ID A0A0D2BFK8_9EURO Unreviewed; 1016 AA.
AC A0A0D2BFK8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=AP-3 complex subunit delta {ECO:0000256|PIRNR:PIRNR037092};
GN ORFNames=PV08_04983 {ECO:0000313|EMBL:KIW17788.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW17788.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW17788.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW17788.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-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}.
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DR EMBL; KN847494; KIW17788.1; -; Genomic_DNA.
DR RefSeq; XP_016238004.1; XM_016379327.1.
DR AlphaFoldDB; A0A0D2BFK8; -.
DR STRING; 91928.A0A0D2BFK8; -.
DR GeneID; 27332066; -.
DR VEuPathDB; FungiDB:PV08_04983; -.
DR HOGENOM; CLU_001908_3_0_1; -.
DR OrthoDB; 2877445at2759; -.
DR Proteomes; UP000053328; 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 Golgi apparatus {ECO:0000256|PIRNR:PIRNR037092};
KW Protein transport {ECO:0000256|PIRNR:PIRNR037092};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Transport {ECO:0000256|PIRNR:PIRNR037092}.
FT DOMAIN 20..624
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT REGION 382..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 112049 MW; 0C2BED12BFA48585 CRC64;
MFEKSLVDLI KGLRSHKGNE AEYIQGAIKE CRSEIRSQDL DLKATALLKL IYLEMFGYDM
TWAAFNVLEV MASPKLMQKR VGYLAAVQSF RPETEILMLA ENLLKKDLTS PTIPILSLPL
TTLPHFVTSS MALSILTELL PRMSHSQPAV RKKTIVTLYR LALVYPETLR VAWPKIKERL
LDEEEDSSVT AATVNVVCEL GWRRPQDFLP LAPRLFELLL AQKNNWMGIK IIKLFAVLTP
LEPRLVKKLV RPLTKLIQET TAMSLLYECI SGIIQGGILD GADSGVDVEE VADLCISKLR
GMIVLDGDPN LKYVALLAFN KIVGTHPALV SMQQDVIMAC LDDPDISIRM QALELVSGMV
NSDSLQAVVN RLMKQLASLP SSNDANGHYD EGQTDMEQRL VPDKRGSENA PLSDEYRHEV
IGRILDMCSY NTYANITDFE WYIEILVHLV RHLAADQDRS QSRAMGENST SLGARIGSQL
RDIAIRVKEL RPETTRAAET LVLISNRAIA YPRHGSAQSQ VLQATAWICG EYAEYLSNPF
EVLNSLIHES SYGFPPGTLA IFIQALPKVV SHIAVVTNRE WNISRGTTMS LLLARATEFL
EKLSSHPNLE VQERSVEFLE LLRLATEALS GQARDSSQAP LLLTSAVPSL FAGLELNPVS
SAAQKKVPLP DDLDLDAPIN PDLPSILQAS QVADEDESGD DIFFSFYHER EPAPAVTSFQ
APLAAALLDS ANEHEPISYQ STPDSPATLA RRKAERLARA RDDPFYIAPA DDTDPRIHEI
ISGTNGGEEL DVESIPIIDL HIDPAQTLAA HQTAGLAELR TARKKKPRKF VIAADETLGF
GPQTPPMSQS LSTSNAGSHS STPTASRPRS LSPNAQLRGK TSTRPTRSLL TVDSSTLQDL
ILEGGSAENE LDILRREAEE AEMARALREV ERKRLEMQRE AERGRTTLGE GVDAEGTVIR
KKKKKRTKAV DAVGDADVEG EPQHDVGTVK KKKKKKKVKP TQPSAAGDAP EARVDE
//
