ID A0A0L7REP6_9HYME Unreviewed; 1321 AA.
AC A0A0L7REP6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=AP-3 complex subunit beta-2 {ECO:0000313|EMBL:KOC69313.1};
GN ORFNames=WH47_05977 {ECO:0000313|EMBL:KOC69313.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC69313.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC69313.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC69313.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; KQ414609; KOC69313.1; -; Genomic_DNA.
DR STRING; 597456.A0A0L7REP6; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0030123; C:AP-3 adaptor complex; IEA:InterPro.
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 PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR PANTHER; PTHR11134:SF1; AP-3 COMPLEX SUBUNIT BETA; 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; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053825}.
FT DOMAIN 1046..1185
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..984
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1029
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1321 AA; 148261 MW; F3FBCDDDD8640C7F CRC64;
MLTAAANSLS NNGGSYSNDR PSSTADPELA TDPASGGFFH SDYKKHEDLK QMLDSNKDGL
KLEAMKRIIG MIAKGRDASE LFPAVVKNVV SKNIEVKKLV YVYLVRYAED QQDLALLSIS
TFQRALKDPN QLIRASALRV LSSIRVSMIV PIVMLAIKDS ASDMSPYVRK TAAHAIPKLY
SLDSEQKEEL TSVLEKLLSD KTTLVVGSAV MAFEEVCPER IDLIHKNYRK LCNLLVDVDE
WGQVSIEEDE NRPFYDSDSD SSNTKKPKST LVSDHRLLLR NTKPLLQSRN ASVVMAVSQL
YHHTAPRREV MIAAKALIRL LRGHREVQSV VLHCITSISI TRKGMFEPFL KSFFVRTSDP
THIKLLKLDI LTNLATETSI GVILREFQTY ISSSDKEFVG ASIQAIGRCA SNIKEVTDTC
LNGLVSLLSN RDEAVVAESV VVIKKLLQTQ PNEHKNIIAH MAKLMDFITI PQARASILWL
LGEYSDRVPK IAPDVLRKMA KNFVNEQDIV KLQILNLAVK LCLNNPIQTK PFCQYVFQLA
KYDQNYDIRD RARFLRRFIF DEDGHKKKLQ QLAKQIFLAL KPAPTLTSRF KNSGYQLGTL
SHYLDMPCAG YRPLPPFPDV APDPSVRDVA SGTVRDIRDE YYRKNKKDRK GMGKEKLFSS
DVFQDTETSI GVILREFQTY ISSSDKEFVG ASIQAIGRCA SNIKEVTDTC LNGLVSLLSN
RDEAVVAESV VVIKKLLQTQ PNEHKNIIAH MAKLMDFITI PQARASILWL LGEYSDRVPK
IAPDVLRKMA KNFVNEQDIV KLQILNLAVK LCLNNPIQTK PFCQYVFQLA KYDQNYDIRD
RARFLRRFIF DEDGHKKKLQ QLAKQIFLAL KPAPTLTSRF KNSGYQLGTL SHYLDMPCAG
YRPLPPFPDV APDPSVRDVA SGTVRDIRDE YYRKNKKDRK GMGKEKLFSS DVFQDDLPAE
ELDNENESSD TSTSDSSDEE SDSSEYTSES GKSENDSEKK KSTKLSDESN SESESEESDS
EESSEDSQES EDEQYKASNQ EVKEKPKSNI DLLLELDDVI PMTPVMPLST GSLLTPTSSN
VANDIREVSA SFIPIKKSEL LNNITGHGLK IEYRFTRSQH LVSSYLVTIE LTFSNEGSEP
IKDIQMGVKN LPKGMLIHDF TGISLLEINS NLSSTLGINF NDSTQPANFN IDFTIGEETH
SYPVTIKAPI GEIIRAVLLP EDMFLTEKNK LKGMNEHIAS VQYSGNKKII SQNVFETANV
AMISSSDEEI RFAAHTLASK SLILVTIKMI ENDSLMICVN CEKMVIGSIL LNELKSNLKI
N
//
