TERA_DROME
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 03-AUG-2022, entry version 154.
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; 112.
DR DIP; DIP-52184N; -.
DR IntAct; Q7KN62; 14.
DR MINT; Q7KN62; -.
DR STRING; 7227.FBpp0111818; -.
DR iPTMnet; Q7KN62; -.
DR PaxDb; Q7KN62; -.
DR PRIDE; Q7KN62; -.
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 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 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 tissues.
DR ExpressionAtlas; Q7KN62; baseline and differential.
DR Genevisible; Q7KN62; DM.
DR GO; GO:0044754; C:autolysosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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: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: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:0006511; P:ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 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; Vps4_C.
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 SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR TIGRFAMs; TIGR01243; CDC48; 1.
DR PROSITE; PS00674; AAA; 2.
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
