AP3D_DROME
ID AP3D_DROME Reviewed; 1034 AA.
AC P54362; O16015; O45031; Q9VY96;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=AP-3 complex subunit delta;
DE AltName: Full=Delta adaptin subunit of AP-3;
DE Short=Delta-adaptin;
DE AltName: Full=Garnet protein;
GN Name=g; ORFNames=CG10986;
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 [MRNA].
RC STRAIN=Canton-S;
RX PubMed=9303295; DOI=10.1093/emboj/16.15.4508;
RA Ooi C.E., Moreira J.E., Dell'Angelica E.C., Poy G., Wassarman D.A.,
RA Bonifacino J.S.;
RT "Altered expression of a novel adaptin leads to defective pigment granule
RT biogenesis in the Drosophila eye color mutant garnet.";
RL EMBO J. 16:4508-4518(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Oregon-R;
RX PubMed=10659786; DOI=10.1139/gen-42-6-1183;
RA Lloyd V.K., Sinclair D.A., Wennberg R., Warner T.S., Honda B.M.,
RA Grigliatti T.A.;
RT "A genetic and molecular characterization of the garnet gene of Drosophila
RT melanogaster.";
RL Genome 42:1183-1193(1999).
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683 AND THR-687, 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: Part of the AP-3 complex, an adapter-related complex which is
CC not clathrin-associated. The complex is associated with the Golgi
CC region as well as more peripheral structures. It facilitates the
CC budding of vesicles from the Golgi membrane and may be directly
CC involved in trafficking to lysosomes (By similarity). {ECO:0000250}.
CC -!- FUNCTION: May be a coat protein involved in the formation of
CC specialized structures like pigment granules.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of two large chains (delta and beta3), a medium chain (mu3) and a small
CC chain (sigma3).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles located at the Golgi complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB97618.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at 5'- and 3'-ends and extensively differs from that shown at positions 1-269, 546 and 840-1034.; Evidence={ECO:0000305};
CC Sequence=AAC01743.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at 5'- and 3'-ends and extensively differs from that shown at positions 1-269, 546 and 840-1034.; Evidence={ECO:0000305};
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DR EMBL; AF002164; AAC14585.1; -; mRNA.
DR EMBL; AF044287; AAC01743.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U31351; AAB97618.1; ALT_SEQ; mRNA.
DR EMBL; AE014298; AAF48307.2; -; Genomic_DNA.
DR RefSeq; NP_524785.2; NM_080046.3.
DR AlphaFoldDB; P54362; -.
DR SMR; P54362; -.
DR BioGRID; 69305; 10.
DR IntAct; P54362; 4.
DR STRING; 7227.FBpp0073673; -.
DR iPTMnet; P54362; -.
DR PaxDb; P54362; -.
DR PRIDE; P54362; -.
DR EnsemblMetazoa; FBtr0073842; FBpp0073673; FBgn0001087.
DR GeneID; 44819; -.
DR KEGG; dme:Dmel_CG10986; -.
DR UCSC; CG10986-RB; d. melanogaster.
DR CTD; 44819; -.
DR FlyBase; FBgn0001087; g.
DR VEuPathDB; VectorBase:FBgn0001087; -.
DR eggNOG; KOG1059; Eukaryota.
DR GeneTree; ENSGT00550000075067; -.
DR HOGENOM; CLU_001908_0_1_1; -.
DR InParanoid; P54362; -.
DR PhylomeDB; P54362; -.
DR SignaLink; P54362; -.
DR BioGRID-ORCS; 44819; 0 hits in 1 CRISPR screen.
DR ChiTaRS; g; fly.
DR GenomeRNAi; 44819; -.
DR PRO; PR:P54362; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0001087; Expressed in wing disc and 25 other tissues.
DR ExpressionAtlas; P54362; baseline and differential.
DR Genevisible; P54362; DM.
DR GO; GO:0030123; C:AP-3 adaptor complex; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IDA:FlyBase.
DR GO; GO:0005798; C:Golgi-associated vesicle; NAS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:FlyBase.
DR GO; GO:0098830; C:presynaptic endosome; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0140312; F:cargo adaptor activity; ISS:FlyBase.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IBA:GO_Central.
DR GO; GO:0048072; P:compound eye pigmentation; IGI:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0006887; P:exocytosis; IMP:FlyBase.
DR GO; GO:0006726; P:eye pigment biosynthetic process; IDA:FlyBase.
DR GO; GO:0008057; P:eye pigment granule organization; IMP:UniProtKB.
DR GO; GO:0006895; P:Golgi to endosome transport; NAS:UniProtKB.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; TAS:FlyBase.
DR GO; GO:0007041; P:lysosomal transport; TAS:FlyBase.
DR GO; GO:1900369; P:negative regulation of post-transcriptional gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0098943; P:neurotransmitter receptor transport, postsynaptic endosome to lysosome; IBA:GO_Central.
DR GO; GO:0007220; P:Notch receptor processing; IMP:FlyBase.
DR GO; GO:0008055; P:ocellus pigment biosynthetic process; IDA:FlyBase.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IMP:FlyBase.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0016182; P:synaptic vesicle budding from endosome; IBA:GO_Central.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR017105; AP3_complex_dsu.
DR InterPro; IPR010474; AP3D_dom_metazoa.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR PANTHER; PTHR22781; PTHR22781; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF06375; AP3D1; 1.
DR PIRSF; PIRSF037092; AP3_complex_delta; 1.
DR SMART; SM01354; BLVR; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1034
FT /note="AP-3 complex subunit delta"
FT /id="PRO_0000193768"
FT REPEAT 35..72
FT /note="HEAT 1"
FT REPEAT 143..180
FT /note="HEAT 2"
FT REPEAT 181..217
FT /note="HEAT 3"
FT REPEAT 219..255
FT /note="HEAT 4"
FT REPEAT 258..297
FT /note="HEAT 5"
FT REPEAT 299..337
FT /note="HEAT 6"
FT REPEAT 338..374
FT /note="HEAT 7"
FT REPEAT 376..414
FT /note="HEAT 8"
FT REPEAT 415..452
FT /note="HEAT 9"
FT REPEAT 570..609
FT /note="HEAT 10"
FT REGION 637..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..784
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 395
FT /note="D -> T (in Ref. 2; AAC01743)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="L -> V (in Ref. 2; AAC01743)"
FT /evidence="ECO:0000305"
FT CONFLICT 442..445
FT /note="QLLD -> RTTY (in Ref. 2; AAC01743)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..465
FT /note="MTNLL -> IDQSA (in Ref. 2; AAC01743)"
FT /evidence="ECO:0000305"
FT CONFLICT 694..695
FT /note="QR -> GQ (in Ref. 2; AAC01743)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="E -> D (in Ref. 1; AAC14585)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="L -> S (in Ref. 3; AAF48307)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="P -> S (in Ref. 3; AAF48307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1034 AA; 114846 MW; ECE1B7A34DC5F8F1 CRC64;
MALKKVKGNF FERMFDKNLT DLVRGIRNNK DNEAKYISTC IEEIKQELRQ DNISVKCNAV
AKLTYIQMLG YDISWAGFNI IEVMSSSRFT CKRIGYLAAS QCFHPDSELL MLTTNMIRKD
LNSQNQYDAG VALSGLSCFI SPDLSRDLAN DIMTLMSSTK PYLRMKAVLM MYKVFLRYPE
ALRPAFPKLK EKLEDPDPGV QSAAVNVICE LARKNPKNYL PLAPIFFKLM TTSTNNWMLI
KIIKLFGALT PLEPRLGKKL IEPLTNLIHS TSAMSLLYEC INTVIAVLIS ISSGMPNHSA
SIQLCVQKLR ILIEDSDQNL KYLGLLAMSK ILKTHPKSVQ AHKDLILACL DDKDESIRLR
ALDLLYGMVS KKNLMEIVKR LLGHMERAEG SAYRDELLYK VIEICAQSSY LYVTNFEWYL
TVLVELIQLE AGSRHGRLIA EQLLDVAIRV PVVRQFAVNE MTNLLDTFTV SAQSNSMYEV
LYAAAWIVGE FAGELEDAEK TLNILLRPRL LPGHIQGVYV QNVIKLFARL ATTCLELQDL
PGLVTLCDHV LDKLQHFNGS SDIEVQERAN SACMLIEMLR NQLSTSTDAM AMDTTTEGGI
PPLAIEIVQE MTLLFTGELI PVAPKAQRKV PLPDGLDLDE WINAPPPEDA ASSSSSEHDK
DELFVSATQA GTGADGGEKR RQSLELTPEQ LERQRMARLI EQSNNPHYLK STPTASGASN
ADQYDNIDDI PITELPLDME GVAALRVGIT KRSDKYLQEQ QAAQGSKDGK KKHKKGKKSK
KAKNKVAYNS SSESEGEPKP LHIVNTTLDM PEGVSMSDSE DKDGKYDPND PHRALDIELD
ITEFEAPAVR SASKKSAADK ENLKTPADLA GGGNAAKKDR KKDKDKDKER KVKREHRESK
RERKEAAVQP VIDLIDADTP TPSPSHISAT SNNNNTSTVL PDAPKHHKKK KNKEKTTDEA
PDALATATGS SIIDVGGEEA SEVASKVHKK KHKKEKSQRK EKKKASESAS VSAIVSIGDY
EQPLGISTPS KEIL
