ID A0A2I3GEB7_NOMLE Unreviewed; 976 AA.
AC A0A2I3GEB7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=AP-3 complex subunit beta {ECO:0000256|PIRNR:PIRNR037096};
GN Name=AP3B2 {ECO:0000313|Ensembl:ENSNLEP00000029642.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000029642.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000029642.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000029642.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor
CC protein complex 3 (AP-3) that plays a role in protein sorting in the
CC late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes
CC mediate both the recruitment of clathrin to membranes and the
CC recognition of sorting signals within the cytosolic tails of
CC transmembrane cargo molecules. AP-3 appears to be involved in the
CC sorting of a subset of transmembrane proteins targeted to lysosomes and
CC lysosome-related organelles. In concert with the BLOC-1 complex, AP-3
CC is required to target cargos into vesicles assembled at cell bodies for
CC delivery into neurites and nerve terminals.
CC {ECO:0000256|ARBA:ARBA00023570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004145}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004145}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004145}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000256|ARBA:ARBA00006613, ECO:0000256|PIRNR:PIRNR037096}.
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DR EMBL; ADFV01044192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01044193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01044194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01044195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01044196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3GEB7; -.
DR Ensembl; ENSNLET00000043121.1; ENSNLEP00000029642.1; ENSNLEG00000011002.3.
DR GeneTree; ENSGT00940000156817; -.
DR Proteomes; UP000001073; Chromosome 6.
DR GO; GO:0030123; C:AP-3 adaptor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; 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; 2.
DR InterPro; IPR026740; AP3_beta.
DR InterPro; IPR029390; AP3B_C.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR PANTHER; PTHR11134:SF11; AP-3 COMPLEX SUBUNIT BETA-2; 1.
DR Pfam; PF01602; Adaptin_N; 2.
DR Pfam; PF14796; AP3B1_C; 1.
DR PIRSF; PIRSF037096; AP3_complex_beta; 3.
DR SMART; SM01355; AP3B1_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037096};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR037096};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transport {ECO:0000256|PIRNR:PIRNR037096}.
FT DOMAIN 695..841
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT REGION 560..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 107212 MW; 4D00A044D68BBC85 CRC64;
HDDLKEMLDT NKDSLKLEAM KRIVAMIARG KNASDLFPAV VKNVACKNIE DPNQLIRASA
LRVLSSIRVP IIVPIMMLAI KEAASDMSPY VRKTAAHAIP KLYSLDSDQK DQLIEVIEKL
LADKTTLVAG SVVMAFEEVC PERIDLIHKN YRKLCNLLID VEEWGQVVII SMLTRYARTQ
FLSPTQNESL LEENAEKAFY GSDEDEAKGA GSEETAAAAL PARKPYVMDP DHRLLLRNTK
PLLQSRSAAV VMAVAQLYFH LAPKAEVGVI AKALVRLLRS HSEVQYVVLQ NVATMSIKRR
DPTQIKILKT YIRSMDKDFV AATIQAIGRC ATNIGRVRDT CLNGLVQLLS NRDELVVAES
VVVIKKLLQM QPAQHGEIIK HLAKLTDNIQ VPMARASILW LIGEYCEHVP RIAPDVLRKM
AKSFTAEEDI VKLQVINLAA KLYLTNSKQT KLLTQYVLSL AKYDQNYDIR DRARFTRQLI
VPSEQGGALS RHAKKLFLAP KPAPVLESSF KDRDHFQLGS LSHLLNAKAT GYQELPDWPE
EAPDPSVRNV EVPEWTKCSN REKRKEKEKP FYSDSEGESG PTESADSDPE SESESDSKSS
SESGSGESSS ESDNEDQDED EEKGRGSESE QSEEDGKRKT KKKVPEGKGE ASSSDEGSDS
SSSSSESEMT SESEEEQLEP ASWRRKTPPS SKSAPATKEI SLLDLEDFTP PSVQPVSPPA
IVSTSLAADL EGLTLTDSTL VPSLLSPVSG VGRQELLHRV AGEGLAVDYT FSRQPFSGDP
HMVSVHIHFS NSSDTPIKGL HVGTPKLPAG ISIQEFPEIE SLAPGESATA VMGINFCDST
QAANFQLCTQ TRQFYVSIQP PVGELMAPVF MSENEFKKEQ GKLMGMNEIT EKLMLPDTCQ
SDHIVVQKVT ATANLGRVPC GTSDEYRFAG RTLTGGSLVL LTLDARPAGA AQLTVNSEKM
VIGTMLVKDV IQALTQ
//
