ID A0A3P9PBP1_POERE Unreviewed; 988 AA.
AC A0A3P9PBP1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=AP-3 complex subunit beta {ECO:0000256|PIRNR:PIRNR037096};
GN Name=AP3B2 {ECO:0000313|Ensembl:ENSPREP00000019336.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000019336.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000019336.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000019336.1};
RG Ensembl;
RL Submitted (SEP-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 STRING; 8081.ENSPREP00000019336; -.
DR Ensembl; ENSPRET00000019543.1; ENSPREP00000019336.1; ENSPREG00000013040.1.
DR GeneTree; ENSGT00940000156817; -.
DR OMA; HFLVRST; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000013040; Expressed in head.
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:SF11; AP-3 COMPLEX SUBUNIT BETA-2; 1.
DR Pfam; PF01602; Adaptin_N; 1.
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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|PIRNR:PIRNR037096, ECO:0000256|SAM:Phobius};
KW Protein transport {ECO:0000256|PIRNR:PIRNR037096};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|PIRNR:PIRNR037096}.
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 722..855
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 110252 MW; 81760E461AE51C79 CRC64;
MSSSSAFNEE KGGSSSVGEP EYGHDPASGG IFSSDYKRHD DLKEMLDSNK DSLKLEAMKR
IVAVSGINVY FGILLISNFG CVKKLVYVYL VRYAEEQQDL ALLSISTFQR GLKDPNQLIR
ASALRVLSSI RVTIIVPIMM LAIKEAASDM SPYVRKTAAH AIPKLYSLDP EQKDQLIEVI
EKLLADKTTL VAGSVVMAFE EVCPERIDLI HKNYRKLCNL LIDVEEWGQV VIINMLTRYA
RTQFLNPNIN ESLLEEGGGG DKTFYGSDED EDEDEEEKEK KAEAAAMAKR KPYVMDPDHR
LLLRNTKPLL QSRNAAVVMA VAQLYFHLAP KAEVGVIAKA LVRLLRSHSE VQYVVLQNVA
TMTIKRRGMF EPYLKSFYIR STDPTQIKIL KLEVLTNLAN ETNISTILRE FQTYIKSMDK
DFVAATIQAI GRCATNIGEV RDTCLNGLVQ LLSNRDELVV AESVVVIKKL LQMQPEKHSD
IIKHMAKLTD NIQVPMARAS ILWLIGEYCE HVPKIAPDVL RKMAKSFTNE EDIVKLQILN
LAAKLYLTNS KQTKLLTQYV LNLAKYDQNY DIRDRARFIR QLIVPTEKSG ALSKYAKKLF
LALKPAPVLE SPFKAWWKIV SVPEWTKCSS REKRKEKKVE KPFYSDSEGE SGPTESADSE
SDSASGSESG SEGSGLASES EESGEVSVSE EDEEEEEEEN KTKKRELKKV VQESESSVSL
NVDFHLFLPV EPAPSPQVTP VNNLLSNSLV TDLEGLSLSE AVLALKSYEL LHRITGEGLS
VEYCFSRQPF SPDANMVAVQ MQFTNSSTSD TKSLHMEDVK LQSGMRVKEF PEIEXLPAGE
TATAVMGIDF CDSTQAANFQ LCTHTRKFFV SIQPPVGELM RPVFLTENEF KKEQGQLMGM
NEITEKLILD AKCRNEHAIV QRVTTAANLS RVPCGSDKEF AGRTVTSGSL VLVTVATREE
GAAQLTINCE KMVIGTMLVK DILLALTQ
//
