VIAF1_DROME
ID VIAF1_DROME Reviewed; 240 AA.
AC Q8MR62; Q86G89; Q9VTS2;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Viral IAP-associated factor homolog;
GN Name=viaf; Synonyms=viaf1; ORFNames=CG18593;
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] {ECO:0000305, ECO:0000312|EMBL:AAG21889.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15371430; DOI=10.1074/jbc.m409623200;
RA Wilkinson J.C., Richter B.W.M., Wilkinson A.S., Burstein E., Rumble J.M.,
RA Balliu B., Duckett C.S.;
RT "VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that
RT modulates caspase activation.";
RL J. Biol. Chem. 279:51091-51099(2004).
RN [2] {ECO:0000312|EMBL:AAF49974.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF49974.2}
RP GENOME REANNOTATION.
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAM52617.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM52617.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-73, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Modulates the activation of caspases during apoptosis.
CC {ECO:0000250|UniProtKB:Q9H2J4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000255}.
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DR EMBL; AF110513; AAG21889.1; -; mRNA.
DR EMBL; AE014296; AAF49974.2; -; Genomic_DNA.
DR EMBL; AY122105; AAM52617.1; -; mRNA.
DR RefSeq; NP_524032.2; NM_079308.2.
DR AlphaFoldDB; Q8MR62; -.
DR SMR; Q8MR62; -.
DR BioGRID; 64724; 5.
DR STRING; 7227.FBpp0075794; -.
DR iPTMnet; Q8MR62; -.
DR PaxDb; Q8MR62; -.
DR PRIDE; Q8MR62; -.
DR DNASU; 39364; -.
DR EnsemblMetazoa; FBtr0076062; FBpp0075794; FBgn0036237.
DR GeneID; 39364; -.
DR KEGG; dme:Dmel_CG18593; -.
DR CTD; 39364; -.
DR FlyBase; FBgn0036237; viaf.
DR VEuPathDB; VectorBase:FBgn0036237; -.
DR eggNOG; KOG3170; Eukaryota.
DR GeneTree; ENSGT00940000175722; -.
DR HOGENOM; CLU_072604_0_0_1; -.
DR InParanoid; Q8MR62; -.
DR OMA; QKPDYSR; -.
DR OrthoDB; 1247977at2759; -.
DR PhylomeDB; Q8MR62; -.
DR BioGRID-ORCS; 39364; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39364; -.
DR PRO; PR:Q8MR62; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036237; Expressed in embryonic/larval hemocyte (Drosophila) and 27 other tissues.
DR Genevisible; Q8MR62; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1903645; P:negative regulation of chaperone-mediated protein folding; ISS:FlyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02114; Phosducin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..240
FT /note="Viral IAP-associated factor homolog"
FT /id="PRO_0000163761"
FT REGION 99..240
FT /note="Thioredoxin fold"
FT /evidence="ECO:0000250"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 156
FT /note="R -> C (in Ref. 1; AAG21889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27440 MW; 7BBF19760F937D77 CRC64;
MQDPNEDTEW NDVLRAKGII GPKAKEAEIT EDQIQKLMDD AIQRRTDLPL NEGQRDKKID
DMSLDELDEL EDSEDEAVLE QYRQRRIAEM RATAEKARFG SVREISGQDY VNEVTKAGEG
IWVVLHLYAN GVPLCALIHH HMQQLAVRFP QTKFVRSVAT TCIPNFPEKN LPTIFIYHEG
ALRKQYIGPL ELRGDKLTAE ELEFMLGQAG AVPTEITEDP RPQIRDKMLA DLEDKSSDFY
