DTBP1_DROME
ID DTBP1_DROME Reviewed; 288 AA.
AC Q9VVT5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Dysbindin protein homolog;
DE AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 8;
DE Short=BLOC-1 subunit 8;
GN Name=Dysb {ECO:0000312|FlyBase:FBgn0036819};
GN ORFNames=CG6856 {ECO:0000312|FlyBase:FBgn0036819};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
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 [4]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, FUNCTION, AND INTERACTION WITH PLDN
RP AND SNAPIN.
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 [5]
RP FUNCTION.
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, stabilizes Pldn
CC protein levels and, together with Pldn, plays a role in promoting
CC efficient synaptic vesicle recycling and re-formation through early
CC endosomes (PubMed:28317021). {ECO:0000269|PubMed:20015953,
CC 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 Pldn and Snapin.
CC {ECO:0000269|PubMed:20015953}.
CC -!- SIMILARITY: Belongs to the dysbindin family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49223.1; -; Genomic_DNA.
DR EMBL; AY071009; AAL48631.1; -; mRNA.
DR RefSeq; NP_001262023.1; NM_001275094.1.
DR RefSeq; NP_649064.1; NM_140807.4.
DR AlphaFoldDB; Q9VVT5; -.
DR SMR; Q9VVT5; -.
DR BioGRID; 65333; 48.
DR IntAct; Q9VVT5; 7.
DR STRING; 7227.FBpp0074829; -.
DR PaxDb; Q9VVT5; -.
DR DNASU; 40052; -.
DR EnsemblMetazoa; FBtr0075062; FBpp0074829; FBgn0036819.
DR EnsemblMetazoa; FBtr0333708; FBpp0305857; FBgn0036819.
DR GeneID; 40052; -.
DR KEGG; dme:Dmel_CG6856; -.
DR UCSC; CG6856-RA; d. melanogaster.
DR CTD; 40052; -.
DR FlyBase; FBgn0036819; Dysb.
DR VEuPathDB; VectorBase:FBgn0036819; -.
DR eggNOG; ENOG502QRS9; Eukaryota.
DR GeneTree; ENSGT00940000176058; -.
DR HOGENOM; CLU_085499_0_0_1; -.
DR InParanoid; Q9VVT5; -.
DR OMA; SRYEESW; -.
DR OrthoDB; 862376at2759; -.
DR PhylomeDB; Q9VVT5; -.
DR SignaLink; Q9VVT5; -.
DR BioGRID-ORCS; 40052; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40052; -.
DR PRO; PR:Q9VVT5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036819; Expressed in saliva-secreting gland and 23 other tissues.
DR ExpressionAtlas; Q9VVT5; baseline and differential.
DR Genevisible; Q9VVT5; DM.
DR GO; GO:0031083; C:BLOC-1 complex; IGI:FlyBase.
DR GO; GO:0098527; C:neuromuscular junction of somatic muscle; IDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0008057; P:eye pigment granule organization; IMP:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0048047; P:mating behavior, sex discrimination; IMP:FlyBase.
DR GO; GO:0045963; P:negative regulation of dopamine metabolic process; IDA:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:FlyBase.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0050807; P:regulation of synapse organization; IGI:FlyBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP:FlyBase.
DR InterPro; IPR007531; Dysbindin.
DR PANTHER; PTHR16294; PTHR16294; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Reference proteome.
FT CHAIN 1..288
FT /note="Dysbindin protein homolog"
FT /id="PRO_0000420202"
FT COILED 147..239
FT /evidence="ECO:0000255"
SQ SEQUENCE 288 AA; 32364 MW; 42A40A9C4AFEC68D CRC64;
MFGNLKKKLS SAIQEGLVIS ENLQQQYRQR VSSGNSGSSQ ASGITTPISP LGLNESLSSS
RSSSLSLSAP FQLTDGVPSH LNVAAGCSLL AKYEDDWQQI HGANEKNAEK AAQIANQISG
IQDQASHQHR IMSELNSSLA GIPTLIAQLQ NSSQVLNSLE EMGKQLEIEL EKLEDLREEC
ELQEFILEQQ FQLSRHKQKK LNELEQYRQQ IAQKHQSKIK DQEQTLLKLQ RERQAVFDDA
FREDMEEYKQ RGQLTKIQTT SNKLALEEVV LEANEVETKD ALEQFLNG
