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Q7KN62 (TERA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transitional endoplasmic reticulum ATPase TER94

EC=3.6.4.6
Alternative name(s):
Valosin-containing protein homolog
Gene names
Name:TER94
Synonyms:VCP
ORF Names:CG2331
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length801 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. Involved in the ubiquitin-proteasome system. Important for oskar mRNA localization and/or anchoring during oogenesis. Involved in germ cell formation. Ref.7 Ref.9

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Homohexamer. Interacts with tud, vas, papi and AGO3. Ref.6 Ref.9 Ref.10

Subcellular location

Cytoplasm. Nucleus. Note: Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Ref.6 Ref.9

Tissue specificity

Present in the mushroom bodies of the protocerebrum and in the glomeruli of the antennal lobe. Present in nurse cells, oocytes and sperm bundles (at protein level). Ref.1 Ref.2 Ref.6

Developmental stage

Present in egg, pupa and imago but not larva (at protein level). Ref.1

Sequence similarities

Belongs to the AAA ATPase family.

Sequence caution

The sequence AAF17568.1 differs from that shown. Reason: Frameshift at positions 136, 142, 757 and 761.

Ontologies

Keywords
   Biological processDifferentiation
Oogenesis
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from genetic interaction PubMed 21304887. Source: FlyBase

ER-associated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 21304887. Source: FlyBase

Golgi organization

Inferred from mutant phenotype Ref.2. Source: FlyBase

dendrite morphogenesis

Inferred from mutant phenotype PubMed 21343367. Source: FlyBase

endoplasmic reticulum membrane fusion

Inferred from sequence or structural similarity Ref.2. Source: FlyBase

endoplasmic reticulum organization

Inferred from mutant phenotype Ref.2. Source: FlyBase

microtubule cytoskeleton organization

Inferred from mutant phenotype Ref.2. Source: FlyBase

oogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 15899868. Source: FlyBase

proteolysis

Inferred from mutant phenotype PubMed 15899868. Source: FlyBase

regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 21343367. Source: FlyBase

regulation of pole plasm oskar mRNA localization

Inferred from mutant phenotype Ref.2. Source: FlyBase

transport

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 19782090. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: FlyBase

fusome

Inferred from direct assay Ref.6PubMed 18355804. Source: FlyBase

lipid particle

Inferred from direct assay PubMed 16543254. Source: FlyBase

microtubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome complex

Non-traceable author statement PubMed 15899868. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q7KN62-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform D (identifier: Q7KN62-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.
Note: No experimental confirmation available.
Isoform C (identifier: Q7KN62-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MADSKG → MDHDGDTRDFMRGYHSEQDEKMKPKDSFDKR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 801801Transitional endoplasmic reticulum ATPase TER94
PRO_0000347178

Regions

Nucleotide binding244 – 2507ATP By similarity

Sites

Binding site3451ATP By similarity
Binding site3811ATP By similarity

Amino acid modifications

Modified residue7161Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 4242Missing in isoform D.
VSP_035052
Alternative sequence1 – 66MADSKG → MDHDGDTRDFMRGYHSEQDE KMKPKDSFDKR in isoform C.
VSP_035053

Experimental info

Mutagenesis4371E → A in ter94-26-8; arrests early in oogenesis. Ref.2
Sequence conflict5241L → P in AAF17568. Ref.2
Sequence conflict563 – 5642AR → GP in AAF17568. Ref.2
Sequence conflict582 – 5843ARG → SRC in AAF17568. Ref.2
Sequence conflict590 – 5912AG → C in AAF17568. Ref.2
Sequence conflict661 – 6622SP → FA in AAF17568. Ref.2
Sequence conflict6621P → A in AAC27447. Ref.1
Sequence conflict7201Missing in AAF17568. Ref.2
Sequence conflict7351E → Q in AAC27447. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: ECF8F173B3B10B07

FASTA80188,859
        10         20         30         40         50         60 
MADSKGEDLA TAILKRKDRP NRLIVEEAQN DDNSVVSLSQ AKMDELQLFR GDTVILKGKR 

        70         80         90        100        110        120 
RKETVCIVLS DDTCPDEKIR MNRVVRNNLC VHLSDVVSVQ SCPDVKYGKR VRILPIDEST 

       130        140        150        160        170        180 
EGVTGNLFEI YLKPYFLEAY RPIHMGDNFI VRAAMRPIEF KVVLTDPEPY CIVAPETVIF 

       190        200        210        220        230        240 
CDGDPIKREE EEESLNAVGY DDIGGCRKQL AQIKEMVELP LRHPSLFKAI GVKPPRGILM 

       250        260        270        280        290        300 
YGPPGTGKTL IARAVANETG AFFFLINGPE IMSKLAGESE SNLRKAFEEA EKNSPAIIFI 

       310        320        330        340        350        360 
DEIDAIAPKR DKTHGEVERR IVSQLLTLMD GMKKSSHLIV MAATNRPNSI DPALRRFGRF 

       370        380        390        400        410        420 
DREIDIGIPD ATGRLEVLRI HTKNMKLHDD VDLEQIAAES HGHVGADLAS LCSEAALQQI 

       430        440        450        460        470        480 
REKMDLIDLE DDKIDAEVLA SLAVTMENFR YAMTKSSPSA LRETVVEVPN TTWTDIGGLE 

       490        500        510        520        530        540 
SVKKELQELV QYPVEHPDKF LKFGMQPSRG VLFYGPPGCG KTLLAKAIAN ECQANFISVK 

       550        560        570        580        590        600 
GPELLTMWFG ESEANVRDIF DKARSAAPCV LFFDELDSIA KARGGNVGDA GGAADRVINQ 

       610        620        630        640        650        660 
ILTEMDGMGA KKNVFIIGAT NRPDIIDPAI LRPGRLDQLI YIPLPDDKSR EAILKANLRK 

       670        680        690        700        710        720 
SPLAKEVDLT YIAKVTQGFS GADLTEICQR ACKLAIRQAI EAEIRREKER AENQNSAMDM 

       730        740        750        760        770        780 
DEDDPVPEIT SAHFEEAMKF ARRSVSDNDI RKYEMFAQTL QQSRGFGQNF RFPGQTGNTS 

       790        800 
GSGNNLPVNS PGDNGDDDLY S 

« Hide

Isoform D [UniParc].

Checksum: 3C3B83366776697E
Show »

FASTA75984,250
Isoform C [UniParc].

Checksum: B6D5F85ECE7BCA33
Show »

FASTA82692,055

References

« Hide 'large scale' references
[1]"TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97, is accumulated in nonproliferating cells: in the reproductive organs and in the brain of the imago."
Pinter M., Jekely G., Szepesi R.J., Farkas A., Theopold U., Meyer H.E., Lindholm D., Nassel D.R., Hultmark D., Friedrich P.
Insect Biochem. Mol. Biol. 28:91-98(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 163-176; 214-220; 229-245; 294-308; 456-479; 485-499; 503-520; 563-580; 613-632; 666-687; 694-707 AND 740-748, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Strain: Canton-S.
[2]"Membrane fusion proteins are required for oskar mRNA localization in the Drosophila egg chamber."
Ruden D.M., Sollars V., Wang X., Mori D., Alterman M., Lu X.
Dev. Biol. 218:314-325(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, MUTAGENESIS OF GLU-437.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Ovary.
[6]"Identification of TER94, an AAA ATPase protein, as a Bam-dependent component of the Drosophila fusome."
Leon A., McKearin D.
Mol. Biol. Cell 10:3825-3834(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION.
[7]"RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis."
Wojcik C., Yano M., DeMartino G.N.
J. Cell Sci. 117:281-292(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins."
Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.
Mech. Dev. 125:865-873(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TUD AND VAS, SUBCELLULAR LOCATION.
[10]"PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition."
Liu L., Qi H., Wang J., Lin H.
Development 138:1863-1873(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAPI AND AGO3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF047037 mRNA. Translation: AAC27447.1.
AF202034 mRNA. Translation: AAF17568.1. Frameshift.
AE013599 Genomic DNA. Translation: ABV53745.1.
AE013599 Genomic DNA. Translation: ABV53746.1.
AE013599 Genomic DNA. Translation: AAF58863.1.
AF132553 mRNA. Translation: AAD27852.1.
RefSeqNP_001097249.1. NM_001103779.2.
NP_001097250.1. NM_001103780.2.
NP_477369.1. NM_058021.4.
UniGeneDm.2968.

3D structure databases

ProteinModelPortalQ7KN62.
SMRQ7KN62. Positions 14-761.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61868. 78 interactions.
IntActQ7KN62. 4 interactions.

Proteomic databases

PaxDbQ7KN62.
PRIDEQ7KN62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088391; FBpp0087479; FBgn0261014. [Q7KN62-1]
GeneID36040.
KEGGdme:Dmel_CG2331.
UCSCCG2331-RA. d. melanogaster. [Q7KN62-1]

Organism-specific databases

CTD36040.
FlyBaseFBgn0261014. TER94.

Phylogenomic databases

eggNOGCOG0464.
GeneTreeENSGT00740000115575.
InParanoidQ7KN62.
KOK13525.
OMAETMEYYR.
OrthoDBEOG7H4DSW.
PhylomeDBQ7KN62.

Gene expression databases

BgeeQ7KN62.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR005938. AAA_ATPase_CDC48.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR01243. CDC48. 1 hit.
PROSITEPS00674. AAA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi36040.
NextBio796507.
PROQ7KN62.

Entry information

Entry nameTERA_DROME
AccessionPrimary (citable) accession number: Q7KN62
Secondary accession number(s): A8DY85 expand/collapse secondary AC list , A8DY86, O76279, Q9U463
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase