ID F4WJF0_ACREC Unreviewed; 1031 AA.
AC F4WJF0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=AP-3 complex subunit beta {ECO:0000256|PIRNR:PIRNR037096};
GN ORFNames=G5I_05829 {ECO:0000313|EMBL:EGI65728.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI65728.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL888182; EGI65728.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WJF0; -.
DR STRING; 103372.F4WJF0; -.
DR eggNOG; KOG1060; Eukaryota.
DR InParanoid; F4WJF0; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
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; 1.
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 PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR PANTHER; PTHR11134:SF1; AP-3 COMPLEX SUBUNIT BETA; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF14796; AP3B1_C; 1.
DR PIRSF; PIRSF037096; AP3_complex_beta; 2.
DR SMART; SM01355; AP3B1_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|PIRNR:PIRNR037096};
KW Protein transport {ECO:0000256|PIRNR:PIRNR037096};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transport {ECO:0000256|PIRNR:PIRNR037096}.
FT DOMAIN 758..897
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..739
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 115816 MW; 77E36AB7AF9C7986 CRC64;
MLTAAASMSN NGGSYSVERP STPDADLFDT MEIPSFMSGL FHPEYKKHDD LKEMLDSNKD
GLKLEAMKRI IGMVAKGKDA SEMFPAVVKN VVSKNIEVKK LVYVYLVRYA EDQQDLALLS
ISTFQRALKD PNQLIRASAL RVLSSIRVSM IVPIVMLAIK DSASDMSPYV RKTAAHAIPK
LYSLDHEQKE ELIGVLEKLL SDKTTLVVGS AVMAFEEVCP ERIDLIHKNY RKLCNLLVDV
DEWGQVNLEE DENRPFYDSD SDDSSNTKKP KFTLDPDHRL LLRNTKPLLQ SRNASVVMAG
GQLYHHAAPR SEVMTAAKAL IRLLRGHREV QSIVLHCIAS ISITRKGMFE PFLKSFFVRT
SDPTHIKLLK LDILTNLVTE TSISVILREF QTYISSSDKE FVGASIQAIG RCASNIKEVT
DMCLNGLVSL LSNRDEAIVA ESVVVIKKLL QTQPNEHKDI IAHMAKLMDF ITVPQARASI
LWLLGEYSDR VPKIAPDVLR KMAKSFVNEQ DIVKLQTLNL AVKLCLNNPS QTKPFCQYVF
QLAKYDQNYD IRDRARFLRH FIFEEEGDVK KLPQFAKRVF LAPKPAPTLT SRFKNSEYQL
GTLSHYLDMP CVGYRPLPPF PEVTQDPSVR DVAPPTAQEL KEERHNRKEK EKKKNKEKEK
PFYSDEESTP AEESDNQSSN SSSSESSDED SDSSEYTSES DKSETDSGKK NETKSDDSES
ESSSDEESDS EDLEEESETQ ENEKEKPKAI KQEVKEKPKS NFDLLLDLDD VVPMTPVMTP
SLGGFLTPIN STITDGIREV STSYVPLKKT TLLNSIIGHG LKIEYRFTRS QHLVSSNLVS
IELTFFNESN DVIKEIQIGN KNLQKGMFIH DFTQISSLDV NATLASTLGV NFNDSTQPAN
FNIDFTINDE KYSCPVSIKP PIGEIIRSVT LPESMFNAEK AKLKGMNEHI AKIPYSRNKN
ALPQKVFETA NVARVSNEDE VIRFAAHTLA SKSLVLVTIK FIDAGQLEVC VNCEKMVIGS
ILLNEFKSNL K
//
