A16L2_CAEEL
ID A16L2_CAEEL Reviewed; 534 AA.
AC Q09406;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Autophagic-related protein 16.2;
GN Name=atg-16.2 {ECO:0000312|WormBase:K06A1.5};
GN ORFNames=K06A1.5 {ECO:0000312|WormBase:K06A1.5};
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-16.1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP HIS-331 AND 533-TRP-ARG-534.
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).
RN [4]
RP FUNCTION.
RX PubMed=28285998; DOI=10.1016/j.cub.2017.02.015;
RA Ames K., Da Cunha D.S., Gonzalez B., Konta M., Lin F., Shechter G.,
RA Starikov L., Wong S., Buelow H.E., Melendez A.;
RT "A Non-Cell-Autonomous Role of BEC-1/BECN1/Beclin1 in Coordinating Cell-
RT Cycle Progression and Stem Cell Proliferation during Germline
RT Development.";
RL Curr. Biol. 27:905-913(2017).
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). Plays a role in the recruitment of
CC lipidated lgg-1 probably to the autophagosome membrane to promote
CC autophagosome formation (PubMed:24185444). Furthermore, association
CC with atg-5 is required for the nucleation of lgg-1 positive
CC autophagosomes (PubMed:24185444). 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-16.1 to regulate autophagic
CC processes (PubMed:24185444, PubMed:28285998). In a daf-18/PTEN- and
CC daf-16/FOXO-dependent manner, required for maintaining the numbers of
CC germ stem cell progenitors in the gonad during the late phases of
CC larval development (PubMed:28285998). {ECO:0000269|PubMed:24185444,
CC ECO:0000269|PubMed:26687600, ECO:0000269|PubMed:28285998}.
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-16.1
CC (via N-terminus) (PubMed:24185444). Interacts (via N-terminus) with
CC atg-5 (PubMed:24185444). Interacts (via WD 5-6 repeats) 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}. Cell
CC membrane {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}.
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DR EMBL; BX284602; CCD72613.1; -; Genomic_DNA.
DR PIR; T34332; T34332.
DR RefSeq; NP_495299.2; NM_062898.3.
DR AlphaFoldDB; Q09406; -.
DR SMR; Q09406; -.
DR BioGRID; 39406; 11.
DR ComplexPortal; CPX-3863; atg-5-atg-12-atg-16.1-atg-16.2 complex.
DR ComplexPortal; CPX-3866; atg-5-atg-12-atg-16.2 complex.
DR DIP; DIP-27464N; -.
DR STRING; 6239.K06A1.5; -.
DR EPD; Q09406; -.
DR PaxDb; Q09406; -.
DR PeptideAtlas; Q09406; -.
DR EnsemblMetazoa; K06A1.5.1; K06A1.5.1; WBGene00019427.
DR GeneID; 174067; -.
DR KEGG; cel:CELE_K06A1.5; -.
DR CTD; 174067; -.
DR WormBase; K06A1.5; CE39948; WBGene00019427; atg-16.2.
DR eggNOG; KOG0288; Eukaryota.
DR GeneTree; ENSGT00940000153936; -.
DR HOGENOM; CLU_000288_57_10_1; -.
DR InParanoid; Q09406; -.
DR OMA; LFVWEVN; -.
DR OrthoDB; 404224at2759; -.
DR PhylomeDB; Q09406; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR PRO; PR:Q09406; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00019427; Expressed in embryo and 4 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035973; P:aggrephagy; IMP:WormBase.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IC:ComplexPortal.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEP:WormBase.
DR GO; GO:0036093; P:germ cell proliferation; IMP:UniProtKB.
DR GO; GO:0042078; P:germ-line stem cell division; IMP:UniProtKB.
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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cell membrane; Cytoplasm; Membrane; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..534
FT /note="Autophagic-related protein 16.2"
FT /id="PRO_0000051509"
FT REPEAT 243..281
FT /note="WD 1"
FT REPEAT 288..329
FT /note="WD 2"
FT REPEAT 330..368
FT /note="WD 3"
FT REPEAT 371..411
FT /note="WD 4"
FT REPEAT 413..452
FT /note="WD 5"
FT REPEAT 459..498
FT /note="WD 6"
FT REPEAT 504..534
FT /note="WD 7"
FT MUTAGEN 331
FT /note="H->Y: Does not impair function (unlike the
FT corresponding mutation in atg-16.1, which causes defects in
FT autophagy)."
FT /evidence="ECO:0000269|PubMed:24185444"
FT MUTAGEN 533..534
FT /note="Missing: In bp636; results in defective degradation
FT of sqst-1."
FT /evidence="ECO:0000269|PubMed:24185444"
SQ SEQUENCE 534 AA; 60496 MW; 85B5EF2504DB7830 CRC64;
MTDNRTSFRL EILNRLCKRE RQQRCVKDMF KNYSLLDEQL QQSHRSRSVS VNDEHFKGNV
NDRLAVMKEE MANVYRMKSK NDQDLIDANR KLADSESRYS LVSSQRDKLR IETDAIVKKM
TVLENELAEL KEENSVINTE RVSLVATCNY LTEKKTQLDN ERFQLLNRIR ELQEKSAEFM
NAEIALQEER AQMRIREQIA KATADLNLGD ERASSAFGTS PETLDEFMMT DVLPSEVKFK
LSTHDGEVHD VEWMSDDTFA TAGSDSKVQI WRVSPNKTDA SKVSTLSGCL GPVNRLDYDS
QRHVCLASSN DKTCRLWNID SQRLLSTFSG HTDKVSSARL FQSHNVISGS ADRTIKNWDI
SSIRCLKSYL VGSTVFDIVA KCGVSQSSFI SSHFDKKVRF WDARSSDATY SVELGQKVSS
LDISMDGLQV LASSRDDTLS LIDVRNYGII HLYSAEQYKT SCDSTRAIFS STGEYVLAGS
SNSSVFIWNT KTTKLEKVVK TARSDSAQIM SLAWNPSGRG LLACDRQKTC TLWR
