AP3D_ASHGO
ID AP3D_ASHGO Reviewed; 899 AA.
AC Q755A1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=AP-3 complex subunit delta;
DE AltName: Full=Adaptor-related protein complex 3 subunit delta;
DE AltName: Full=Delta-adaptin 3;
DE Short=Delta-adaptin;
GN Name=APL5; OrderedLocusNames=AFL076W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 the vacuole (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of 2 large adaptins (APL5 and APL6), a medium adaptin (APM3) and a
CC small adaptin (APS3). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q08951}.
CC Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q08951}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q08951}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q08951}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles located at the Golgi complex.
CC {ECO:0000250|UniProtKB:Q08951}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; AE016819; AAS53296.1; -; Genomic_DNA.
DR RefSeq; NP_985472.1; NM_210826.1.
DR AlphaFoldDB; Q755A1; -.
DR SMR; Q755A1; -.
DR STRING; 33169.AAS53296; -.
DR EnsemblFungi; AAS53296; AAS53296; AGOS_AFL076W.
DR GeneID; 4621701; -.
DR KEGG; ago:AGOS_AFL076W; -.
DR eggNOG; KOG1059; Eukaryota.
DR HOGENOM; CLU_001908_1_1_1; -.
DR InParanoid; Q755A1; -.
DR OMA; LYESINC; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0030123; C:AP-3 adaptor complex; IBA:GO_Central.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
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 3: Inferred from homology;
KW Coiled coil; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..899
FT /note="AP-3 complex subunit delta"
FT /id="PRO_0000227675"
FT REPEAT 37..74
FT /note="HEAT 1"
FT REPEAT 155..192
FT /note="HEAT 2"
FT REPEAT 194..229
FT /note="HEAT 3"
FT REPEAT 231..267
FT /note="HEAT 4"
FT REPEAT 268..305
FT /note="HEAT 5"
FT REPEAT 308..344
FT /note="HEAT 6"
FT REPEAT 345..382
FT /note="HEAT 7"
FT REPEAT 384..428
FT /note="HEAT 8"
FT REPEAT 480..518
FT /note="HEAT 9"
FT REPEAT 536..580
FT /note="HEAT 10"
FT REPEAT 590..613
FT /note="HEAT 11"
FT REPEAT 614..656
FT /note="HEAT 12"
FT REGION 668..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 841..862
FT /evidence="ECO:0000255"
FT COMPBIAS 741..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..878
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 101753 MW; 0199759AC054F047 CRC64;
MSSLYAPTDE VKRRLRPFGL FFEKSLKDLI KGIRSQQSPE QLHEFLTRVL SECREEVKHA
DFNMKTNAVL KLTYLEMYGF DMSWANFHVL EVMSSTRFQQ KRVGYLAASQ SFYKDHDILM
LATNLLRKDL KYSLSNETVR MGVALSGLSA MVTPELARDI CEDLFLMLHS TKPYIRKKAV
TALFKVFLQY PEGLRDNFEK FVDRLEDDDL SVVSATVSVI CELSKHNPQP FIQLSPILYQ
MLIKVDNNWV IIRLLKLFTN LAQIEPKLRV KILPNVLELM DSTTAISVVY ESINCIVKGN
MLNSDDYDSA VACLDKLHDF CTSNDPNLRY LSCVLFYKIG KINTDFIANF DVLILRLLVD
VDVSIRSKTL ELLEGIVTED NLVDFVQRLL KQFVDVDKIC VNDQEFSIDI PEYYKSKMIH
AICKITAMKN YANVTDFEWY IALLSDLCIV SQDLQDKTLA QKLGEQIRNI MVKVPDLRDR
TLAQIVQLVK SEDITARLPG VLKECIWCLG EYSSLLDNKD EYILLLAENS KLYEPELQQT
LIPAILKIYS NWCNESVVDT GRIKWVTERI ITPLEDLIIS KNFEVQERSS EALEFLRLCL
DSLSEDASDS LPLLLTEVLP SFFNAFELQP ITSGTQRKLQ QSISVDCDTP FLTESELEQL
LADDTSVDGI VSPDVSDTES DSEMYVPGAA PKDKGSSPTH ELTTAELEAI NERRKQERVG
NPFYLDDADV GSVKKVDILD NLSNSKPSSS GSLVRLSSES KAKEKKKKVK VRVISDAVIV
DGVNTADVTD DRPSNTPSAR NKIALQLKNK LDSFDFTKPR DEGDYDPDVD LQKLREKFAQ
QRLLDESAAA EEEVVVVKKK KRSKDGSKSS KKKSRSKSKP SSKGGDTAEA ELLPGLTTE
