AP3D1_HUMAN
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 03-AUG-2022, entry version 205.
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};
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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; 101.
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; 66.
DR MINT; O14617; -.
DR STRING; 9606.ENSP00000347416; -.
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; O14617; -.
DR PeptideAtlas; O14617; -.
DR PRIDE; 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 Antibodypedia; 22913; 101 antibodies from 28 providers.
DR DNASU; 8943; -.
DR Ensembl; ENST00000345016.9; ENSP00000344055.4; ENSG00000065000.19. [O14617-1]
DR Ensembl; ENST00000643116.3; ENSP00000495274.2; ENSG00000065000.19. [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 CTD; 8943; -.
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; YYAAAWI; -.
DR OrthoDB; 598949at2759; -.
DR PhylomeDB; O14617; -.
DR TreeFam; TF105666; -.
DR PathwayCommons; O14617; -.
DR SignaLink; O14617; -.
DR SIGNOR; O14617; -.
DR BioGRID-ORCS; 8943; 27 hits in 1081 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 206 other tissues.
DR ExpressionAtlas; O14617; baseline and differential.
DR Genevisible; O14617; HS.
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; IC: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; IC: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; IC:ComplexPortal.
DR GO; GO:1903232; P:melanosome assembly; IC: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; IC: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:0061088; P:regulation of sequestering of zinc ion; IMP:BHF-UCL.
DR GO; GO:0016182; P:synaptic vesicle budding from endosome; IBA:GO_Central.
DR GO; GO:0016183; P:synaptic vesicle coating; IC:ComplexPortal.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; IBA:GO_Central.
DR GO; GO:0036465; P:synaptic vesicle recycling; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IC:ComplexPortal.
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 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
