ID A0A2K5I3L8_COLAP Unreviewed; 1083 AA.
AC A0A2K5I3L8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=AP-3 complex subunit beta {ECO:0000256|PIRNR:PIRNR037096};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000011112.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000011112.1}
RP IDENTIFICATION.
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 RefSeq; XP_011809280.1; XM_011953890.1.
DR AlphaFoldDB; A0A2K5I3L8; -.
DR Ensembl; ENSCANT00000034007.1; ENSCANP00000011112.1; ENSCANG00000028939.1.
DR GeneID; 105520271; -.
DR CTD; 8120; -.
DR OMA; HFLVRST; -.
DR OrthoDB; 7857at2759; -.
DR Proteomes; UP000233080; Unplaced.
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 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; 1.
DR Pfam; PF14796; AP3B1_C; 1.
DR PIRSF; PIRSF037096; AP3_complex_beta; 1.
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:UP000233080};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037096}.
FT DOMAIN 802..948
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 119511 MW; 749EF1532AEB4B21 CRC64;
MSAAPAYSED KGGSAGPGEP EYGHDPASGG IFSSDYKRHD DLKEMLDTNK DSLKLEAMKR
IVAMIARGKN ASDLFPAVVK NVACKNIEVK KLVYVYLVRY AEEQQDLALL SISTFQRGLK
DPNQLIRASA LRVLSSIRVP IIVPIMMLAI KEAASDMSPY VRKTAAHAIP KLYSLDSDQK
DQLIEVIEKL LADKTTLVAG SVVMAFEEVC PERIDLIHKN YRKLCNLLID VEEWGQVVII
SMLTRYARTQ FLSPTQNESL LEENAEKAFY GSEEDEAKGA GSEEKAAAAL PARKPYIMDP
DHRLLLRNTK PLLQSRSAAV VMAVAQLYFH LAPKAEVGVI AKALVRLLRS HSEVQYVVLQ
NVATMSIKRR GMFEPYLKSF YIRSTDPTQI KILKLEVLTN LANETNIPTV LREFQTYIRS
MDKDFVAATI QAIGRCATNI GRVRDTCLNG LVQLLSNRDE LVVAESVVVI KKLLQMQPAQ
HGEIIKHLAK LTDNIQVPMA RASILWLIGE YCEHVPRIAP DVLRKMAKSF TAEEDIVKLQ
VINLAAKLYL TNSKQTKLLT QYVLSLAKYD QNYDIRDRAR FTRQLIVPSE QGGALSRHAK
KLFLAPKPAP VLESSFKDRD HFQLGSLSHL LNAKATGYQE LPDWPEEAPD PSVRNVEVPE
WTKCSNREKR KEKEKPFYSD SEGESGPTES ADSDPESESE SDSKSSSESG SGESSSESDN
EDQDEDEEKG RGSESEQSEE DGKRKTKKKK VPEGKGEASS SDEDSDSSSS TSESEMTSES
EEEQLEPASW RRKTPPSSKR APATKEISLL DLEDFTPPSV QPVSPPAIVS TSLAADLEGL
TLTDSTLVPS LLSPVSRVGR QELLHRVAGE GLVVDYTFSR QPFSGDPHMV SVHIHFSNSS
DTPIKGLHVG TPKLPAGISI QEFPEIESLA PGESATAVMG INFCDSTQAA NFQLCTQTRQ
FYVSIQPPVG ELMAPVFMSE NEFKKEQGKL MGMNEITEKL MLPDTCRSDH TVVQKVTATA
NLGRVPCGTS DEYRFAGRTL TSGSLVLLTL DARPAGAAQL TVNSEKMVIG TMLVKDVIQA
LTQ
//