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Database: UniProt
Entry: A0A2K5I3L8_COLAP
LinkDB: A0A2K5I3L8_COLAP
Original site: A0A2K5I3L8_COLAP 
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
//
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