ID A0A3P9Q1T4_POERE Unreviewed; 977 AA.
AC A0A3P9Q1T4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=AP-3 complex subunit beta {ECO:0000256|PIRNR:PIRNR037096};
GN Name=AP3B1 {ECO:0000313|Ensembl:ENSPREP00000027969.1};
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:ENSPREP00000027969.1, 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:ENSPREP00000027969.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000027969.1};
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 AlphaFoldDB; A0A3P9Q1T4; -.
DR Ensembl; ENSPRET00000028276.1; ENSPREP00000027969.1; ENSPREG00000018892.1.
DR GeneTree; ENSGT00940000157603; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000018892; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0030123; C:AP-3 adaptor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030131; C:clathrin 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; 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; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR PANTHER; PTHR11134:SF10; AP-3 COMPLEX SUBUNIT BETA-1; 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 SMART; SM01020; B2-adapt-app_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:UP000242638};
KW Transport {ECO:0000256|PIRNR:PIRNR037096}.
FT DOMAIN 722..841
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT DOMAIN 865..975
FT /note="Beta-adaptin appendage C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01020"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 108984 MW; BE9F705433E0D246 CRC64;
STSNSFSLYN DQQGGAEAAV EAGQETTATS SSGGAAFGLF STDFKKNEDL KEMLESNKES
LKLEAMKRIV QLISKGKNAS DLFPAVVKNV ASKNIELKKL VYVYLVRYAE EQQDLALLSI
STFQRALKDP NQFIRASALR VLSSIRVPII VPIMMLAIKE AASDLSPYVR KTSAHAIQKL
YSLDADQKEH LIEVIEKLLK DKSTLVAGSV VVAFEEVCPD RIDLIHRNYR KLCNLLVDVE
EWGQVVIINM LTRYARTQFT SPWKEDGIFD ESEKAFYDSD SEEKQGQREA KPYIMDPDHR
LLLRNTKPLL QSRNTASFFV RHVLLVCILR LFSFLFSCRE VQYVVLQNIA TMSIQRKGMF
EPYMKSFYVR STDATHIKTL KLEILTNLAN EANISTILRE FQTYVKSQDK AFAAATIQAI
GRCATNISEV TDTCLNGLVL LLSNRDETVV AESVVVIKKL LQTQPTQHCD IIKHMAKLFD
NITVPMARAS ILWLMGEYCE RVPKIAPDVL RKMAKTFTSE EDIVKLQTVN LAAKLYLTNS
KQTKLLTQYI LNLGKYDQNY DIRDRTRFIR QLIVPSEKSG ALNKYARRIL LASKPAPVLE
SAFKDRDRFQ LGTLSHSLNI KTTGYQELSD WPAAAPDPSV RNVEVIEPVQ EWAPSLGKAK
KPKSDDRFYS DDEEEKEKEG SGSGSEDSSS SSSGSSSSSS SSEGMFNLSE IQYVDKMCRD
LSRRIDPSWL PVSVTDFIPI SLQVTSSPFG PVKTHELLHH MTGKGLSAKY HFPRQPCLYQ
PSMVAVQVIL TNSSDHSLEE IHIGDRSPGS LNVHCFNSVE RLEPGASVSV SMGIDFSDST
QAANFQLCTK EDQFSVSIQP AVGELLMPST MKEPDFCSEQ KKLMGMNETS ATITMATANT
SKQNISKQVL SVANVGVVSS DQNNLQRFAG RTVSSGALVL VTLELRESST ALLTINTEKT
VMASMLLRDL KQALFQA
//
