AP3D1_BOVIN
ID AP3D1_BOVIN Reviewed; 1207 AA.
AC Q865S1; Q03368; Q28876;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=AP-3 complex subunit delta-1;
DE AltName: Full=AP-3 complex subunit delta;
DE AltName: Full=Adaptor-related protein complex 3 subunit delta-1;
DE AltName: Full=BLVPCP1;
DE AltName: Full=Bovine leukemia virus cell receptor;
DE Short=BLV-R;
DE AltName: Full=Delta-adaptin;
GN Name=AP3D1; Synonyms=BLVR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, IDENTIFICATION IN THE
RP AP-3 COMPLEX, AND LACK OF FUNCTION AS RECEPTOR FOR BOVINE LEUKEMIA VIRUS.
RC TISSUE=Brain;
RX PubMed=12692298; DOI=10.1099/vir.0.18763-0;
RA Suzuki T., Matsubara Y., Kitani H., Ikeda H.;
RT "Evaluation of the delta subunit of bovine adaptor protein complex 3 as a
RT receptor for bovine leukaemia virus.";
RL J. Gen. Virol. 84:1309-1316(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 493-845.
RC TISSUE=Kidney;
RX PubMed=7998843; DOI=10.1007/bf01379141;
RA Ban J., Truong A.T., Horion B., Altaner C., Burny A., Portetelle D.,
RA Kettmann R.;
RT "Isolation of the missing 5'-end of the encoding region of the bovine
RT leukemia virus cell receptor gene.";
RL Arch. Virol. 138:379-383(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 758-1207.
RC TISSUE=Kidney;
RX PubMed=8380453; DOI=10.1128/jvi.67.2.1050-1057.1993;
RA Ban J., Portetelle D., Altaner C., Horion B., Milan D., Krchnak V.,
RA Burny A., Kettmann R.;
RT "Isolation and characterization of a 2.3-kilobase-pair cDNA fragment
RT encoding the binding domain of the bovine leukemia virus cell receptor.";
RL J. Virol. 67:1050-1057(1993).
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 lysosomes. Involved in process of CD8+ T-
CC cell and NK cell degranulation. In concert with the BLOC-1 complex, AP-
CC 3 is required to target cargos into vesicles assembled at cell bodies
CC for delivery into neurites and nerve terminals.
CC {ECO:0000250|UniProtKB:O14617, ECO:0000250|UniProtKB:O54774}.
CC -!- SUBUNIT: AP-3 associates with the BLOC-1 complex (By similarity).
CC Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two
CC large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or
CC AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small
CC adaptin (sigma-type subunit APS1 or AP3S2) (PubMed:12692298). Interacts
CC with SLC30A2 (By similarity). Interacts with CLN3 (via dileucine
CC motif); this interaction facilitates lysosomal targeting (By
CC similarity). {ECO:0000250|UniProtKB:O14617,
CC ECO:0000269|PubMed:12692298}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12692298}. Golgi
CC apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- MISCELLANEOUS: Was originally thought to be a bovine leukemia virus
CC receptor. {ECO:0000305|PubMed:7998843}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30633.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA30633.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB32770.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA36591.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB015979; BAA36591.1; ALT_INIT; mRNA.
DR EMBL; S75828; AAB32770.2; ALT_SEQ; Genomic_DNA.
DR EMBL; M98430; AAA30633.1; ALT_SEQ; mRNA.
DR RefSeq; NP_776423.3; NM_173998.4.
DR AlphaFoldDB; Q865S1; -.
DR SMR; Q865S1; -.
DR STRING; 9913.ENSBTAP00000011906; -.
DR PaxDb; Q865S1; -.
DR PeptideAtlas; Q865S1; -.
DR PRIDE; Q865S1; -.
DR Ensembl; ENSBTAT00000011906; ENSBTAP00000011906; ENSBTAG00000009034.
DR GeneID; 281023; -.
DR KEGG; bta:281023; -.
DR CTD; 8943; -.
DR VEuPathDB; HostDB:ENSBTAG00000009034; -.
DR VGNC; VGNC:25988; AP3D1.
DR eggNOG; KOG1059; Eukaryota.
DR GeneTree; ENSGT00550000075067; -.
DR HOGENOM; CLU_001908_0_0_1; -.
DR InParanoid; Q865S1; -.
DR OrthoDB; 598949at2759; -.
DR TreeFam; TF105666; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000009034; Expressed in pigment epithelium of eye and 106 other tissues.
DR ExpressionAtlas; Q865S1; baseline.
DR GO; GO:0030123; C:AP-3 adaptor complex; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098830; C:presynaptic endosome; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0098943; P:neurotransmitter receptor transport, postsynaptic endosome to lysosome; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0016182; P:synaptic vesicle budding from endosome; IBA:GO_Central.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR017105; AP3_complex_dsu.
DR InterPro; IPR010474; AP3D_dom_metazoa.
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 Pfam; PF06375; AP3D1; 1.
DR SMART; SM01354; BLVR; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT CHAIN 2..1207
FT /note="AP-3 complex subunit delta-1"
FT /id="PRO_0000193765"
FT REPEAT 34..71
FT /note="HEAT 1"
FT REPEAT 142..179
FT /note="HEAT 2"
FT REPEAT 180..216
FT /note="HEAT 3"
FT REPEAT 218..254
FT /note="HEAT 4"
FT REPEAT 257..296
FT /note="HEAT 5"
FT REPEAT 298..336
FT /note="HEAT 6"
FT REPEAT 337..373
FT /note="HEAT 7"
FT REPEAT 375..409
FT /note="HEAT 8"
FT REPEAT 521..558
FT /note="HEAT 9"
FT REGION 630..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 659..679
FT /evidence="ECO:0000255"
FT COILED 725..752
FT /evidence="ECO:0000255"
FT COILED 846..870
FT /evidence="ECO:0000255"
FT COMPBIAS 633..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..754
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 762
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14617"
FT CONFLICT 758
FT /note="S -> R (in Ref. 2; AAB32770 and 3; AAA30633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1207 AA; 136390 MW; 8E07DD39B33E529A CRC64;
MALKMVKGSI DRMFDKNLQD LVRGIRNHKE DEAKYISQCI DEIKQELKQD NIAVKANAVC
KLTYLQMLGY DISWAAFNII EVMSASKFTF KRIGYLAASQ CFHEGTDVIM LTTNQIRKDL
SSPSQYDTGV ALTGLSCFVT PDLARDLAND IMTLMSHTKP YIRKKAVLIM YKVFLKYPES
LRPAFPRLKE KLEDPDPGVQ SAAVNVICEL ARRNPKNYLS LAPLFFKLMT SSTNNWVLIK
IIKLFGALTP LEPRLGKKLI EPLTNLIHST SAMSLLYECV NTVIAVLISL SSGMPNHSAS
IQLCVQKLRI LIEDSDQNLK YLGLLAMSKI LRTHPKSVQA HKDLVLQCLD DKDESIRLRA
LDLLYGMVSK KNLMEIVKKL MTHVDKAEGT TYRDELLTKI IDICSQSNYQ HITNFEWYIS
ILVELTRLEG TRHGHLIAAQ MLDVAIRVKA IRRFAVAQMS ALLDSAHLVA SSPQRSGICE
VLYAAAWICG EFSEHLQEPQ QTLEAMLRPK VTTLPGHIQA VYVQNVVKLY AAILQQKEQA
ADTSAAQEVT QLLVERLPQF VQSADLEVQE RASCILQLVK HVQKLQAKDV PVAEEVSALF
AGELNPVAPK AQKKVPVPEG LDLDAWINEP LSDSESEDEK PKAMFQDEEQ RHTKPRAPEA
DEQELARRRE ARRQEQANNP FYIKSSPSPQ KRYQDAPGVE HIPVVQIDLS VPLKVPGMPL
SDQYVKLEEE RRHRQRLEKD KRKKKKRERE RRGTRRHSSL HTESDEDIAP AQRVDIVTEE
MPENALPSDE DDKDPNDPYR ALDIDLDKPL ADSEKLPVQK HRNAETSKSP EKEDVPLVEK
KSKKPKKKEK KHKEKEREKK KKEVEKGEDL DFWLSTTPPA ATPALEELEV NTTVTVLKEG
QEEPRGEEQD AEEDREQDLE KKPSKHKKKK HKKDKEERPK DKRKSKKKVP PADEEAAEPV
ENGTLEEEPL PPMSSYILLA ENSYIKMTYD VQGSLQKDSQ VTVSVVLENQ SDSFLKSMEL
NVLDSLNARL ARPEGSSVHD GVPVPFQLPP GISNEAQFVF TIQSIVMAQK LKGTLSFIAK
NDEGSTHEKL DFKLHFTCTS YLVTTPCYSD AFAKLLESGD LSMSSIKVDG ISMSFHNLLA
KICFHHRFSV VERVDSCASM YSRSIQGHHV CLLVKKGEKS VSVDGKCSDP TLLSNLLEEM
KETLATC
