GenomeNet

Database: UniProt
Entry: A0A261BWQ1_9PELO
LinkDB: A0A261BWQ1_9PELO
Original site: A0A261BWQ1_9PELO 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system