ID A0A2V1AU45_9ASCO Unreviewed; 1067 AA.
AC A0A2V1AU45;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=AP-3 complex subunit delta {ECO:0000256|PIRNR:PIRNR037092};
GN ORFNames=CXQ85_000319 {ECO:0000313|EMBL:PVH21345.1};
OS [Candida] haemuloni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH21345.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH21345.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH21345.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) 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:PVH21345.1}.
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DR EMBL; PKFO01000005; PVH21345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1AU45; -.
DR STRING; 45357.A0A2V1AU45; -.
DR EnsemblFungi; CXQ85_000319-t46_1; CXQ85_000319-t46_1-p1; CXQ85_000319.
DR VEuPathDB; FungiDB:CXQ85_000319; -.
DR OrthoDB; 2877445at2759; -.
DR Proteomes; UP000244309; 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:UP000244309};
KW Transport {ECO:0000256|PIRNR:PIRNR037092}.
FT DOMAIN 53..660
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT REGION 686..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..729
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 120453 MW; 0298A417822B6657 CRC64;
MSSFQMQSSE MLARLKPFGI SFEKSLNDLI KGIRAHFKES PESLRDFLDN AIEECKNELT
TTDLEVKATA VLKLAYLEMY GFDMSWCNFQ ILEIMSSSRF QQKRIGYLAA MQSFKNEKDL
LILATNQFKK DLSSHNHIEI GLALSGIATI VTPNLAQDIV DDVLVKLTHS KPYIRKKAVL
ALFKIFLQYP ESLRSSLPRV IEKLDDEDIA VVSATITVVC EISKKNPNIF IAYLPKFFSI
LEETQNNWLI IRILKLFQSL SKVEPRMKKR ILPSILSLMS KTEATSLVYE SISCIVNGGM
LSPTSSRDKE IAKECITHLI SFFAKGDANL RFVGLIALIS ILKVYPEFMH KVNGVSGYVM
HSLEVKDTIV MKKALEICQY LVTEDNILEL IRVLLLQLVP DESSTHIPES LKLEIASKIL
QIASKDNYAN IPNFNWYVTV LKDVVNMTLL PVVTKGSPNA APALSKRTSD IIARKLGAEF
KTVATKVPSL RPYLMKNVVY EFVKDERTLQ YSPLLMRDIY WLMGEYVGEL GNTDDDSDEE
DDDNQDFALG YKIQMLNTII NSYVDKKLSG PTRFPISQLL IQLPNPEVQT TLIPALVKLY
SDLVTDYISY YDQSGKMPSQ QYGQLAYFLL KSIKFLENWE QNSDYEVQER ALSWLEFLRL
SLDAMGGENS PLLKKLEDDE LVFYKKNQPT SSNESSQEEE SDEEEEASSD SDDSSDEEVS
QEETPLDEDQ EQANGNSNNT DFDVNETHEV PHLLTSVLPS FFKGYTLNPV AASAQKMVGL
PDDLELDVPI NTPPSYCLIE DQQIDIFYSD EESDEETPIE KEERTKVDEE VTRERLERMK
DDPFYITPSE KKGRSKSKPQ LLNTPSDNAA SETPSEKNSF VSLDELAKKE AKKSKKIKKH
KVTVLSEESL GGDVPGQVSE LGDSDANKKK KSNRILIKAA DPRAEEYDVD LDALRQQLEE
KEKKKFAKEA KKKKKADKEK SKSKSKKTKS KPTEETSTVG EPKADKPEAE NTGEEGEAES
KKPVEADAET VPEVKSATPE VITDQQAIEV SSKPKTKKKK KKAVILD
//
