VP16B_DROME
ID VP16B_DROME Reviewed; 447 AA.
AC Q9VAG4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Vacuolar protein sorting-associated protein 16B {ECO:0000305};
DE AltName: Full=Protein full-of-bacteria {ECO:0000303|PubMed:21282466};
GN Name=Vps16B {ECO:0000312|FlyBase:FBgn0039702};
GN Synonyms=fob {ECO:0000303|PubMed:21282466};
GN ORFNames=CG18112 {ECO:0000312|FlyBase:FBgn0039702};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21282466; DOI=10.1083/jcb.201008119;
RA Akbar M.A., Tracy C., Kahr W.H., Kraemer H.;
RT "The full-of-bacteria gene is required for phagosome maturation during
RT immune defense in Drosophila.";
RL J. Cell Biol. 192:383-390(2011).
CC -!- FUNCTION: Essential for phagosome maturation and the innate immune
CC response to bacteria. During phagosome maturation it is required for
CC the fusion of late endosomes/lysosomes and phagosomes.
CC {ECO:0000269|PubMed:21282466}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H269}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H269}. Early endosome
CC {ECO:0000250|UniProtKB:Q9H269}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q920Q4}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000250|UniProtKB:Q9H269}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile, with no obvious morphological
CC defects. Strongly susceptible to bacterial infection, displaying
CC reduced survival after infection with E.coli and E.faecalis. The
CC initial phagocytic uptake of bacteria by the hemocytes is not affected,
CC however bacterial clearance by the phagosomes is severely reduced.
CC Phagosomes fail to fuse with late endosomes/lysosomes, preventing the
CC phagosomes from acquiring their characteristics and maturing into fully
CC acidified phagolysosomes. No effect on endocytic trafficking and
CC starvation-induced autophagy. The Notch and EGF receptor pathways are
CC also unaffected. {ECO:0000269|PubMed:21282466}.
CC -!- SIMILARITY: Belongs to the VPS16 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56946.1; -; Genomic_DNA.
DR EMBL; BT003209; AAO24964.1; -; mRNA.
DR RefSeq; NP_651731.1; NM_143474.3.
DR AlphaFoldDB; Q9VAG4; -.
DR IntAct; Q9VAG4; 1.
DR STRING; 7227.FBpp0084899; -.
DR PaxDb; Q9VAG4; -.
DR PRIDE; Q9VAG4; -.
DR DNASU; 43521; -.
DR EnsemblMetazoa; FBtr0085533; FBpp0084899; FBgn0039702.
DR GeneID; 43521; -.
DR KEGG; dme:Dmel_CG18112; -.
DR UCSC; CG18112-RA; d. melanogaster.
DR CTD; 43521; -.
DR FlyBase; FBgn0039702; Vps16B.
DR VEuPathDB; VectorBase:FBgn0039702; -.
DR eggNOG; KOG4677; Eukaryota.
DR GeneTree; ENSGT00390000013955; -.
DR HOGENOM; CLU_029487_1_0_1; -.
DR InParanoid; Q9VAG4; -.
DR OMA; QIQSTLY; -.
DR OrthoDB; 812306at2759; -.
DR PhylomeDB; Q9VAG4; -.
DR SignaLink; Q9VAG4; -.
DR BioGRID-ORCS; 43521; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 43521; -.
DR PRO; PR:Q9VAG4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039702; Expressed in secondary oocyte and 19 other tissues.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0033263; C:CORVET complex; ISS:FlyBase.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030897; C:HOPS complex; IDA:FlyBase.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071224; P:cellular response to peptidoglycan; IMP:FlyBase.
DR GO; GO:0016197; P:endosomal transport; ISS:FlyBase.
DR GO; GO:0006955; P:immune response; IDA:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0090382; P:phagosome maturation; IDA:FlyBase.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IMP:FlyBase.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; ISS:FlyBase.
DR GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR InterPro; IPR040057; Spe-39.
DR InterPro; IPR006925; Vps16_C.
DR PANTHER; PTHR13364; PTHR13364; 1.
DR Pfam; PF04840; Vps16_C; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Endosome; Immunity; Innate immunity; Lysosome;
KW Membrane; Phagocytosis; Reference proteome.
FT CHAIN 1..447
FT /note="Vacuolar protein sorting-associated protein 16B"
FT /id="PRO_0000437208"
SQ SEQUENCE 447 AA; 50412 MW; ABCD663DC95D823D CRC64;
MDLQLDSESY WNRSSRAAFS FDDEDEVDLA PDLVSNGILA DDTISEASFN NSVALNLSIK
SILSEEALKL VLQEQALDDR VLPKGVSPEE ELKLLRRQLQ STLYSPNLEA TAQKLLQGKT
APLEMFKSLH EKQQLLDTLM AQGGGHAVIT VLLFLKRTLN TTQFHGILRE RPKALEQYLS
YLKESGDLAG HIELLQLFGR HQEAALKQFQ AALASGDTST RKKHLQLLVD AYATAGVGVI
PLYEQVFHAA LKMQQLMEKD SALGKLLRDQ PTPVEVLYAC CQVNSNWKEQ DMLKPVSPQR
FAADQQISPA QYEWTALNER AQAQAYADLE CIFERVPSWH PLKTKQFHIS FDLTLAVLRL
YELQAPSTVL QLFLSKMGNS VEKLALAQRV KCIKAVIDAM AGLKQQQELQ QLKDTLPERS
EEQFYCENAL KSLQSKRWTT DNIKLKL
