ID A0A0P7B5I7_9HYPO Unreviewed; 1091 AA.
AC A0A0P7B5I7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=AP-3 complex subunit delta {ECO:0000256|PIRNR:PIRNR037092};
GN ORFNames=AK830_g4908 {ECO:0000313|EMBL:KPM41669.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM41669.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM41669.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM41669.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|PIRNR:PIRNR037092}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer.
CC {ECO:0000256|PIRNR:PIRNR037092}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000256|PIRNR:PIRNR037092}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000256|PIRNR:PIRNR037092}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM41669.1}.
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DR EMBL; LKCW01000061; KPM41669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7B5I7; -.
DR STRING; 78410.A0A0P7B5I7; -.
DR OrthoDB; 2877445at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0030123; C:AP-3 adaptor complex; IEA:InterPro.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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:SF12; AP-3 COMPLEX SUBUNIT DELTA-1; 1.
DR PANTHER; PTHR22781; DELTA ADAPTIN-RELATED; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR PIRSF; PIRSF037092; AP3_complex_delta; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|PIRNR:PIRNR037092};
KW Protein transport {ECO:0000256|PIRNR:PIRNR037092};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Transport {ECO:0000256|PIRNR:PIRNR037092}.
FT DOMAIN 110..699
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 973..1010
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1091 AA; 119511 MW; 99897085E3723199 CRC64;
MPQRLTPGGS PLRCSGRLAR RVEGGGSVMG PSRTSPPTTT SLSLITTTPT PPPPNAPNIQ
HAPNHLAATD PRKTLTKALV PPLLLVPSSP PSTPRSRSGP PHVGHPQASY LKATALLKLI
YLEMVGHDMS WASFHVLEVM SSPKYHQKRV GYLGAVQSFR PDTEVLMLAT NLLKKDLGST
APTVISLPVA TLPHVITPSL ALSTLADLLP RLSHSHSNIR KKTLVTLYRL ALVYPEALRA
AWPKIKERLM DPDEDPSVTA AIVNVVCELG WRRPHDFLPL APRLFELLVD GGNNWMAIKL
IKLFATLTPL EPRLVRKLLP PLTNIIRTTP AMSLLYECIN GIIQGGILGG ADDVSGTDEI
ATLCVNKLRG MIMIDGDPNL KYVALLAFNK IVITHPYLVS QQEDVILECI DSSDITIRIQ
ALDLVQGMVT GDNLMSIVSR LMKQLKTSMP VRDRQQAGTP PVEPSDSDTD GSFAESGAAK
NPGQAPLPDD YRIDVIGRIL AMCAKDNYSS VLDFDWYIAV LTQLVRMAPL SRRVDVDPGF
SSRPRGDVSE KIGDELRNIA VKVRAMRPAT VRASEDILNQ LTADTPPGYS ITSGALKSVS
WIMGEYAPQL PAPDDNLNSL LQLIPRTTNP EVITTTLQAV TKIFATVVGD EMEQWTAERK
SRVSLLMARI IHVFEPLQLN PSLEVQERAV EFTELLKLTS EAASGQPAST DELQQDPPLL
LTQAIPSLFN GWELNSVAKG AQHNVPLPDG LDLDEPIHAN LAKLLSEADS VGLATDDSDD
FEVYYHQRPP PTSIDSSAPA ISKLVEPAED YVGSYQQATE DSYLDADIVA RRKAERLERN
KDDPFYIPSK SATPQTSTPI HNILHNSNGP DLDIDSIPIM QLDLDKTGNS TPPQQYQQKQ
PRPQARPRQK VVIAADETLE GSDGGRTYDS ENNSDSFTKT KARKLKQSLL KVDSSNIRSF
NLEGQPTEGS FDHERQQRED AEMQQAMKEV ERLRLEMQRA NERIQVAQGV DAEGTVVKKK
KKIKKVAPDG DEPKKTKKKK KTRVALLDEP ADEGSAASVD SPPVGGAEVD VVVAKKKKKK
KRQPALIEDA T
//
