTEED DDLYG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X54240 mRNA. Translation: CAA38146.1. BC046949 mRNA. Translation: AAH46949.1.
PIR	S19738.
RefSeq	NP_001095217.1. NM_001101747.1.
UniGene	Xl.8775.
3D structure databases
ProteinModelPortal	P23787.
SMR	P23787. Positions 21-763.
ModBase	Search...
Proteomic databases
PRIDE	P23787.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	380491.
KEGG	xla:380491.
Organism-specific databases
CTD	7415.
Xenbase	XB-GENE-969578. vcp.
Phylogenomic databases
HOVERGEN	HBG001226.
KO	K13525.
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
InterPro	IPR003593. AAA+_ATPase. IPR009010. Asp_de-COase-like_dom. IPR005938. ATPase_AAA_CDC48. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR004201. Cdc48_dom2. IPR003338. CDC4_N-term_subdom. IPR015415. Vps4_C. [Graphical view]
PANTHER	PTHR23077:SF18. PTHR23077:SF18. 1 hit.
Pfam	PF00004. AAA. 2 hits. PF02933. CDC48_2. 1 hit. PF02359. CDC48_N. 1 hit. PF09336. Vps4_C. 1 hit. [Graphical view]
SMART	SM00382. AAA. 2 hits. SM01072. CDC48_2. 1 hit. SM01073. CDC48_N. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR01243. CDC48. 1 hit.
PROSITE	PS00674. AAA. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TERA_XENLA

Accession

Primary (citable) accession number: P23787
Secondary accession number(s): Q7ZWL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents