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Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (Protein CDC48) (Valosin-containing protein) (VCP)

 TERA_DANRE              Reviewed;         806 AA.
Q7ZU99; Q76KA4;
01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
20-JUN-2018, entry version 136.
RecName: Full=Transitional endoplasmic reticulum ATPase {ECO:0000250|UniProtKB:P23787};
Short=TER ATPase {ECO:0000250|UniProtKB:P23787};
EC=3.6.4.6 {ECO:0000250|UniProtKB:P23787};
AltName: Full=Protein CDC48 {ECO:0000303|PubMed:12914916, ECO:0000312|EMBL:BAC87740.1};
AltName: Full=Valosin-containing protein {ECO:0000303|PubMed:12914916, ECO:0000312|EMBL:AAH50488.1};
Short=VCP {ECO:0000250|UniProtKB:P23787, ECO:0000303|PubMed:12914916};
Name=vcp {ECO:0000312|EMBL:AAH50488.1,
ECO:0000312|ZFIN:ZDB-GENE-030131-5408}; Synonyms=cdc48;
ORFNames=si:ch211-113n10.2;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1] {ECO:0000305, ECO:0000312|EMBL:BAC87740.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND MUTAGENESIS OF
TYR-805.
TISSUE=Embryo {ECO:0000269|PubMed:12914916};
PubMed=12914916; DOI=10.1016/S0014-5793(03)00723-3;
Imamura S., Ojima N., Yamashita M.;
"Cold-inducible expression of the cell division cycle gene CDC48 and
its promotion of cell proliferation during cold acclimation in
zebrafish cells.";
FEBS Lett. 549:14-20(2003).
[2] {ECO:0000305, ECO:0000312|EMBL:AAS92631.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney marrow {ECO:0000269|PubMed:15520368};
PubMed=15520368; DOI=10.1073/pnas.0407241101;
Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y.,
Sheng Y., Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I.,
Kanki J.P., Liu T.X., Look A.T., Chen Z.;
"Hematopoietic gene expression profile in zebrafish kidney marrow.";
Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[4] {ECO:0000312|EMBL:CAM13143.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=AB {ECO:0000312|EMBL:AAH50488.1};
TISSUE=Kidney {ECO:0000312|EMBL:AAH67384.1};
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305}
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Embryo {ECO:0000269|PubMed:18307296};
PubMed=18307296; DOI=10.1021/pr700667w;
Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B.,
den Hertog J., Slijper M., Heck A.J.R.;
"Online automated in vivo zebrafish phosphoproteomics: from large-
scale analysis down to a single embryo.";
J. Proteome Res. 7:1555-1564(2008).
-!- 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). Enhances cell cycle progression and inhibits
apoptosis at low temperatures (PubMed:12914916). Essential for the
maturation of ubiquitin-containing autophagosomes and the
clearance of ubiquitinated protein by autophagy (By similarity).
Acts as a negative regulator of type I interferon production by
promoting ubiquitination of ddx58/rig-i (By similarity). May play
a role in the ubiquitin-dependent sorting of membrane proteins to
lysosomes where they undergo degradation (By similarity). May more
particularly play a role in caveolins sorting in cells (By
similarity). By controlling the steady-state expression of the
IGF1R receptor, indirectly regulates the insulin-like growth
factor receptor signaling pathway (By similarity).
{ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072,
ECO:0000269|PubMed:12914916}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:P23787}.
-!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P23787}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P23787}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P55072}. Nucleus
{ECO:0000250|UniProtKB:P23787}.
-!- INDUCTION: By cold. {ECO:0000269|PubMed:12914916}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; AB093594; BAC87740.1; -; mRNA.
EMBL; AY576993; AAS92631.1; -; mRNA.
EMBL; CR318632; CAM13143.1; -; Genomic_DNA.
EMBL; BC050488; AAH50488.1; -; mRNA.
EMBL; BC067384; AAH67384.1; -; mRNA.
RefSeq; NP_958889.1; NM_201481.1.
UniGene; Dr.75122; -.
ProteinModelPortal; Q7ZU99; -.
SMR; Q7ZU99; -.
IntAct; Q7ZU99; 1.
MINT; Q7ZU99; -.
STRING; 7955.ENSDARP00000012048; -.
iPTMnet; Q7ZU99; -.
PaxDb; Q7ZU99; -.
PRIDE; Q7ZU99; -.
Ensembl; ENSDART00000023779; ENSDARP00000012048; ENSDARG00000020008.
GeneID; 327197; -.
KEGG; dre:327197; -.
CTD; 7415; -.
ZFIN; ZDB-GENE-030131-5408; vcp.
eggNOG; KOG0730; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00900000141071; -.
HOGENOM; HOG000223224; -.
InParanoid; Q7ZU99; -.
KO; K13525; -.
OMA; PIDDTTE; -.
OrthoDB; EOG091G024K; -.
PhylomeDB; Q7ZU99; -.
TreeFam; TF300542; -.
Reactome; R-DRE-110320; Translesion Synthesis by POLH.
Reactome; R-DRE-3371511; HSF1 activation.
Reactome; R-DRE-382556; ABC-family proteins mediated transport.
Reactome; R-DRE-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-DRE-5358346; Hedgehog ligand biogenesis.
Reactome; R-DRE-5689877; Josephin domain DUBs.
Reactome; R-DRE-5689896; Ovarian tumor domain proteases.
Reactome; R-DRE-6798695; Neutrophil degranulation.
Reactome; R-DRE-8876725; Protein methylation.
PRO; PR:Q7ZU99; -.
Proteomes; UP000000437; Chromosome 5.
Bgee; ENSDARG00000020008; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB.
GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
GO; GO:0007626; P:locomotory behavior; IMP:ZFIN.
GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:2000058; P:regulation of ubiquitin-dependent protein catabolic process; IMP:ZFIN.
GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR005938; AAA_ATPase_CDC48.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR004201; Cdc48_dom2.
InterPro; IPR029067; CDC48_domain_2-like_sf.
InterPro; IPR003338; CDC4_N-term_subdom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015415; Vps4_C.
Pfam; PF00004; AAA; 2.
Pfam; PF02933; CDC48_2; 1.
Pfam; PF02359; CDC48_N; 1.
Pfam; PF09336; Vps4_C; 1.
SMART; SM00382; AAA; 2.
SMART; SM01072; CDC48_2; 1.
SMART; SM01073; CDC48_N; 1.
SUPFAM; SSF50692; SSF50692; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54585; SSF54585; 1.
TIGRFAMs; TIGR01243; CDC48; 1.
PROSITE; PS00674; AAA; 2.
1: Evidence at protein level;
ATP-binding; Autophagy; Cell cycle; Complete proteome; Cytoplasm;
DNA damage; DNA repair; Endoplasmic reticulum; Hydrolase;
Lipid-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Transport.
CHAIN 1 806 Transitional endoplasmic reticulum
ATPase.
/FTId=PRO_0000382233.
NP_BIND 247 253 ATP. {ECO:0000250|UniProtKB:P55072}.
NP_BIND 521 526 ATP. {ECO:0000250|UniProtKB:Q01853}.
BINDING 348 348 ATP. {ECO:0000250|UniProtKB:P55072}.
BINDING 384 384 ATP. {ECO:0000250|UniProtKB:P55072}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000269|PubMed:18307296}.
MUTAGEN 805 805 Y->A: Inhibits cell-proliferation and
enhances apoptosis at low temperatures.
{ECO:0000269|PubMed:12914916}.
CONFLICT 641 643 QLI -> HIM (in Ref. 1; BAC87740).
{ECO:0000305}.
CONFLICT 709 709 R -> L (in Ref. 1; BAC87740).
{ECO:0000305}.
SEQUENCE 806 AA; 89424 MW; E126C61DFD7EE174 CRC64;
MASGGESKND DLSTAILKQK NRPNRLIVDE SINEDNSVVS LSQAKMDELQ LFRGDTVLLK
GKKRRETVCI VLSDDTCSDE KVRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT
VIHCEGEPIK REDEEESLNE VGYDDIGGVR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF
GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPNITWEDIG
GLDDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNV GDGGGAADRV
INQILTEMDG MSSKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRIAILKAN
LRKSPISKDV DLDFLAKMTN GFSGADLTEI CQRACKLAIR ESIENEIRRE RERQTNPSAM
EVEEDDPVPE IRKDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSSNQGG
SGPSQGSSGG GGGNVFNEDN DDDLYG


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