ID   TERA_DROME              Reviewed;         801 AA.
AC   Q7KN62; A8DY85; A8DY86; O76279; Q9U463;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Transitional endoplasmic reticulum ATPase TER94;
DE            EC=3.6.4.6;
DE   AltName: Full=Valosin-containing protein homolog;
GN   Name=TER94; Synonyms=VCP; ORFNames=CG2331;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 163-176;
RP   214-220; 229-245; 294-308; 456-479; 485-499; 503-520; 563-580; 613-632;
RP   666-687; 694-707 AND 740-748, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=Canton-S;
RX   PubMed=9639875; DOI=10.1016/s0965-1748(97)00095-7;
RA   Pinter M., Jekely G., Szepesi R.J., Farkas A., Theopold U., Meyer H.E.,
RA   Lindholm D., Nassel D.R., Hultmark D., Friedrich P.;
RT   "TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97, is
RT   accumulated in nonproliferating cells: in the reproductive organs and in
RT   the brain of the imago.";
RL   Insect Biochem. Mol. Biol. 28:91-98(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, AND MUTAGENESIS
RP   OF GLU-437.
RX   PubMed=10656772; DOI=10.1006/dbio.1999.9583;
RA   Ruden D.M., Sollars V., Wang X., Mori D., Alterman M., Lu X.;
RT   "Membrane fusion proteins are required for oskar mRNA localization in the
RT   Drosophila egg chamber.";
RL   Dev. Biol. 218:314-325(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Ovary;
RX   PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA   Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
RN   [6]
RP   TISSUE SPECIFICITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=10564274; DOI=10.1091/mbc.10.11.3825;
RA   Leon A., McKearin D.;
RT   "Identification of TER94, an AAA ATPase protein, as a Bam-dependent
RT   component of the Drosophila fusome.";
RL   Mol. Biol. Cell 10:3825-3834(1999).
RN   [7]
RP   FUNCTION.
RX   PubMed=14657277; DOI=10.1242/jcs.00841;
RA   Wojcik C., Yano M., DeMartino G.N.;
RT   "RNA interference of valosin-containing protein (VCP/p97) reveals multiple
RT   cellular roles linked to ubiquitin/proteasome-dependent proteolysis.";
RL   J. Cell Sci. 117:281-292(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [9]
RP   FUNCTION, INTERACTION WITH TUD AND VAS, AND SUBCELLULAR LOCATION.
RX   PubMed=18590813; DOI=10.1016/j.mod.2008.06.005;
RA   Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.;
RT   "Isolation of new polar granule components in Drosophila reveals P body and
RT   ER associated proteins.";
RL   Mech. Dev. 125:865-873(2008).
RN   [10]
RP   INTERACTION WITH PAPI AND AGO3.
RX   PubMed=21447556; DOI=10.1242/dev.059287;
RA   Liu L., Qi H., Wang J., Lin H.;
RT   "PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in
RT   the nuage to silence transposition.";
RL   Development 138:1863-1873(2011).
RN   [11] {ECO:0007744|PDB:4RV0}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-186 IN COMPLEX WITH NPL4, AND
RP   INTERACTION WITH TER94.
RX   PubMed=26471729; DOI=10.15252/embj.201591888;
RA   Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
RA   Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
RT   "A non-canonical role of the p97 complex in RIG-I antiviral signaling.";
RL   EMBO J. 34:2903-2920(2015).
CC   -!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
CC       mitosis and for their reassembly after mitosis. Involved in the
CC       formation of the transitional endoplasmic reticulum (tER). The transfer
CC       of membranes from the endoplasmic reticulum to the Golgi apparatus
CC       occurs via 50-70 nm transition vesicles which derive from part-rough,
CC       part-smooth transitional elements of the endoplasmic reticulum (tER).
CC       Vesicle budding from the tER is an ATP-dependent process. Involved in
CC       the ubiquitin-proteasome system. Important for oskar mRNA localization
CC       and/or anchoring during oogenesis. Involved in germ cell formation.
CC       {ECO:0000269|PubMed:14657277, ECO:0000269|PubMed:18590813}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC   -!- SUBUNIT: Homohexamer (PubMed:10564274). Interacts with tud, vas, papi
CC       and AGO3 (PubMed:18590813, PubMed:21447556). Interacts with Npl4
CC       (PubMed:26471729). {ECO:0000269|PubMed:10564274,
CC       ECO:0000269|PubMed:18590813, ECO:0000269|PubMed:21447556,
CC       ECO:0000269|PubMed:26471729}.
CC   -!- INTERACTION:
CC       Q7KN62; Q7K0S5: Gint3; NbExp=5; IntAct=EBI-224053, EBI-93425;
CC       Q7KN62; A1ZAB3: Ptp52F; NbExp=5; IntAct=EBI-224053, EBI-3410206;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10564274}. Nucleus
CC       {ECO:0000269|PubMed:10564274}. Note=Component of the meiotic nuage,
CC       also named P granule, a germ-cell-specific organelle required to
CC       repress transposon activity during meiosis (PubMed:18590813).
CC       {ECO:0000269|PubMed:18590813}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A;
CC         IsoId=Q7KN62-1; Sequence=Displayed;
CC       Name=D;
CC         IsoId=Q7KN62-2; Sequence=VSP_035052;
CC       Name=C;
CC         IsoId=Q7KN62-3; Sequence=VSP_035053;
CC   -!- TISSUE SPECIFICITY: Present in the mushroom bodies of the protocerebrum
CC       and in the glomeruli of the antennal lobe. Present in nurse cells,
CC       oocytes and sperm bundles (at protein level).
CC       {ECO:0000269|PubMed:10564274, ECO:0000269|PubMed:10656772,
CC       ECO:0000269|PubMed:9639875}.
CC   -!- DEVELOPMENTAL STAGE: Present in egg, pupa and imago but not larva (at
CC       protein level). {ECO:0000269|PubMed:9639875}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF17568.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF047037; AAC27447.1; -; mRNA.
DR   EMBL; AF202034; AAF17568.1; ALT_FRAME; mRNA.
DR   EMBL; AE013599; ABV53745.1; -; Genomic_DNA.
DR   EMBL; AE013599; ABV53746.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58863.1; -; Genomic_DNA.
DR   EMBL; AF132553; AAD27852.1; -; mRNA.
DR   RefSeq; NP_001097249.1; NM_001103779.2. [Q7KN62-3]
DR   RefSeq; NP_001097250.1; NM_001103780.2. [Q7KN62-2]
DR   RefSeq; NP_477369.1; NM_058021.4. [Q7KN62-1]
DR   PDB; 4RV0; X-ray; 2.00 A; A/C/E/G=20-186.
DR   PDBsum; 4RV0; -.
DR   AlphaFoldDB; Q7KN62; -.
DR   SMR; Q7KN62; -.
DR   BioGRID; 61868; 113.
DR   DIP; DIP-52184N; -.
DR   IntAct; Q7KN62; 15.
DR   MINT; Q7KN62; -.
DR   STRING; 7227.FBpp0111818; -.
DR   GlyGen; Q7KN62; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q7KN62; -.
DR   PaxDb; 7227-FBpp0111818; -.
DR   DNASU; 36040; -.
DR   EnsemblMetazoa; FBtr0088391; FBpp0087479; FBgn0286784. [Q7KN62-1]
DR   EnsemblMetazoa; FBtr0112905; FBpp0111818; FBgn0286784. [Q7KN62-3]
DR   EnsemblMetazoa; FBtr0112906; FBpp0111819; FBgn0286784. [Q7KN62-2]
DR   GeneID; 36040; -.
DR   KEGG; dme:Dmel_CG2331; -.
DR   UCSC; CG2331-RA; d. melanogaster. [Q7KN62-1]
DR   UCSC; CG2331-RC; d. melanogaster.
DR   UCSC; CG2331-RD; d. melanogaster.
DR   AGR; FB:FBgn0286784; -.
DR   CTD; 36040; -.
DR   FlyBase; FBgn0286784; TER94.
DR   VEuPathDB; VectorBase:FBgn0286784; -.
DR   eggNOG; KOG0730; Eukaryota.
DR   GeneTree; ENSGT00900000141071; -.
DR   HOGENOM; CLU_000688_12_0_1; -.
DR   InParanoid; Q7KN62; -.
DR   OMA; HACHDIK; -.
DR   OrthoDB; 168438at2759; -.
DR   PhylomeDB; Q7KN62; -.
DR   Reactome; R-DME-110320; Translesion Synthesis by POLH.
DR   Reactome; R-DME-3371511; HSF1 activation.
DR   Reactome; R-DME-382556; ABC-family proteins mediated transport.
DR   Reactome; R-DME-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-DME-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-8951664; Neddylation.
DR   Reactome; R-DME-9013407; RHOH GTPase cycle.
DR   Reactome; R-DME-9755511; KEAP1-NFE2L2 pathway.
DR   SignaLink; Q7KN62; -.
DR   BioGRID-ORCS; 36040; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; TER94; fly.
DR   GenomeRNAi; 36040; -.
DR   PRO; PR:Q7KN62; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0286784; Expressed in egg cell and 42 other cell types or tissues.
DR   ExpressionAtlas; Q7KN62; baseline and differential.
DR   GO; GO:0044754; C:autolysosome; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045169; C:fusome; IDA:FlyBase.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:FlyBase.
DR   GO; GO:0031965; C:nuclear membrane; HDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR   GO; GO:0043186; C:P granule; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR   GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
DR   GO; GO:0061909; P:autophagosome-lysosome fusion; IMP:FlyBase.
DR   GO; GO:0098586; P:cellular response to virus; IMP:FlyBase.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0016320; P:endoplasmic reticulum membrane fusion; ISS:FlyBase.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:FlyBase.
DR   GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR   GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR   GO; GO:0035096; P:larval midgut cell programmed cell death; IMP:FlyBase.
DR   GO; GO:0097212; P:lysosomal membrane organization; IMP:FlyBase.
DR   GO; GO:0007040; P:lysosome organization; IMP:FlyBase.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase.
DR   GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007279; P:pole cell formation; IGI:FlyBase.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:FlyBase.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR   GO; GO:0046598; P:positive regulation of viral entry into host cell; IMP:FlyBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:FlyBase.
DR   GO; GO:0006508; P:proteolysis; IMP:FlyBase.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:FlyBase.
DR   GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR   CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR   CDD; cd19528; RecA-like_CDC48_r2-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 6.10.20.150; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005938; AAA_ATPase_CDC48.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR004201; Cdc48_dom2.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR003338; CDC4_N-term_subdom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015415; Spast_Vps4_C.
DR   NCBIfam; TIGR01243; CDC48; 1.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 2.
DR   Pfam; PF02933; CDC48_2; 1.
DR   Pfam; PF02359; CDC48_N; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 1.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 2.
DR   Genevisible; Q7KN62; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Hydrolase; Nucleotide-binding; Nucleus; Oogenesis; Phosphoprotein;
KW   Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..801
FT                   /note="Transitional endoplasmic reticulum ATPase TER94"
FT                   /id="PRO_0000347178"
FT   REGION          764..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..791
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         244..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   BINDING         381
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   BINDING         518..523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   MOD_RES         716
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   VAR_SEQ         1..42
FT                   /note="Missing (in isoform D)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_035052"
FT   VAR_SEQ         1..6
FT                   /note="MADSKG -> MDHDGDTRDFMRGYHSEQDEKMKPKDSFDKR (in
FT                   isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_035053"
FT   MUTAGEN         437
FT                   /note="E->A: In ter94-26-8; arrests early in oogenesis."
FT                   /evidence="ECO:0000269|PubMed:10656772"
FT   CONFLICT        524
FT                   /note="L -> P (in Ref. 2; AAF17568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        563..564
FT                   /note="AR -> GP (in Ref. 2; AAF17568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        582..584
FT                   /note="ARG -> SRC (in Ref. 2; AAF17568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590..591
FT                   /note="AG -> C (in Ref. 2; AAF17568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        661..662
FT                   /note="SP -> FA (in Ref. 2; AAF17568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        662
FT                   /note="P -> A (in Ref. 1; AAC27447)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        720
FT                   /note="Missing (in Ref. 2; AAF17568)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        735
FT                   /note="E -> Q (in Ref. 1; AAC27447)"
FT                   /evidence="ECO:0000305"
FT   STRAND          22..27
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   HELIX           40..46
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   HELIX           83..88
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          96..101
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          109..115
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   HELIX           127..130
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   HELIX           132..136
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          156..172
FT                   /evidence="ECO:0007829|PDB:4RV0"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:4RV0"
SQ   SEQUENCE   801 AA;  88859 MW;  ECF8F173B3B10B07 CRC64;
     MADSKGEDLA TAILKRKDRP NRLIVEEAQN DDNSVVSLSQ AKMDELQLFR GDTVILKGKR
     RKETVCIVLS DDTCPDEKIR MNRVVRNNLC VHLSDVVSVQ SCPDVKYGKR VRILPIDEST
     EGVTGNLFEI YLKPYFLEAY RPIHMGDNFI VRAAMRPIEF KVVLTDPEPY CIVAPETVIF
     CDGDPIKREE EEESLNAVGY DDIGGCRKQL AQIKEMVELP LRHPSLFKAI GVKPPRGILM
     YGPPGTGKTL IARAVANETG AFFFLINGPE IMSKLAGESE SNLRKAFEEA EKNSPAIIFI
     DEIDAIAPKR DKTHGEVERR IVSQLLTLMD GMKKSSHLIV MAATNRPNSI DPALRRFGRF
     DREIDIGIPD ATGRLEVLRI HTKNMKLHDD VDLEQIAAES HGHVGADLAS LCSEAALQQI
     REKMDLIDLE DDKIDAEVLA SLAVTMENFR YAMTKSSPSA LRETVVEVPN TTWTDIGGLE
     SVKKELQELV QYPVEHPDKF LKFGMQPSRG VLFYGPPGCG KTLLAKAIAN ECQANFISVK
     GPELLTMWFG ESEANVRDIF DKARSAAPCV LFFDELDSIA KARGGNVGDA GGAADRVINQ
     ILTEMDGMGA KKNVFIIGAT NRPDIIDPAI LRPGRLDQLI YIPLPDDKSR EAILKANLRK
     SPLAKEVDLT YIAKVTQGFS GADLTEICQR ACKLAIRQAI EAEIRREKER AENQNSAMDM
     DEDDPVPEIT SAHFEEAMKF ARRSVSDNDI RKYEMFAQTL QQSRGFGQNF RFPGQTGNTS
     GSGNNLPVNS PGDNGDDDLY S
//