ATG16_XENTR
ID ATG16_XENTR Reviewed; 622 AA.
AC Q5I0B9; Q28DG5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Autophagy-related protein 16;
DE AltName: Full=APG16-like 1;
GN Name=atg16; Synonyms=apg16l; ORFNames=TEgg115a02.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an essential role in autophagy: interacts with ATG12-
CC ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3
CC (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated
CC form of LC3 named LC3-II. Thereby, controls the elongation of the
CC nascent autophagosomal membrane. {ECO:0000250|UniProtKB:Q676U5}.
CC -!- SUBUNIT: Homooligomer. Part of either the minor and major complexes
CC respectively composed of 4 sets of ATG12-ATG5 and ATG16L1 (400 kDa) or
CC 8 sets of ATG12-ATG5 and ATG16L1 (800 kDa).
CC {ECO:0000250|UniProtKB:Q676U5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q676U5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q676U5}. Note=Recruited to omegasomes membranes
CC by WIPI2. Omegasomes are endoplasmic reticulum connected strutures at
CC the origin of preautophagosomal structures. Localized to
CC preautophagosomal structure (PAS) where it is involved in the membrane
CC targeting of ATG5. {ECO:0000250|UniProtKB:Q676U5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5I0B9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5I0B9-2; Sequence=VSP_020115;
CC -!- SIMILARITY: Belongs to the WD repeat ATG16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ82169.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR855526; CAJ82169.1; ALT_INIT; mRNA.
DR EMBL; BC088497; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001017343.1; NM_001017343.2. [Q5I0B9-1]
DR AlphaFoldDB; Q5I0B9; -.
DR SMR; Q5I0B9; -.
DR STRING; 8364.ENSXETP00000031538; -.
DR GeneID; 550097; -.
DR KEGG; xtr:550097; -.
DR CTD; 55054; -.
DR Xenbase; XB-GENE-1011170; atg16l1.
DR InParanoid; Q5I0B9; -.
DR OrthoDB; 404224at2759; -.
DR Reactome; R-XTR-1632852; Macroautophagy.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000013872; Expressed in ovary and 12 other tissues.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0039689; P:negative stranded viral RNA replication; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR045160; ATG16.
DR InterPro; IPR013923; Autophagy-rel_prot_16_dom.
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; PF08614; ATG16; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autophagy; Coiled coil; Cytoplasm; Membrane;
KW Protein transport; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..622
FT /note="Autophagy-related protein 16"
FT /id="PRO_0000050851"
FT REPEAT 335..374
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 379..418
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 421..460
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 462..499
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 501..540
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 547..588
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 590..622
FT /note="WD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..230
FT /note="WIPI2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q676U5"
FT REGION 230..242
FT /note="FIP200-binding"
FT /evidence="ECO:0000250|UniProtKB:Q676U5"
FT REGION 244..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..230
FT /evidence="ECO:0000255"
FT COMPBIAS 257..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 216..300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_020115"
SQ SEQUENCE 622 AA; 69723 MW; AC2C794CFB8FA0AE CRC64;
MAAGCRGPAC PSWRLHISRE LRRRDREQRQ VFEELISQYK RLLEKSDLQS VLADKLQAEK
YEQQSRHDSS PGPDGMRNDM LLQDMAQMRI KHQEELTELH KKRGELAQTV IELNNQMQQK
DKEIQANEEK IAKYLQTIQD LETECQDLRN KLQELERANQ TLKDEYDALQ ITFTALEDKL
RKTTEDNQEL VSRWMAEKAQ EANRLNAENE KDSKRRQARL QKELAEAAKE PLSFEHDDDI
EVLNDNADPV GDSAGAQATG RNISKRNSQP AVGGLLDSIT NIFGLSESPS LSHRSDSSRR
RSLNSFPASP DCADTPGAGN REVRVPATAV YSFDAHDGEV NAVRFSPGSR LLATGGMDRR
VKLWDVIGNK CEAKGSLTGS NAGITSIEFD SAGSYLLAAS NDFASRIWTV DDYRLRHTLT
GHSGKVLSAK FLLDNARIVS GSHDRTLKLW DLRSKVCIKT VFAGSSCNDI VCTEQCVMSG
HFDKKIRFWD IRTECIVREL ELQGRITALD LNPERTQLLS CSRDDLIKIT DLRANAVQQT
FSAPGFKCGS DWTRVIFSPD GSYVSAGSAE GTLYFWNVLT GKVERMFSKQ HSSSINAVAW
SPSGTHVVSV DKGSRGVLWS DF
