ID A0A261BWQ1_9PELO Unreviewed; 902 AA.
AC A0A261BWQ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=AP-3 complex subunit beta C-terminal domain-containing protein {ECO:0000259|SMART:SM01355};
DE Flags: Fragment;
GN ORFNames=FL83_10872 {ECO:0000313|EMBL:OZG14737.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG14737.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG14737.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG14737.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG14737.1}.
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DR EMBL; NIPN01000064; OZG14737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261BWQ1; -.
DR STRING; 1503980.A0A261BWQ1; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR GO; GO:0030123; C:AP-3 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; IPR002553; Clathrin/coatomer_adapt-like_N.
DR PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR PANTHER; PTHR11134:SF1; AP-3 COMPLEX SUBUNIT BETA; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF14796; AP3B1_C; 1.
DR PIRSF; PIRSF037096; AP3_complex_beta; 3.
DR SMART; SM01355; AP3B1_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000216463}.
FT DOMAIN 671..783
FT /note="AP-3 complex subunit beta C-terminal"
FT /evidence="ECO:0000259|SMART:SM01355"
FT REGION 583..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..660
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG14737.1"
SQ SEQUENCE 902 AA; 101459 MW; FE4392C485D34C7C CRC64;
MTSFVEGLTS PEMEIAEGGV ILDNRTRFAD LKAMLDSNKD NLKVDAMKRI INLIAKGKDV
SELFAAVVKN VAAKNVELKK LVFVYLVRYA EEQQDLALLS ISTFQRALKD PNQLIRGSAL
RVLTSIRVPM VAPIMLLAIK DAVRDMSPYV RKVAAHAIPK LYSLEPELEP QLVDCIDFLL
ADRRSLVLGS AVYAFDEICP HRLDLLHKHF RALCRGLADV DEWGQIVMIN MLTRYSRHEL
ADPDRSPPDT DIVLLLNSAR PLLQSRNCSV VMAVIARALV RLLRGPRETQ YVVLTNIATI
CEQNPVEEGT FAISKTMFDP FLKSFFVRSC DSSLVKQLKL HVLTSLVSES NVHIILRELQ
TYVHMSDLAS PAVEAIGRCA VRVGAVSDQC MTGLVQLISS SDEKVVCSAV VVIKRLLHAS
APLNLLSRLM RLMPKMIAAQ ARACVIWLVA THVDQVIHMA PDFLRLIAKK FSTESELVKL
EALKLAVKLW LVKRDDSEKI VQYVFQLARF DLSYDVRDRC RFLRNLMFNT EILSQHMEEI
FMSKKPAPEL ISSFKERDQF QLGSLSHVLN QRCTKYIDLP EFPAASSDPT LRKEAHAPNE
LKLDEDSDEE SGEEEDEDEE EDEEESGEDS EDDDDEEESE EESEEDEDEE EVEEEEEEED
KSVNGKSKPS ESNALDLLID VDFSAAGSRQ IMNPTHIESK EIELLNVIEG QGLSLSISYP
RINDGQYTAI RFGITNKTDE DLEGIELKSA EGLDVKGNSR IERIPAGSRV SVDLLIDFGD
SATSREWILS RDDGQQKHFR FEVPYGEQVQ PIRLSSEDIS KEKSRLGGLN RHVIQLEHPI
DASRIPEVVN VFRSEDSGVF TCQTRSRKDV CILTLNGEKT IECCCDNSVI GRMLAFAVSK
NC
//