ID L5KLM4_PTEAL Unreviewed; 1087 AA.
AC L5KLM4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=AP-3 complex subunit beta {ECO:0000256|PIRNR:PIRNR037096};
GN ORFNames=PAL_GLEAN10024916 {ECO:0000313|EMBL:ELK11458.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK11458.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB030673; ELK11458.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KLM4; -.
DR STRING; 9402.L5KLM4; -.
DR eggNOG; KOG1060; Eukaryota.
DR InParanoid; L5KLM4; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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; IPR029394; AP3B1_Ser.
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 Pfam; PF14797; SEEEED; 1.
DR PIRSF; PIRSF037096; AP3_complex_beta; 1.
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:UP000010552};
KW Transport {ECO:0000256|PIRNR:PIRNR037096}.
FT DOMAIN 804..951
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT DOMAIN 975..1085
FT /note="Beta-adaptin appendage C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01020"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..726
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 121063 MW; FEA21F44F9A5C09D CRC64;
MSSNSFAYNE QSGGGEATEL GQEATATISP SGAFGLFSSD LKKNEDLKQM LESNKDSAKL
EAMKRIVGMI AKGKNASELF PAVVKNVASK NIEIKKLVYV YLVRYAEEQQ DLALLSISTF
QRALKDPNQL IRASALRVLS SIRVPIIVPI MMLAIKEASA DLSPYVRKNA AHAIQKLYSL
DPEQKEMLIE VIEKLLKDKS TLVAGSVVMA FEEVCPDRID LIHKNYRKLC NLLVDVEEWG
QVVIIHMLTR YARTQFVSPW KEDDGLQDNE KNFYESDDEQ KEKTEKKKFY TMDPDHRLLI
RNTKPLLQSF KTFIVVMAVA QLYWHIAPKS EAGIISKSLV RLLRSNREVQ YIVLQNIATM
SIQRKGMFEP YLKSFYVRST DPTMIKTLKL EILTNLANEA NISTLLREFQ TYVKSQDKQF
AAATIQTIGR CATNISEVTD TCLNGLVCLL SNRDEIVVAE SVVVIKKLLQ MQPAQHGEII
KHMAKLLDSI TVPVARASIL WLTGENCERV PKIAPDVLRK MAKNFTSEDD LVKLQILNLG
AKLYLTNSKQ TKLLTQYILN LGKYDQNYDI RDRTRFIRQL IVPNEKSGAL SKYAKKIFLA
QKPAPLLESP YKDRDHFQLG TLSHTLNTKA TGYLELSNWP EVAPDPSVRN VEVIELAKEW
TPAGKAKKEN PAKKFYSESE EEEDSSDSSS DSESESASES GEQDEEGDSS DESSEDSSSE
SESESGSESE VENRRDKNSK TKGKGDSEYG EKENENSETS DSSNEESSSI EESSSDSESE
SENELESRKV TKEKEKKTKQ DRKPVTKDVS LLDLDDFNPV STPVALPMPA FSPSLIADLE
GLNLSTSSSV ISVSTPVFVP MKTHVLLHRM SGKGLAAHYF FPRQPCIFGD KMVSVQITLS
NTTDRKIENI HTGQKKLPTG MQMHVFNPIE SLEPEGSITV SMGIDFCDST QTASFQLCTK
DDCFNVNIQP PVGELLLPVA ISEKDFKKEQ GMLTGMNETS TIIIVAPQNF TSSVILQKVV
NVANVGVVPS GQDNIHRFAA KTVHSGSLML VTVELKEGST AQLIINTEKT VIGSVLLREL
KPVLSQG
//
