BL1S6_DROME
ID BL1S6_DROME Reviewed; 167 AA.
AC Q9VTM0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 6;
DE Short=BLOC-1 subunit 6;
DE AltName: Full=Pallid protein homolog;
GN Name=Pldn {ECO:0000303|PubMed:28317021, ECO:0000312|FlyBase:FBgn0036192};
GN Synonyms=Pallidin {ECO:0000312|FlyBase:FBgn0036192};
GN ORFNames=CG14133 {ECO:0000312|FlyBase:FBgn0036192};
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 [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 [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 [3]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, FUNCTION, AND INTERACTION WITH BLOS1;
RP BLOS4 AND DYSB.
RX PubMed=20015953; DOI=10.1093/hmg/ddp555;
RA Cheli V.T., Daniels R.W., Godoy R., Hoyle D.J., Kandachar V., Starcevic M.,
RA Martinez-Agosto J.A., Poole S., DiAntonio A., Lloyd V.K., Chang H.C.,
RA Krantz D.E., Dell'Angelica E.C.;
RT "Genetic modifiers of abnormal organelle biogenesis in a Drosophila model
RT of BLOC-1 deficiency.";
RL Hum. Mol. Genet. 19:861-878(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28317021; DOI=10.1523/eneuro.0335-16.2017;
RA Chen X., Ma W., Zhang S., Paluch J., Guo W., Dickman D.K.;
RT "The BLOC-1 Subunit Pallidin Facilitates Activity-Dependent Synaptic
RT Vesicle Recycling.";
RL ENeuro 4:0-0(2017).
CC -!- FUNCTION: Component of the biogenesis of lysosome-related organelles
CC complex-1 (BLOC-1) involved in pigment granule biogenesis and membrane
CC trafficking in synapses (PubMed:20015953, PubMed:28317021). In response
CC to high synaptic activity at neuromuscular junctions, plays a key role
CC in promoting efficient synaptic vesicle recycling and re-formation
CC through early endosomes (PubMed:28317021).
CC {ECO:0000269|PubMed:20015953, ECO:0000269|PubMed:28317021}.
CC -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC complex-1 (BLOC-1) composed of Blos1, Blos2, Blos3, Blos4, Dysb, Muted,
CC Pldn and Snapin. Interacts with Blos1, Blos4 and Dysb.
CC {ECO:0000269|PubMed:20015953}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:28317021}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:28317021}. Cytoplasm, myofibril,
CC sarcomere, Z line {ECO:0000269|PubMed:28317021}. Note=At the
CC neuromuscular junctions, present at both pre- and postsynaptic
CC compartments where it associates with cytoskeletal neuronal microtubule
CC structures and muscle Z-lines. {ECO:0000269|PubMed:28317021}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from embryo to
CC adult stages (at protein level) (PubMed:28317021). In larvae, expressed
CC at the neuromuscular junction both pre- and postsynaptically (at
CC protein level) (PubMed:28317021). {ECO:0000269|PubMed:28317021}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:28317021). In the
CC neuromuscular junctions, results in abnormal tubular endosomal
CC compartments and a reduction in early endosomes which leads to a
CC decrease recycling and recovery of the synaptic vesicle pool and
CC results in failure to sustain neurotransmitter release during high-
CC frequency stimulation (PubMed:28317021). Does not affect synaptic
CC morphology or basal function (PubMed:28317021).
CC {ECO:0000269|PubMed:28317021}.
CC -!- SIMILARITY: Belongs to the BLOC1S6 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF50027.2; -; Genomic_DNA.
DR RefSeq; NP_648494.2; NM_140237.2.
DR AlphaFoldDB; Q9VTM0; -.
DR SMR; Q9VTM0; -.
DR BioGRID; 64676; 19.
DR IntAct; Q9VTM0; 6.
DR STRING; 7227.FBpp0289374; -.
DR PaxDb; Q9VTM0; -.
DR PRIDE; Q9VTM0; -.
DR EnsemblMetazoa; FBtr0300097; FBpp0289374; FBgn0036192.
DR GeneID; 39315; -.
DR KEGG; dme:Dmel_CG14133; -.
DR UCSC; CG14133-RB; d. melanogaster.
DR CTD; 39315; -.
DR FlyBase; FBgn0036192; Pldn.
DR VEuPathDB; VectorBase:FBgn0036192; -.
DR eggNOG; ENOG502TCAT; Eukaryota.
DR GeneTree; ENSGT00510000047812; -.
DR HOGENOM; CLU_139371_0_0_1; -.
DR InParanoid; Q9VTM0; -.
DR OMA; MMSDVKR; -.
DR OrthoDB; 1497449at2759; -.
DR PhylomeDB; Q9VTM0; -.
DR BioGRID-ORCS; 39315; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39315; -.
DR PRO; PR:Q9VTM0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036192; Expressed in digestive system element and 25 other tissues.
DR ExpressionAtlas; Q9VTM0; baseline and differential.
DR Genevisible; Q9VTM0; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031083; C:BLOC-1 complex; IGI:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0098975; C:postsynapse of neuromuscular junction; IDA:FlyBase.
DR GO; GO:0030133; C:transport vesicle; IBA:GO_Central.
DR GO; GO:0061174; C:type I terminal bouton; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0008057; P:eye pigment granule organization; IMP:UniProtKB.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP:FlyBase.
DR InterPro; IPR017242; BLOC-1_pallidin.
DR InterPro; IPR028119; Snapin/Pallidin/Snn1.
DR Pfam; PF14712; Snapin_Pallidin; 1.
DR PIRSF; PIRSF037609; BLOC-1_complex_pallidin; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome; Synapse.
FT CHAIN 1..167
FT /note="Biogenesis of lysosome-related organelles complex 1
FT subunit 6"
FT /id="PRO_0000420200"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 102..160
FT /evidence="ECO:0000255"
SQ SEQUENCE 167 AA; 18963 MW; 79682CEF7183F1A3 CRC64;
MLKSSNINSV LNELPNDPAR DSTAQSSHNG KPKQDAETCC SSQDNEVMAS LAALQLSAGV
LQIAEPPLNH VRTQLRELIG RQNKTYIDLS KEKYKLDCSE VARLNDMMSD VKRYKDKLTK
IKKEMQGVYQ RTKELKKRAA NVAACKQRDY QRKLERLQHE ESLIGSQ
