ID   A0A3Q3T1C7_9TELE        Unreviewed;      1001 AA.
AC   A0A3Q3T1C7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=AP-3 complex subunit beta {ECO:0000256|PIRNR:PIRNR037096};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000034355.2, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000034355.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q3T1C7; -.
DR   STRING; 205130.ENSMAMP00000034355; -.
DR   Ensembl; ENSMAMT00000035229.2; ENSMAMP00000034355.2; ENSMAMG00000023084.2.
DR   GeneTree; ENSGT00940000156817; -.
DR   Proteomes; UP000261640; 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; 2.
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:UP000261640};
KW   Transport {ECO:0000256|PIRNR:PIRNR037096}.
FT   DOMAIN          750..867
FT                   /note="AP-3 complex subunit beta C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01355"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..689
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..742
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1001 AA;  111825 MW;  DD594BAC7794CD8B CRC64;
     MSASSAFNDE KGGSSSVGEP EYGHDPASGG IFSSDYKRHD DLKEMLDSNK DSLKLEAMKR
     IVAMIARGKN ASDLFPAVVK NVACKNIEVK KLVYVYLVRY AEEQQDLALL SISTFQRGLK
     DPNQLIRASA LRVLSSIRVT IIVPIMMLAI KEAASDMSPY VRKTAAHAIP KLYSLDPEQK
     DQLIEVIEKL LADKTTLVAG SVVMAFEEVC PERIDLIHKN YRKLCNLLID VEEWGQVVII
     NMLTRYARTQ FLNPNINESL LEEGGGGEKT FYGSDEDEDE DEEEKEKKVE VAALAKRKPY
     VMDPDHRLLL RNTKPLLQSR NAAVVMAVAQ LYFHLAPKAE VGVIAKALVR LLRSHSEVQF
     VVLQNVATMT IKRRGMFEPY LKSFYIRSTD PTQIKVLKLE VLTNLANETN ISTILREFQT
     YIKSMDKDFV AATIQAIGRC ATNISEVRDT CLNGLVQLLS NRDELVVAES VVVIKKLLQM
     QPEKHSDIIK HMAKLTDNIQ VPMARASILW LIGEYCEHVP KIAPDVLRKM AKSFTNEEDI
     VKLQIINLSA KLYLTNSKQT KLLTQYVLNL AKYDQNYDIR DRARFIRQLI VPTEKSGALS
     KYAKKLFLAL KPAPVLESPF KDRDHFQLGS LSHLLNAKAG GYQELPDWPE AAPDPSVRNV
     EVKESVPEWT KCSSREKRKE KKVEKPFYSD SEGESGPTES ADSESDSASG SESGSGSEES
     GSGSESEESE EGSESEEEEE DEEEKDKKKK KKKELKKPVN HFSSPRPLQT IAPSSALKSY
     ELLHRITGEG LQVEYCFSRQ PFSPDANMVA VQMQFTNNAT SDTKNLHMED VKLQSGMRVK
     EFPEIELLPA GETSTAVMGI DFCDSTQAAN FQLCTHTKKF FVSIQPPVGE LMRPIFLTEN
     EAVANLRLMG MNEITEKLTL DAKCRNEHTI VQRVTSAANL SRVPCGSDKE CRFAGRTVTS
     GSLVLVTVAT KEEGAAQLTV NCEKMVIGTM LVKDILLALT Q
//