SNAPN_DROME
ID SNAPN_DROME Reviewed; 134 AA.
AC Q9VQF9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=SNAPIN protein homolog;
DE AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 7;
DE Short=BLOC-1 subunit 7;
GN Name=Snapin {ECO:0000312|FlyBase:FBgn0031455};
GN ORFNames=CG9958 {ECO:0000312|FlyBase:FBgn0031455};
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 BLOS2
RP 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).
CC -!- FUNCTION: Component of the biogenesis of lysosome-related organelles
CC complex-1 (BLOC-1) involved in pigment granule biogenesis
CC (PubMed:20015953). May participate in the coupling of lysosomes to
CC microtubule plus-end-directed kinesin motor (By similarity).
CC {ECO:0000250|UniProtKB:O95295, ECO:0000269|PubMed:20015953}.
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 Blos2 and Dysb.
CC {ECO:0000269|PubMed:20015953}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z266};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z266}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Z266}.
CC -!- SIMILARITY: Belongs to the SNAPIN family. {ECO:0000305}.
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DR EMBL; AE014134; AAF51215.1; -; Genomic_DNA.
DR RefSeq; NP_722835.1; NM_164499.2.
DR AlphaFoldDB; Q9VQF9; -.
DR SMR; Q9VQF9; -.
DR BioGRID; 534274; 3.
DR IntAct; Q9VQF9; 2.
DR STRING; 7227.FBpp0077417; -.
DR PaxDb; Q9VQF9; -.
DR PRIDE; Q9VQF9; -.
DR DNASU; 3772677; -.
DR EnsemblMetazoa; FBtr0077737; FBpp0077417; FBgn0031455.
DR GeneID; 3772677; -.
DR KEGG; dme:Dmel_CG9958; -.
DR UCSC; CG9958-RA; d. melanogaster.
DR CTD; 23557; -.
DR FlyBase; FBgn0031455; Snapin.
DR VEuPathDB; VectorBase:FBgn0031455; -.
DR eggNOG; ENOG502S1VY; Eukaryota.
DR GeneTree; ENSGT00390000008274; -.
DR HOGENOM; CLU_124640_0_0_1; -.
DR InParanoid; Q9VQF9; -.
DR OMA; QLDTHVH; -.
DR PhylomeDB; Q9VQF9; -.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 3772677; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 3772677; -.
DR PRO; PR:Q9VQF9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031455; Expressed in saliva-secreting gland and 12 other tissues.
DR Genevisible; Q9VQF9; DM.
DR GO; GO:0031083; C:BLOC-1 complex; ISS:FlyBase.
DR GO; GO:0099078; C:BORC complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; IMP:FlyBase.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0042592; P:homeostatic process; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032418; P:lysosome localization; IBA:GO_Central.
DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:FlyBase.
DR GO; GO:0016082; P:synaptic vesicle priming; NAS:FlyBase.
DR InterPro; IPR017246; Snapin.
DR InterPro; IPR028119; Snapin/Pallidin/Snn1.
DR PANTHER; PTHR31305; PTHR31305; 1.
DR Pfam; PF14712; Snapin_Pallidin; 1.
DR PIRSF; PIRSF037631; Snapin; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Membrane; Reference proteome.
FT CHAIN 1..134
FT /note="SNAPIN protein homolog"
FT /id="PRO_0000420204"
FT COILED 50..124
FT /evidence="ECO:0000255"
SQ SEQUENCE 134 AA; 15056 MW; B9C3B4E5910B67E0 CRC64;
MDSDSTVTSL EENTENFCTN PTRDILAEGI TNLFKPTIER LDERVASTIQ LQAELRGQLD
ALAAQLRDIE KAQSQIPEFA DKVKELLNVK HKVTVISNVL VTSQERLTGL HKLIEKEQRR
RQALLDSALS TNIS
