A16L1_CAEEL
ID A16L1_CAEEL Reviewed; 527 AA.
AC Q19124;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Autophagic-related protein 16.1;
GN Name=atg-16.1 {ECO:0000312|WormBase:F02E8.5};
GN ORFNames=F02E8.5 {ECO:0000312|WormBase:F02E8.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBUNIT, INTERACTION WITH ATG-5 AND ATG-16.2, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP HIS-326.
RX PubMed=24185444; DOI=10.4161/auto.26095;
RA Zhang H., Wu F., Wang X., Du H., Wang X., Zhang H.;
RT "The two C. elegans ATG-16 homologs have partially redundant functions in
RT the basal autophagy pathway.";
RL Autophagy 9:1965-1974(2013).
RN [3]
RP FUNCTION, AND INTERACTION WITH LGG-2.
RX PubMed=26687600; DOI=10.1016/j.molcel.2015.11.019;
RA Wu F., Watanabe Y., Guo X.Y., Qi X., Wang P., Zhao H.Y., Wang Z.,
RA Fujioka Y., Zhang H., Ren J.Q., Fang T.C., Shen Y.X., Feng W., Hu J.J.,
RA Noda N.N., Zhang H.;
RT "Structural Basis of the Differential Function of the Two C. elegans Atg8
RT Homologs, LGG-1 and LGG-2, in Autophagy.";
RL Mol. Cell 60:914-929(2015).
CC -!- FUNCTION: Most likely a component of the atg-5-atg-12-atg-16.1/atg-16.2
CC complex, which is recruited to the preautophagosomal membrane and
CC associates with lgg-2 to promote autophagosome formation
CC (PubMed:24185444, PubMed:26687600). Although its role in autophagosome
CC formation may be distinct to the role of atg-16.2, it functions in a
CC partially redundant manner with atg-16.2 to regulate autophagic
CC processes (PubMed:24185444). {ECO:0000269|PubMed:24185444,
CC ECO:0000269|PubMed:26687600}.
CC -!- SUBUNIT: Homodimer (via N-terminus) (PubMed:24185444). Most likely a
CC component of a complex at least containing atg-5, lgg-3, atg-16.1
CC and/or atg-16.2 (Probable). Interacts (via N-terminus) with atg-16.2
CC (via N-terminus) (PubMed:24185444). Interacts (via N-terminus) with
CC atg-5 (PubMed:24185444). Interacts (via WD domain) with lgg-2; the
CC interaction is direct (PubMed:26687600). {ECO:0000269|PubMed:24185444,
CC ECO:0000269|PubMed:26687600, ECO:0000305|PubMed:24185444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24185444}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons, pharyngeal muscles, body wall
CC muscle cells and intestinal cells. {ECO:0000269|PubMed:24185444}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000305|PubMed:24185444}.
CC -!- SIMILARITY: Belongs to the WD repeat tipD family. {ECO:0000305}.
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; BX284606; CCD83386.1; -; Genomic_DNA.
DR PIR; T15958; T15958.
DR RefSeq; NP_508768.1; NM_076367.3.
DR AlphaFoldDB; Q19124; -.
DR SMR; Q19124; -.
DR BioGRID; 45652; 4.
DR ComplexPortal; CPX-3863; atg-5-atg-12-atg-16.1-atg-16.2 complex.
DR ComplexPortal; CPX-3865; atg-5-atg-12-atg-16.1 complex.
DR STRING; 6239.F02E8.5; -.
DR EPD; Q19124; -.
DR PaxDb; Q19124; -.
DR PeptideAtlas; Q19124; -.
DR EnsemblMetazoa; F02E8.5.1; F02E8.5.1; WBGene00017178.
DR GeneID; 180717; -.
DR KEGG; cel:CELE_F02E8.5; -.
DR CTD; 180717; -.
DR WormBase; F02E8.5; CE53669; WBGene00017178; atg-16.1.
DR eggNOG; KOG0288; Eukaryota.
DR GeneTree; ENSGT00940000153936; -.
DR HOGENOM; CLU_000288_57_10_1; -.
DR InParanoid; Q19124; -.
DR OrthoDB; 404224at2759; -.
DR PhylomeDB; Q19124; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR PRO; PR:Q19124; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017178; Expressed in embryo and 3 other tissues.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IC:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0034045; C:phagophore assembly site membrane; IC:ComplexPortal.
DR GO; GO:0035973; P:aggrephagy; IGI:WormBase.
DR GO; GO:0000045; P:autophagosome assembly; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IC:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; IC:ComplexPortal.
DR GO; GO:0006497; P:protein lipidation; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR045160; ATG16.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19878; PTHR19878; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..527
FT /note="Autophagic-related protein 16.1"
FT /id="PRO_0000051501"
FT REPEAT 239..277
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 283..324
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 325..363
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 365..406
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 408..447
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 454..493
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 497..527
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT MUTAGEN 326
FT /note="H->Y: In qx57; results in defective degradation of
FT sqst-1, pgl-1 and sepa-1 protein aggregates."
FT /evidence="ECO:0000269|PubMed:24185444"
SQ SEQUENCE 527 AA; 59425 MW; 269C465A1CC7503A CRC64;
MADSYRKLII ERLEDVKQRN KQTATLYNNY SKLAEQLEKK HKYGTSSSNS SQLETGELAR
VKEEMAELYR SKCQNDQRLI DANHRIADFE KKSSAIIAEK IALEATAKSI CAKYAKTEVE
LQRLKVDNDQ LNDERIASNT TVTMLTKQIQ DIENDRIHFL NKIRELNEQR VDFLNAEVAL
EEKRRNSRIQ DMITSAVQDI TDKDTKLEEM LRAMPDTNSN GDLLLGDSVP SRAEFVLECE
EGEVNDVHWL DGETFATGGS DRNIKIWKVD GHGGYTRIGT LAGSNAAFTR IDYERDRKHF
IASSNDKNVR IWNLDNSRLL STLSGHSDQV TCVKFYQSHS AVSGSADRVI KIWDIQNQRC
SRSLFPASKV LDVATNMGAS PSLFASGHFD KKLRFYDGRS TDPVRTVDMG GRITSLDVTM
SGCELLVSTR DDTISLIDLR TFQTVHCYSA ENYRTSSDLS RVVLSSGNEY VAAGSSNGSI
FVWNRNSTKL EKQLCSNSEN AIFSLSWNPT GYGLLSSSKQ KFVTLWK
