AP3D1_MOUSE
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 03-AUG-2022, entry version 171.
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, Pancreas,
RC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 iPTMnet; O54774; -.
DR PhosphoSitePlus; O54774; -.
DR SwissPalm; O54774; -.
DR EPD; O54774; -.
DR jPOST; O54774; -.
DR MaxQB; O54774; -.
DR PaxDb; O54774; -.
DR PeptideAtlas; O54774; -.
DR PRIDE; O54774; -.
DR ProteomicsDB; 296210; -.
DR Antibodypedia; 22913; 101 antibodies from 28 providers.
DR Ensembl; ENSMUST00000020420; ENSMUSP00000020420; ENSMUSG00000020198.
DR GeneID; 11776; -.
DR KEGG; mmu:11776; -.
DR UCSC; uc007gek.1; mouse.
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; YYAAAWI; -.
DR OrthoDB; 598949at2759; -.
DR PhylomeDB; O54774; -.
DR TreeFam; TF105666; -.
DR BioGRID-ORCS; 11776; 6 hits in 75 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 254 other tissues.
DR ExpressionAtlas; O54774; baseline and differential.
DR Genevisible; O54774; MM.
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; IC: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; IC: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; IC:ComplexPortal.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0098943; P:neurotransmitter receptor transport, postsynaptic endosome to lysosome; IDA:SynGO.
DR GO; GO:0060155; P:platelet dense granule organization; IC: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:0061088; P:regulation of sequestering of zinc ion; ISO:MGI.
DR GO; GO:0016182; P:synaptic vesicle budding from endosome; IDA:SynGO.
DR GO; GO:0016183; P:synaptic vesicle coating; IC:ComplexPortal.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; IMP:MGI.
DR GO; GO:0036465; P:synaptic vesicle recycling; IC: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:0006829; P:zinc ion transport; TAS:BHF-UCL.
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 SMART; SM01354; BLVR; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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
