ID   AP3D1_HUMAN             Reviewed;        1153 AA.
AC   O14617; O00202; O75262; Q59HF5; Q96G11; Q9H3C6;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 214.
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;
GN   Name=AP3D1; ORFNames=PRO0039;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   TISSUE=Fetal brain;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=9151686; DOI=10.1083/jcb.137.4.835;
RA   Simpson F., Peden A.A., Christopoulou L., Robinson M.S.;
RT   "Characterization of the adaptor-related protein complex, AP-3.";
RL   J. Cell Biol. 137:835-845(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 74-603 (ISOFORM 1).
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W.,
RA   Gao F., Liu M., He F.;
RT   "Functional prediction of the coding sequences of 75 new genes deduced by
RT   analysis of cDNA clones from human fetal liver.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   INTERACTION WITH CLN3.
RX   PubMed=15598649; DOI=10.1074/jbc.m411862200;
RA   Kyttaelae A., Yliannala K., Schu P., Jalanko A., Luzio J.P.;
RT   "AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein
RT   CLN3 via its dileucine motif.";
RL   J. Biol. Chem. 280:10277-10283(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-634; SER-636 AND
RP   SER-658, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688; SER-758; SER-759;
RP   THR-762; SER-764 AND SER-788, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP   SER-828 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931
RP   (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-634; SER-636;
RP   SER-788 AND SER-829, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632 AND SER-658, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658 AND SER-829, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-634; SER-636 AND
RP   SER-788, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785 (ISOFORM 2), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   INTERACTION WITH SLC30A2.
RX   PubMed=25808614; DOI=10.1002/jcp.24992;
RA   Hennigar S.R., Kelleher S.L.;
RT   "TNFalpha post-translationally targets ZnT2 to accumulate zinc in
RT   lysosomes.";
RL   J. Cell. Physiol. 230:2345-2350(2015).
RN   [18]
RP   FUNCTION, AND INVOLVEMENT IN HPS10.
RX   PubMed=26744459; DOI=10.1182/blood-2015-09-671636;
RA   Ammann S., Schulz A., Kraegeloh-Mann I., Dieckmann N.M., Niethammer K.,
RA   Fuchs S., Eckl K.M., Plank R., Werner R., Altmueller J., Thiele H.,
RA   Nuernberg P., Bank J., Strauss A., von Bernuth H., Zur Stadt U., Grieve S.,
RA   Griffiths G.M., Lehmberg K., Hennies H.C., Ehl S.;
RT   "Mutations in AP3D1 associated with immunodeficiency and seizures define a
RT   new type of Hermansky-Pudlak syndrome.";
RL   Blood 127:997-1006(2016).
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. Involved in process of CD8+ T-
CC       cell and NK cell degranulation (PubMed:26744459). In concert with the
CC       BLOC-1 complex, AP-3 is required to target cargos into vesicles
CC       assembled at cell bodies for delivery into neurites and nerve terminals
CC       (By similarity). {ECO:0000250|UniProtKB:O54774,
CC       ECO:0000269|PubMed:26744459}.
CC   -!- SUBUNIT: AP-3 associates with the BLOC-1 complex (By similarity).
CC       Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two
CC       large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or
CC       AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small
CC       adaptin (sigma-type subunit APS1 or AP3S2) (By similarity). Interacts
CC       with SLC30A2 (PubMed:25808614). Interacts with CLN3 (via dileucine
CC       motif); this interaction facilitates lysosomal targeting
CC       (PubMed:15598649). {ECO:0000250|UniProtKB:Q865S1,
CC       ECO:0000269|PubMed:15598649, ECO:0000269|PubMed:25808614}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=O14617-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O14617-2; Sequence=VSP_000165, VSP_000166;
CC       Name=3;
CC         IsoId=O14617-3; Sequence=VSP_000167;
CC       Name=4;
CC         IsoId=O14617-4; Sequence=VSP_000168;
CC       Name=5;
CC         IsoId=O14617-5; Sequence=VSP_017106;
CC   -!- TISSUE SPECIFICITY: Present in all adult tissues examined with the
CC       highest levels in skeletal muscle, heart, pancreas and testis.
CC       {ECO:0000269|PubMed:9151686}.
CC   -!- DISEASE: Hermansky-Pudlak syndrome 10 (HPS10) [MIM:617050]: A form of
CC       Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal
CC       recessive disorder characterized by oculocutaneous albinism, bleeding
CC       due to platelet storage pool deficiency, and lysosomal storage defects.
CC       This syndrome results from defects of diverse cytoplasmic organelles
CC       including melanosomes, platelet dense granules and lysosomes. Ceroid
CC       storage in the lungs is associated with pulmonary fibrosis, a common
CC       cause of premature death in individuals with HPS. HPS10 patients
CC       manifest albinism, neutropenia, immunodeficiency, neurodevelopmental
CC       delay, generalized seizures, and impaired hearing.
CC       {ECO:0000269|PubMed:26744459}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG35473.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Presence of an unrelated sequence found on chromosome 7.; Evidence={ECO:0000305};
CC       Sequence=AAH10065.1; Type=Miscellaneous discrepancy; Note=Lack of 8 exons and truncation of 2 other exons in the C- terminus. Alternative splicing seems doubtful, since exon-intron junctions are not the consensus ones.; Evidence={ECO:0000305};
CC       Sequence=BAD92041.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AF002163; AAC51761.1; -; mRNA.
DR   EMBL; U91930; AAD03777.1; -; mRNA.
DR   EMBL; AB208804; BAD92041.1; ALT_INIT; mRNA.
DR   EMBL; AC005545; AAC34212.1; -; Genomic_DNA.
DR   EMBL; AC005545; AAC34214.1; -; Genomic_DNA.
DR   EMBL; BC010065; AAH10065.1; ALT_SEQ; mRNA.
DR   EMBL; AF130042; AAG35473.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS42459.1; -. [O14617-1]
DR   CCDS; CCDS58638.1; -. [O14617-5]
DR   RefSeq; NP_001248755.1; NM_001261826.1. [O14617-5]
DR   RefSeq; NP_003929.4; NM_003938.6. [O14617-1]
DR   PDB; 4AFI; X-ray; 2.80 A; A/B=680-729.
DR   PDBsum; 4AFI; -.
DR   AlphaFoldDB; O14617; -.
DR   SMR; O14617; -.
DR   BioGRID; 114455; 139.
DR   ComplexPortal; CPX-5051; Ubiquitous AP-3 Adaptor complex, sigma3a variant.
DR   ComplexPortal; CPX-5052; Ubiquitous AP-3 Adaptor complex, sigma3b variant.
DR   ComplexPortal; CPX-5053; Neuronal AP-3 Adaptor complex, sigma3b variant.
DR   ComplexPortal; CPX-5055; Neuronal AP-3 Adaptor complex, sigma3a variant.
DR   CORUM; O14617; -.
DR   DIP; DIP-46793N; -.
DR   IntAct; O14617; 72.
DR   MINT; O14617; -.
DR   STRING; 9606.ENSP00000495274; -.
DR   GlyGen; O14617; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O14617; -.
DR   MetOSite; O14617; -.
DR   PhosphoSitePlus; O14617; -.
DR   SwissPalm; O14617; -.
DR   BioMuta; AP3D1; -.
DR   EPD; O14617; -.
DR   jPOST; O14617; -.
DR   MassIVE; O14617; -.
DR   MaxQB; O14617; -.
DR   PaxDb; 9606-ENSP00000347416; -.
DR   PeptideAtlas; O14617; -.
DR   ProteomicsDB; 48117; -. [O14617-1]
DR   ProteomicsDB; 48118; -. [O14617-2]
DR   ProteomicsDB; 48119; -. [O14617-3]
DR   ProteomicsDB; 48120; -. [O14617-4]
DR   ProteomicsDB; 48121; -. [O14617-5]
DR   Pumba; O14617; -.
DR   Antibodypedia; 22913; 108 antibodies from 28 providers.
DR   DNASU; 8943; -.
DR   Ensembl; ENST00000345016.9; ENSP00000344055.4; ENSG00000065000.20. [O14617-1]
DR   Ensembl; ENST00000643116.3; ENSP00000495274.2; ENSG00000065000.20. [O14617-5]
DR   GeneID; 8943; -.
DR   KEGG; hsa:8943; -.
DR   MANE-Select; ENST00000643116.3; ENSP00000495274.2; NM_001261826.3; NP_001248755.1. [O14617-5]
DR   UCSC; uc002luz.4; human. [O14617-1]
DR   AGR; HGNC:568; -.
DR   DisGeNET; 8943; -.
DR   GeneCards; AP3D1; -.
DR   GeneReviews; AP3D1; -.
DR   HGNC; HGNC:568; AP3D1.
DR   HPA; ENSG00000065000; Low tissue specificity.
DR   MalaCards; AP3D1; -.
DR   MIM; 607246; gene.
DR   MIM; 617050; phenotype.
DR   neXtProt; NX_O14617; -.
DR   OpenTargets; ENSG00000065000; -.
DR   Orphanet; 1000; Ocular albinism with late-onset sensorineural deafness.
DR   Orphanet; 54; X-linked recessive ocular albinism.
DR   PharmGKB; PA24859; -.
DR   VEuPathDB; HostDB:ENSG00000065000; -.
DR   eggNOG; KOG1059; Eukaryota.
DR   GeneTree; ENSGT00550000075067; -.
DR   HOGENOM; CLU_001908_0_0_1; -.
DR   InParanoid; O14617; -.
DR   OMA; EQQNNPH; -.
DR   OrthoDB; 2877445at2759; -.
DR   PhylomeDB; O14617; -.
DR   TreeFam; TF105666; -.
DR   PathwayCommons; O14617; -.
DR   SignaLink; O14617; -.
DR   SIGNOR; O14617; -.
DR   BioGRID-ORCS; 8943; 29 hits in 1159 CRISPR screens.
DR   ChiTaRS; AP3D1; human.
DR   GeneWiki; AP3D1; -.
DR   GenomeRNAi; 8943; -.
DR   Pharos; O14617; Tbio.
DR   PRO; PR:O14617; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O14617; Protein.
DR   Bgee; ENSG00000065000; Expressed in tendon of biceps brachii and 208 other cell types or tissues.
DR   ExpressionAtlas; O14617; baseline and differential.
DR   GO; GO:0030123; C:AP-3 adaptor complex; IBA:GO_Central.
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; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0098830; C:presynaptic endosome; IBA:GO_Central.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR   GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR   GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IEA:Ensembl.
DR   GO; GO:0035654; P:clathrin-coated vesicle cargo loading, AP-3-mediated; NAS:ComplexPortal.
DR   GO; GO:0035646; P:endosome to melanosome transport; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR   GO; GO:0046907; P:intracellular transport; NAS:ComplexPortal.
DR   GO; GO:1903232; P:melanosome assembly; NAS:ComplexPortal.
DR   GO; GO:0032438; P:melanosome organization; IC:ParkinsonsUK-UCL.
DR   GO; GO:0098943; P:neurotransmitter receptor transport, postsynaptic endosome to lysosome; IBA:GO_Central.
DR   GO; GO:0060155; P:platelet dense granule organization; NAS:ComplexPortal.
DR   GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0072657; P:protein localization to membrane; IMP:ParkinsonsUK-UCL.
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:0016183; P:synaptic vesicle coating; NAS:ComplexPortal.
DR   GO; GO:0048499; P:synaptic vesicle membrane organization; IBA:GO_Central.
DR   GO; GO:0036465; P:synaptic vesicle recycling; NAS:ComplexPortal.
DR   GO; GO:0016192; P:vesicle-mediated transport; NAS:ComplexPortal.
DR   GO; GO:0140916; P:zinc ion import into lysosome; IMP:BHF-UCL.
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; O14617; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Albinism; Alternative splicing; Coiled coil;
KW   Cytoplasm; Golgi apparatus; Hermansky-Pudlak syndrome; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1153
FT                   /note="AP-3 complex subunit delta-1"
FT                   /id="PRO_0000193766"
FT   REPEAT          34..71
FT                   /note="HEAT 1"
FT   REPEAT          77..114
FT                   /note="HEAT 2"
FT   REPEAT          142..179
FT                   /note="HEAT 3"
FT   REPEAT          180..216
FT                   /note="HEAT 4"
FT   REPEAT          254..292
FT                   /note="HEAT 5"
FT   REPEAT          299..336
FT                   /note="HEAT 6"
FT   REPEAT          338..373
FT                   /note="HEAT 7"
FT   REPEAT          375..409
FT                   /note="HEAT 8"
FT   REPEAT          431..468
FT                   /note="HEAT 9"
FT   REPEAT          497..535
FT                   /note="HEAT 10"
FT   REPEAT          548..585
FT                   /note="HEAT 11"
FT   REGION          629..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          659..679
FT                   /evidence="ECO:0000255"
FT   COILED          725..756
FT                   /evidence="ECO:0000255"
FT   COILED          845..869
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        633..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..693
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..754
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..886
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         632
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         634
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT   MOD_RES         636
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT   MOD_RES         658
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         758
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         759
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         762
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         764
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         788
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT   MOD_RES         829
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         117..285
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9303295"
FT                   /id="VSP_000167"
FT   VAR_SEQ         168..258
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9151686,
FT                   ECO:0000303|PubMed:9303295"
FT                   /id="VSP_000165"
FT   VAR_SEQ         746..877
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9303295"
FT                   /id="VSP_000168"
FT   VAR_SEQ         866
FT                   /note="K -> KKAEDLDFWLSTTPPPAPAPAPAPVPSTDECEDAKTEAQGEEDDAEG
FT                   QDQD (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9151686,
FT                   ECO:0000303|PubMed:9303295"
FT                   /id="VSP_000166"
FT   VAR_SEQ         866
FT                   /note="K -> KKAEDLDFWLSTTPPPAPAPAPAPVPSTGELSVNTVTTPKDECEDAK
FT                   TEAQGEEDDAEGQDQD (in isoform 5)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_017106"
FT   VARIANT         541
FT                   /note="G -> R (in dbSNP:rs34569645)"
FT                   /id="VAR_033517"
FT   VARIANT         1072
FT                   /note="I -> V (in dbSNP:rs25673)"
FT                   /id="VAR_033518"
FT   CONFLICT        3
FT                   /note="L -> F (in Ref. 2; AAD03777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="Missing (in Ref. 4; AAC34214)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252
FT                   /note="E -> G (in Ref. 5; AAH10065)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595..603
FT                   /note="EVSALFAGE -> DFVHCCYEL (in Ref. 6; AAG35473)"
FT                   /evidence="ECO:0000305"
FT   STRAND          704..706
FT                   /evidence="ECO:0007829|PDB:4AFI"
FT   STRAND          722..728
FT                   /evidence="ECO:0007829|PDB:4AFI"
FT   MOD_RES         O14617-2:785
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         O14617-2:828
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         O14617-5:931
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
SQ   SEQUENCE   1153 AA;  130158 MW;  1B491DD64EAD5096 CRC64;
     MALKMVKGSI DRMFDKNLQD LVRGIRNHKE DEAKYISQCI DEIKQELKQD NIAVKANAVC
     KLTYLQMLGY DISWAAFNII EVMSASKFTF KRIGYLAASQ SFHEGTDVIM 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 YITNFEWYIS
     ILVELTRLEG TRHGHLIAAQ MLDVAIRVKA IRKFAVSQMS ALLDSAHLLA SSTQRNGICE
     VLYAAAWICG EFSEHLQEPH HTLEAMLRPR VTTLPGHIQA VYVQNVVKLY ASILQQKEQA
     GEAEGAQAVT QLMVDRLPQF VQSADLEVQE RASCILQLVK HIQKLQAKDV PVAEEVSALF
     AGELNPVAPK AQKKVPVPEG LDLDAWINEP LSDSESEDER PRAVFHEEEQ RRPKHRPSEA
     DEEELARRRE ARKQEQANNP FYIKSSPSPQ KRYQDTPGVE HIPVVQIDLS VPLKVPGLPM
     SDQYVKLEEE RRHRQKLEKD KRRKKRKEKE KKGKRRHSSL PTESDEDIAP AQQVDIVTEE
     MPENALPSDE DDKDPNDPYR ALDIDLDKPL ADSEKLPIQK HRNTETSKSP EKDVPMVEKK
     SKKPKKKEKK HKEKERDKEK KKEKEKKKSP KPKKKKHRKE KEERTKGKKK SKKQPPGSEE
     AAGEPVQNGA PEEEQLPPES SYSLLAENSY VKMTCDIRGS LQEDSQVTVA IVLENRSSSI
     LKGMELSVLD SLNARMARPQ GSSVHDGVPV PFQLPPGVSN EAQYVFTIQS IVMAQKLKGT
     LSFIAKNDEG ATHEKLDFRL HFSCSSYLIT TPCYSDAFAK LLESGDLSMS SIKVDGIRMS
     FQNLLAKICF HHHFSVVERV DSCASMYSRS IQGHHVCLLV KKGENSVSVD GKCSDSTLLS
     NLLEEMKATL AKC
//