ID   AP3D1_MOUSE             Reviewed;        1199 AA.
AC   O54774;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=AP-3 complex subunit delta-1;
DE   AltName: Full=AP-3 complex subunit delta;
DE   AltName: Full=Adaptor-related protein complex 3 subunit delta-1;
DE   AltName: Full=Delta-adaptin;
DE            Short=mBLVR1;
GN   Name=Ap3d1; Synonyms=Ap3d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   PubMed=9420263; DOI=10.1128/jvi.72.1.593-599.1998;
RA   Suzuki T., Ikeda H.;
RT   "The mouse homolog of the bovine leukemia virus receptor is closely related
RT   to the delta subunit of adaptor-related protein complex AP-3, not
RT   associated with the cell surface.";
RL   J. Virol. 72:593-599(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-755; THR-758;
RP   SER-760; SER-784 AND SER-825, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-634; SER-636;
RP   SER-755; THR-758; SER-760 AND SER-784, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-758 AND SER-760, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-634; SER-754;
RP   SER-755; THR-758; SER-760; SER-784 AND SER-825, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION, AND ASSOCIATION WITH THE BLOC-1 COMPLEX.
RX   PubMed=21998198; DOI=10.1091/mbc.e11-07-0592;
RA   Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B.,
RA   Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
RT   "The schizophrenia susceptibility factor dysbindin and its associated
RT   complex sort cargoes from cell bodies to the synapse.";
RL   Mol. Biol. Cell 22:4854-4867(2011).
CC   -!- FUNCTION: Part of the AP-3 complex, an adaptor-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). Involved in
CC       process of CD8+ T-cell and NK cell degranulation (By similarity). In
CC       concert with the BLOC-1 complex, AP-3 is required to target cargos into
CC       vesicles assembled at cell bodies for delivery into neurites and nerve
CC       terminals (PubMed:21998198). {ECO:0000250|UniProtKB:O14617,
CC       ECO:0000269|PubMed:21998198}.
CC   -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC       of two large adaptins (delta-type subunit AP3D1 and beta-type subunit
CC       AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and
CC       a small adaptin (sigma-type subunit APS1 or AP3S2) (By similarity). AP-
CC       3 associates with the BLOC-1 complex. Interacts with SLC30A2. Interacts
CC       with CLN3 (via dileucine motif); this interaction facilitates lysosomal
CC       targeting (By similarity). {ECO:0000250|UniProtKB:O14617,
CC       ECO:0000250|UniProtKB:Q865S1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AB004305; BAA24578.1; -; mRNA.
DR   EMBL; BC048786; AAH48786.1; -; mRNA.
DR   EMBL; BC053066; AAH53066.1; -; mRNA.
DR   CCDS; CCDS35984.1; -.
DR   PIR; T13946; T13946.
DR   RefSeq; NP_031486.1; NM_007460.1.
DR   AlphaFoldDB; O54774; -.
DR   SMR; O54774; -.
DR   BioGRID; 198134; 25.
DR   ComplexPortal; CPX-5145; Ubiquitous AP-3 Adaptor complex, sigma3a variant.
DR   ComplexPortal; CPX-5146; Ubiquitous AP-3 Adaptor complex, sigma3b variant.
DR   ComplexPortal; CPX-5147; Neuronal AP-3 Adaptor complex, sigma3a variant.
DR   ComplexPortal; CPX-5148; Neuronal AP-3 Adaptor complex, sigma3b variant.
DR   DIP; DIP-32163N; -.
DR   IntAct; O54774; 11.
DR   MINT; O54774; -.
DR   STRING; 10090.ENSMUSP00000020420; -.
DR   GlyGen; O54774; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O54774; -.
DR   MetOSite; O54774; -.
DR   PhosphoSitePlus; O54774; -.
DR   SwissPalm; O54774; -.
DR   EPD; O54774; -.
DR   jPOST; O54774; -.
DR   MaxQB; O54774; -.
DR   PaxDb; 10090-ENSMUSP00000020420; -.
DR   PeptideAtlas; O54774; -.
DR   ProteomicsDB; 296210; -.
DR   Pumba; O54774; -.
DR   Antibodypedia; 22913; 108 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000020420.9; ENSMUSP00000020420.8; ENSMUSG00000020198.9.
DR   GeneID; 11776; -.
DR   KEGG; mmu:11776; -.
DR   UCSC; uc007gek.1; mouse.
DR   AGR; MGI:107734; -.
DR   CTD; 8943; -.
DR   MGI; MGI:107734; Ap3d1.
DR   VEuPathDB; HostDB:ENSMUSG00000020198; -.
DR   eggNOG; KOG1059; Eukaryota.
DR   GeneTree; ENSGT00550000075067; -.
DR   HOGENOM; CLU_001908_0_0_1; -.
DR   InParanoid; O54774; -.
DR   OMA; EQQNNPH; -.
DR   OrthoDB; 2877445at2759; -.
DR   PhylomeDB; O54774; -.
DR   TreeFam; TF105666; -.
DR   BioGRID-ORCS; 11776; 6 hits in 80 CRISPR screens.
DR   ChiTaRS; Ap3d1; mouse.
DR   PRO; PR:O54774; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; O54774; Protein.
DR   Bgee; ENSMUSG00000020198; Expressed in ileal epithelium and 258 other cell types or tissues.
DR   ExpressionAtlas; O54774; baseline and differential.
DR   GO; GO:0030123; C:AP-3 adaptor complex; IBA:GO_Central.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; NAS:ComplexPortal.
DR   GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0098830; C:presynaptic endosome; IDA:SynGO.
DR   GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR   GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR   GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
DR   GO; GO:0019882; P:antigen processing and presentation; IMP:MGI.
DR   GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IMP:MGI.
DR   GO; GO:0035654; P:clathrin-coated vesicle cargo loading, AP-3-mediated; NAS:ComplexPortal.
DR   GO; GO:0035646; P:endosome to melanosome transport; ISO:MGI.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR   GO; GO:0046907; P:intracellular transport; NAS:ComplexPortal.
DR   GO; GO:1903232; P:melanosome assembly; NAS:ComplexPortal.
DR   GO; GO:0098943; P:neurotransmitter receptor transport, postsynaptic endosome to lysosome; IDA:SynGO.
DR   GO; GO:0060155; P:platelet dense granule organization; NAS:ComplexPortal.
DR   GO; GO:0051138; P:positive regulation of NK T cell differentiation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0072657; P:protein localization to membrane; ISO:MGI.
DR   GO; GO:0033365; P:protein localization to organelle; IMP:MGI.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   GO; GO:0016182; P:synaptic vesicle budding from endosome; IDA:SynGO.
DR   GO; GO:0016183; P:synaptic vesicle coating; NAS:ComplexPortal.
DR   GO; GO:0048499; P:synaptic vesicle membrane organization; IMP:MGI.
DR   GO; GO:0036465; P:synaptic vesicle recycling; NAS:ComplexPortal.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
DR   GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR   GO; GO:0140916; P:zinc ion import into lysosome; ISO:MGI.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.30.450.50; Longin domain; 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:SF12; AP-3 COMPLEX SUBUNIT DELTA-1; 1.
DR   PANTHER; PTHR22781; DELTA ADAPTIN-RELATED; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF06375; AP3D1; 1.
DR   SMART; SM01354; BLVR; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   Genevisible; O54774; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O14617"
FT   CHAIN           2..1199
FT                   /note="AP-3 complex subunit delta-1"
FT                   /id="PRO_0000193767"
FT   REPEAT          34..71
FT                   /note="HEAT 1"
FT   REPEAT          142..179
FT                   /note="HEAT 2"
FT   REPEAT          180..216
FT                   /note="HEAT 3"
FT   REPEAT          218..254
FT                   /note="HEAT 4"
FT   REPEAT          257..296
FT                   /note="HEAT 5"
FT   REPEAT          298..336
FT                   /note="HEAT 6"
FT   REPEAT          337..373
FT                   /note="HEAT 7"
FT   REPEAT          375..409
FT                   /note="HEAT 8"
FT   REPEAT          521..558
FT                   /note="HEAT 9"
FT   REGION          623..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          659..679
FT                   /evidence="ECO:0000255"
FT   COILED          722..750
FT                   /evidence="ECO:0000255"
FT   COILED          843..863
FT                   /evidence="ECO:0000255"
FT   COILED          911..934
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        633..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..751
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..769
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..838
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..864
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..916
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..946
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O14617"
FT   MOD_RES         632
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         634
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         636
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14617"
FT   MOD_RES         754
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         755
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         758
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         760
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         784
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         825
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1199 AA;  135081 MW;  29D2D036B36C3B05 CRC64;
     MALKMVKGSI DRMFDKNLQD LVRGIRNHKE DEAKYISQCI DEIKQELKQD NIAVKANAVC
     KLTYLQMLGY DISWAAFNII EVMSASKFTF KRVGYLAASQ CFHEGTDVIM LTTNQIRKDL
     SSPSQYDTGV ALTGLSCFVT PDLARDLAND IMTLMSHTKP YIRKKAVLIM YKVFLKYPES
     LRPAFPRLKE KLEDPDPGVQ SAAVNVICEL ARRNPKNYLS LAPLFFKLMT SSTNNWVLIK
     IIKLFGALTP LEPRLGKKLI EPLTNLIHST SAMSLLYECV NTVIAVLISL SSGMPNHSAS
     IQLCVQKLRI LIEDSDQNLK YLGLLAMSKI LKTHPKSVQS HKDLILQCLD DKDESIRLRA
     LDLLYGMVSK KNLMEIVKKL MTHVDKAEGT TYRDELLTKI IDICSQSNYQ HITNFEWYIS
     ILVELTRLEG TRHGHLIAAQ MLDVAIRVKA IRKFAVSQMS SLLDSAHLVA SSTQRNGICE
     VLYAAAWICG EFSEHLQGPQ QTLEAMLRPK VTTLPGHIQA VYVQNVVKLY ASILQQKEQA
     ADTEAAQEVT QLLVERLPQF VQSADLEVQE RASCILQLVK HVQKLQAKGV PVAEEVSALF
     AGELNPVAPK AQKKVPVPEG LDLDAWINEP PSDSESEDEK PKAIFHEEEP RHTRRRQPEE
     DEEELARRRE ARKQEQANNP FYIKSSPSPQ KRYQDAPGVE HIPVVQIDLS VPLKVPGMPM
     SDQYVKLEEQ RRHRQRLEKD KKRKKKEKGK RRHSSLPTES DEDIAPAQRV DIITEEMPEN
     ALPSDEDDKD PNDPYRALDI DLDKPLADSE KLPVQKHRNA EAVKSPEKEG VLGVEKKSKK
     PKKKEKKTKE REREKKDKKG EDLDFWLSTT PPPAAAPIPA PSTEELAAST ITSPKDECEV
     LKGEEEDHVD HDQERKSSRH KKKKHRKEKE KEERPRDKKK AKKKQVAPLE NGAAAEEEEE
     PIPPMSSYCL LAESPYIKVT YDIQASLQKD SQVTVSIILE NQSSSFLKNM ELNVLDSLNT
     KMTRPEGSSV HDGVPVPFQL PPGVSNEAQF VFTIQSIVMA QKLKGTLSFI AKDDEGATHE
     KLDFRLHFSC SSYLITTPCY SDAFAKLLES GDLSMNSIKV DGISMSFQNL LAKICFYHHF
     SVVERVDSCA SMYSRSIQGH HVCLLVKKGE SSVSVDGKCS DATLLSSLLE EMKTTLAQC
//