AP3D_ARATH
ID AP3D_ARATH Reviewed; 869 AA.
AC Q9C744;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=AP-3 complex subunit delta;
DE AltName: Full=Adaptor-related protein complex 3 subunit delta;
DE AltName: Full=Delta-adaptin;
DE Short=At-d-Ad;
DE Short=At-delta-Ad;
DE AltName: Full=Protein-affected trafficking 4;
GN Name=DELTA-ADR; Synonyms=PAT4; OrderedLocusNames=At1g48760;
GN ORFNames=F11I4.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND REVIEW.
RX PubMed=11598180; DOI=10.1091/mbc.12.10.2907;
RA Boehm M., Bonifacino J.S.;
RT "Adaptins: the final recount.";
RL Mol. Biol. Cell 12:2907-2920(2001).
RN [5]
RP INTERACTION WITH EPSIN2, AND SUBCELLULAR LOCATION.
RX PubMed=17277094; DOI=10.1104/pp.106.095349;
RA Lee G.-J., Kim H., Kang H., Jang M., Lee D.W., Lee S., Hwang I.;
RT "EpsinR2 interacts with clathrin, adaptor protein-3, AtVTI12, and
RT phosphatidylinositol-3-phosphate. Implications for EpsinR2 function in
RT protein trafficking in plant cells.";
RL Plant Physiol. 143:1561-1575(2007).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=19884248; DOI=10.1093/pcp/pcp137;
RA Niihama M., Takemoto N., Hashiguchi Y., Tasaka M., Morita M.T.;
RT "ZIP genes encode proteins involved in membrane trafficking of the TGN-
RT PVC/vacuoles.";
RL Plant Cell Physiol. 50:2057-2068(2009).
RN [7]
RP MUTANT PAT4, DISRUPTION PHENOTYPE, FUNCTION, AND COMPONENT OF THE AP-3
RP COMPLEX.
RX PubMed=21670741; DOI=10.1038/cr.2011.99;
RA Zwiewka M., Feraru E., Moeller B., Hwang I., Feraru M.I., Kleine-Vehn J.,
RA Weijers D., Friml J.;
RT "The AP-3 adaptor complex is required for vacuolar function in
RT Arabidopsis.";
RL Cell Res. 21:1711-1722(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex which
CC seems to be clathrin-associated. The complex is associated with the
CC Golgi 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 the vacuole. It also function in maintaining
CC the identity of lytic vacuoles and in regulating the transition between
CC storage and lytic vacuoles. {ECO:0000269|PubMed:21670741}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of two large adaptins (delta-type subunit and beta-type subunit), a
CC medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC subunit). Binds to EPSIN2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Localizes also to a novel cellular
CC compartment, the 'delta compartment', characterized by colocalization
CC of EPSIN2 and DELTA-ADR. {ECO:0000269|PubMed:17277094}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype except defective lytic
CC vacuoles with altered morphology and accumulation of proteins.
CC {ECO:0000269|PubMed:19884248, ECO:0000269|PubMed:21670741}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; AC073555; AAG60121.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32345.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32346.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32347.1; -; Genomic_DNA.
DR EMBL; AY056123; AAL07009.1; -; mRNA.
DR RefSeq; NP_001031156.1; NM_001036079.1.
DR RefSeq; NP_175308.1; NM_103771.2.
DR RefSeq; NP_849785.1; NM_179454.1.
DR AlphaFoldDB; Q9C744; -.
DR SMR; Q9C744; -.
DR BioGRID; 26523; 2.
DR IntAct; Q9C744; 1.
DR STRING; 3702.AT1G48760.2; -.
DR iPTMnet; Q9C744; -.
DR PaxDb; Q9C744; -.
DR PRIDE; Q9C744; -.
DR ProteomicsDB; 244405; -.
DR EnsemblPlants; AT1G48760.1; AT1G48760.1; AT1G48760.
DR EnsemblPlants; AT1G48760.2; AT1G48760.2; AT1G48760.
DR EnsemblPlants; AT1G48760.3; AT1G48760.3; AT1G48760.
DR GeneID; 841298; -.
DR Gramene; AT1G48760.1; AT1G48760.1; AT1G48760.
DR Gramene; AT1G48760.2; AT1G48760.2; AT1G48760.
DR Gramene; AT1G48760.3; AT1G48760.3; AT1G48760.
DR KEGG; ath:AT1G48760; -.
DR Araport; AT1G48760; -.
DR TAIR; locus:2008129; AT1G48760.
DR eggNOG; KOG1059; Eukaryota.
DR HOGENOM; CLU_001908_4_0_1; -.
DR InParanoid; Q9C744; -.
DR OMA; VCDHMRR; -.
DR OrthoDB; 598949at2759; -.
DR PhylomeDB; Q9C744; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q9C744; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C744; baseline and differential.
DR Genevisible; Q9C744; AT.
DR GO; GO:0030123; C:AP-3 adaptor complex; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0007032; P:endosome organization; IMP:TAIR.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IMP:TAIR.
DR GO; GO:0080171; P:lytic vacuole organization; IMP:TAIR.
DR GO; GO:1990019; P:protein storage vacuole organization; IMP:TAIR.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0006903; P:vesicle targeting; IEP:TAIR.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR017105; AP3_complex_dsu.
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 PIRSF; PIRSF037092; AP3_complex_delta; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..869
FT /note="AP-3 complex subunit delta"
FT /id="PRO_0000397854"
FT REPEAT 33..70
FT /note="HEAT 1"
FT REPEAT 107..142
FT /note="HEAT 2"
FT REPEAT 143..179
FT /note="HEAT 3"
FT REPEAT 180..216
FT /note="HEAT 4"
FT REPEAT 218..254
FT /note="HEAT 5"
FT REPEAT 292..329
FT /note="HEAT 6"
FT REPEAT 330..366
FT /note="HEAT 7"
FT REGION 738..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..846
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 869 AA; 97154 MW; 05F33D80A24F970B CRC64;
MSSSSTSIMD NLFQRSLEDL IKGFRLQLLG ESNFISRAVE EIRREIKATD LSTKSTALHK
LSYLAALHGV DMSWAAFHAV EVVSSSRFQH KRIGYQAITQ SFNDQTSVML LITNQVRKDL
NSANEYEVSL ALECLSRIGT HDLARDLTPE VFTLLGSSKS FVKKKAIGVV LRVFEKYHDA
VKVCFKRLVE NLETSDPQIL SAVVGVFCEL ATKDPQSCLP LAPEFYKVLV DSRNNWVLIK
VLKIFAKLAL IEPRLGKKVA EPICEHMRRT VAKSLVFECV RTVVSSLSDN EAAVKLAVAK
IREFLVEDDP NLKYLGLNAL SIVAPKHLWA VLENKEVVVK AMSDEDPNVK LEALHLLMAM
VNEDNVSEIS RILMNYALKS DPLFCNEIIF SVLSACSRNA YEIIVDFDWY LSLLGEMARI
PHCQRGEDIE HQLIDIGMRV RDARPQLVRV SWALLIDPAL LGNLFLHPIL SAAAWVSGEY
VEFSKNPYET VEALLQPRTD LLPPSIKAIY IHSAFKVLVF CLGSYFSSQE PTSSSLAQES
SSGSLLVNVF THESILSLVN VIELGLGPLS GYHDVEVQER AKNVLGYISV IKQEIAEQLN
LQDNETEASR VTAFMEDVFS EEFGPISATA QEKVCVPDGL ELKENLGDLE EICGEHLKPV
ESDSVSYTDK ISFSVSKLRI RDQQEATSSS SPPHEASSLL AEHRKRHGMY YLTSQKEDQD
SNGTSSDYPL ANELANEISQ DSFNPKRKPN QSKPRPVVVK LDDGDESRIT PQAKTNIQTA
NDDESLSRAI QSALLVKNKG KEKDRYEGNP NSGQQEKEES SRIENHQNSE KKKKKKKKKK
GEGSSKHKSR RQNEVASASE QVIIPDFLL
