A16L1_MOUSE
ID A16L1_MOUSE Reviewed; 607 AA.
AC Q8C0J2; Q6KAT7; Q80U97; Q80U98; Q80U99; Q80Y53; Q9DB63;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Autophagy-related protein 16-1 {ECO:0000305};
DE AltName: Full=APG16-like 1 {ECO:0000303|PubMed:18849966};
GN Name=Atg16l1 {ECO:0000303|PubMed:18849966, ECO:0000312|MGI:MGI:1924290};
GN Synonyms=Apg16l {ECO:0000303|PubMed:12665549};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ATG5, AND SUBUNIT.
RX PubMed=12665549; DOI=10.1242/jcs.00381;
RA Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M., Takao T.,
RA Natsume T., Ohsumi Y., Yoshimori T.;
RT "Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic
RT isolation membrane with the Apg12-Apg5 conjugate.";
RL J. Cell Sci. 116:1679-1688(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Fetal brain;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH RAB33B.
RX PubMed=18448665; DOI=10.1091/mbc.e07-12-1231;
RA Itoh T., Fujita N., Kanno E., Yamamoto A., Yoshimori T., Fukuda M.;
RT "Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates
RT autophagosome formation.";
RL Mol. Biol. Cell 19:2916-2925(2008).
RN [6]
RP FUNCTION.
RX PubMed=18849966; DOI=10.1038/nature07416;
RA Cadwell K., Liu J.Y., Brown S.L., Miyoshi H., Loh J., Lennerz J.K.,
RA Kishi C., Kc W., Carrero J.A., Hunt S., Stone C.D., Brunt E.M.,
RA Xavier R.J., Sleckman B.P., Li E., Mizushima N., Stappenbeck T.S.,
RA Virgin H.W. IV;
RT "A key role for autophagy and the autophagy gene Atg16l1 in mouse and human
RT intestinal Paneth cells.";
RL Nature 456:259-263(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUBUNIT.
RX PubMed=22082872; DOI=10.4161/auto.7.12.18025;
RA Ishibashi K., Fujita N., Kanno E., Omori H., Yoshimori T., Itoh T.,
RA Fukuda M.;
RT "Atg16L2, a novel isoform of mammalian Atg16L that is not essential for
RT canonical autophagy despite forming an Atg12-5-16L2 complex.";
RL Autophagy 7:1500-1513(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH RB1CC1.
RX PubMed=23392225; DOI=10.1038/embor.2013.6;
RA Nishimura T., Kaizuka T., Cadwell K., Sahani M.H., Saitoh T., Akira S.,
RA Virgin H.W., Mizushima N.;
RT "FIP200 regulates targeting of Atg16L1 to the isolation membrane.";
RL EMBO Rep. 14:284-291(2013).
RN [10]
RP FUNCTION.
RX PubMed=24238340; DOI=10.1016/j.immuni.2013.10.013;
RA Sorbara M.T., Ellison L.K., Ramjeet M., Travassos L.H., Jones N.L.,
RA Girardin S.E., Philpott D.J.;
RT "The protein ATG16L1 suppresses inflammatory cytokines induced by the
RT intracellular sensors Nod1 and Nod2 in an autophagy-independent manner.";
RL Immunity 39:858-873(2013).
RN [11]
RP INTERACTION WITH RB1CC1.
RX PubMed=23262492; DOI=10.1038/nsmb.2475;
RA Gammoh N., Florey O., Overholtzer M., Jiang X.;
RT "Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-
RT dependent and -independent autophagy.";
RL Nat. Struct. Mol. Biol. 20:144-149(2013).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=24089209; DOI=10.1038/nature12639;
RA Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I.,
RA Codogno P., Satir B.H., Satir P., Cuervo A.M.;
RT "Functional interaction between autophagy and ciliogenesis.";
RL Nature 502:194-200(2013).
RN [13]
RP FUNCTION IN AUTOPHAGY, CLEAVAGE BY CASP3, AND MUTAGENESIS OF ASP-299 AND
RP THR-300.
RX PubMed=24553140; DOI=10.1038/nature13044;
RA Murthy A., Li Y., Peng I., Reichelt M., Katakam A.K., Noubade R.,
RA Roose-Girma M., Devoss J., Diehl L., Graham R.R., van Lookeren Campagne M.;
RT "A Crohn's disease variant in Atg16l1 enhances its degradation by caspase
RT 3.";
RL Nature 506:456-462(2014).
RN [14]
RP FUNCTION, INTERACTION WITH WIPI2 AND RB1CC1, AND SUBCELLULAR LOCATION.
RX PubMed=24954904; DOI=10.1016/j.molcel.2014.05.021;
RA Dooley H.C., Razi M., Polson H.E., Girardin S.E., Wilson M.I., Tooze S.A.;
RT "WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and
RT pathogen clearance by recruiting Atg12-5-16L1.";
RL Mol. Cell 55:238-252(2014).
RN [15]
RP MUTAGENESIS OF THR-300.
RX PubMed=24821797; DOI=10.1073/pnas.1407001111;
RA Lassen K.G., Kuballa P., Conway K.L., Patel K.K., Becker C.E.,
RA Peloquin J.M., Villablanca E.J., Norman J.M., Liu T.C., Heath R.J.,
RA Becker M.L., Fagbami L., Horn H., Mercer J., Yilmaz O.H., Jaffe J.D.,
RA Shamji A.F., Bhan A.K., Carr S.A., Daly M.J., Virgin H.W., Schreiber S.L.,
RA Stappenbeck T.S., Xavier R.J.;
RT "Atg16L1 T300A variant decreases selective autophagy resulting in altered
RT cytokine signaling and decreased antibacterial defense.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7741-7746(2014).
RN [16]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SPATA33.
RX PubMed=33087875; DOI=10.1038/s41418-020-00638-2;
RA Zhang Y., Xu X., Hu M., Wang X., Cheng H., Zhou R.;
RT "SPATA33 is an autophagy mediator for cargo selectivity in germline
RT mitophagy.";
RL Cell Death Differ. 28:1076-1090(2021).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF 231-PRO--PRO-607.
RX PubMed=33586810; DOI=10.15252/embj.2020105543;
RA Wang Y., Sharma P., Jefferson M., Zhang W., Bone B., Kipar A., Bitto D.,
RA Coombes J.L., Pearson T., Man A., Zhekova A., Bao Y., Tripp R.A.,
RA Carding S.R., Yamauchi Y., Mayer U., Powell P.P., Stewart J.P., Wileman T.;
RT "Non-canonical autophagy functions of ATG16L1 in epithelial cells limit
RT lethal infection by influenza A virus.";
RL EMBO J. 40:e105543-e105543(2021).
CC -!- FUNCTION: Plays an essential role in both canonical and non-canonical
CC autophagy: interacts with ATG12-ATG5 to mediate the lipidation to ATG8
CC family proteins (MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and
CC GABARAP) (PubMed:12665549, PubMed:18849966, PubMed:23392225,
CC PubMed:24553140, PubMed:24954904, PubMed:33586810). Acts as a molecular
CC hub, coordinating autophagy pathways via distinct domains that support
CC either canonical or non-canonical signaling (PubMed:33586810). During
CC canonical autophagy, interacts with ATG12-ATG5 to mediate the
CC conjugation of phosphatidylethanolamine (PE) to ATG8 proteins, to
CC produce a membrane-bound activated form of ATG8 (By similarity).
CC Thereby, controls the elongation of the nascent autophagosomal membrane
CC (By similarity). Also involved in non-canonical autophagy, a parallel
CC pathway involving conjugation of ATG8 proteins to single membranes at
CC endolysosomal compartments, probably by catalyzing conjugation of
CC phosphatidylserine (PS) to ATG8 (By similarity). Non-canonical
CC autophagy plays a key role in epithelial cells to limit lethal
CC infection by influenza A (IAV) virus (PubMed:33586810). Regulates
CC mitochondrial antiviral signaling (MAVS)-dependent type I interferon
CC (IFN-I) production (By similarity). Negatively regulates NOD1- and
CC NOD2-driven inflammatory cytokine response.Instead, promotes with NOD2
CC an autophagy-dependent antibacterial pathway (PubMed:24238340). Plays a
CC role in regulating morphology and function of Paneth cell (By
CC similarity). {ECO:0000250|UniProtKB:Q676U5,
CC ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:18849966,
CC ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:24238340,
CC ECO:0000269|PubMed:24553140, ECO:0000269|PubMed:24954904,
CC ECO:0000269|PubMed:33586810}.
CC -!- SUBUNIT: Homodimer (By similarity). Homooligomer (PubMed:12665549).
CC Heterooligomer with ATG16L2 (PubMed:22082872). Interacts with WIPI1 (By
CC similarity). Interacts with WIPI2 (PubMed:24954904). Interacts with
CC RB1CC1; the interaction is required for ULK1 complex-dependent
CC autophagy (PubMed:23392225, PubMed:23262492). Interacts with ATG5
CC (PubMed:12665549). 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). Interacts with RAB33B
CC (PubMed:18448665). Interacts (via WD repeats) with TMEM59; the
CC interaction mediates unconventional autophagic activity of TMEM59 (By
CC similarity). Interacts with TLR2 and NOD2 (By similarity). Interacts
CC (via WD repeats) with MEFV (By similarity). Interacts (via N-terminal)
CC with CLTC (By similarity). Interacts with NOD2 (By similarity).
CC Interacts with TUFM (By similarity). Interacts with TRIM16 (By
CC similarity). Interacts (via WD repeats) with SPATA33 (PubMed:33087875).
CC {ECO:0000250|UniProtKB:Q676U5, ECO:0000269|PubMed:12665549,
CC ECO:0000269|PubMed:18448665, ECO:0000269|PubMed:22082872,
CC ECO:0000269|PubMed:23262492, ECO:0000269|PubMed:23392225,
CC ECO:0000269|PubMed:24954904, ECO:0000269|PubMed:33087875}.
CC -!- INTERACTION:
CC Q8C0J2; Q99J83: Atg5; NbExp=4; IntAct=EBI-769195, EBI-2911848;
CC Q8C0J2; P23242: Gja1; NbExp=2; IntAct=EBI-769195, EBI-298630;
CC Q8C0J2; Q61025: Ift20; NbExp=2; IntAct=EBI-769195, EBI-16077253;
CC Q8C0J2; Q9ESK9: Rb1cc1; NbExp=4; IntAct=EBI-769195, EBI-647302;
CC Q8C0J2-2; Q8C0J2-2: Atg16l1; NbExp=2; IntAct=EBI-11580812, EBI-11580812;
CC Q8C0J2-3; Q9ESK9: Rb1cc1; NbExp=3; IntAct=EBI-16029274, EBI-647302;
CC Q8C0J2-3; Q9H1Y0: ATG5; Xeno; NbExp=2; IntAct=EBI-16029274, EBI-1047414;
CC Q8C0J2-3; Q8TDY2: RB1CC1; Xeno; NbExp=6; IntAct=EBI-16029274, EBI-1047793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33087875}.
CC Preautophagosomal structure membrane {ECO:0000269|PubMed:24954904};
CC Peripheral membrane protein {ECO:0000305}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q676U5}; Peripheral membrane protein
CC {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q676U5};
CC Peripheral membrane protein {ECO:0000305}. Note=Recruited to omegasomes
CC membranes by WIPI2 (PubMed:24954904). Omegasomes are endoplasmic
CC reticulum connected strutures at the origin of preautophagosomal
CC structures. Localized to preautophagosomal structure (PAS) where it is
CC involved in the membrane targeting of ATG5 (PubMed:24954904). Localizes
CC also to discrete punctae along the ciliary axoneme (PubMed:24954904).
CC Upon activation of non-canonical autophagy, recruited to single-
CC membrane endolysosomal compartments (By similarity).
CC {ECO:0000250|UniProtKB:Q676U5, ECO:0000269|PubMed:24954904}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Apg16Lbeta {ECO:0000303|PubMed:12665549};
CC IsoId=Q8C0J2-1; Sequence=Displayed;
CC Name=2; Synonyms=Apg16Lalpha {ECO:0000303|PubMed:12665549};
CC IsoId=Q8C0J2-2; Sequence=VSP_013391;
CC Name=3; Synonyms=Apg16Lgamma {ECO:0000303|PubMed:12665549};
CC IsoId=Q8C0J2-3; Sequence=VSP_013392;
CC Name=4;
CC IsoId=Q8C0J2-4; Sequence=VSP_013392, VSP_013394, VSP_013395;
CC Name=5;
CC IsoId=Q8C0J2-5; Sequence=VSP_013391, VSP_013393;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:12665549). Expressed in
CC the testis and sperm midpiece (at protein level) (PubMed:33087875).
CC {ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:33087875}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in liver.
CC {ECO:0000269|PubMed:12665549}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Highly expressed in liver.
CC {ECO:0000269|PubMed:12665549}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in brain.
CC {ECO:0000269|PubMed:12665549}.
CC -!- DOMAIN: The WD repeats are required for non-canonical autophagy but not
CC for canonical autophagy. {ECO:0000250|UniProtKB:Q676U5}.
CC -!- PTM: Proteolytic cleavage by activated CASP3 leads to degradation and
CC may regulate autophagy upon cellular stress and apoptotic stimuli.
CC {ECO:0000269|PubMed:24553140}.
CC -!- PTM: Phosphorylation at Ser-139 promotes association with the ATG12-
CC ATG5 conjugate to form the ATG12-ATG5-ATG16L1 complex.
CC {ECO:0000250|UniProtKB:Q676U5}.
CC -!- SIMILARITY: Belongs to the WD repeat ATG16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21370.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB087879; BAC55090.1; -; mRNA.
DR EMBL; AB087880; BAC55091.1; -; mRNA.
DR EMBL; AB087881; BAC55092.1; -; mRNA.
DR EMBL; AK005181; BAB23866.1; -; mRNA.
DR EMBL; AK030983; BAC27201.1; -; mRNA.
DR EMBL; AK131120; BAD21370.1; ALT_INIT; Transcribed_RNA.
DR EMBL; BC049122; AAH49122.1; -; mRNA.
DR CCDS; CCDS15136.1; -. [Q8C0J2-1]
DR CCDS; CCDS56637.1; -. [Q8C0J2-3]
DR CCDS; CCDS56638.1; -. [Q8C0J2-2]
DR RefSeq; NP_001192320.1; NM_001205391.1. [Q8C0J2-3]
DR RefSeq; NP_084122.2; NM_029846.4. [Q8C0J2-1]
DR PDB; 6SUR; X-ray; 3.47 A; I/J/K/L/M/N=154-210.
DR PDB; 6Y09; X-ray; 2.40 A; C/D=141-265.
DR PDB; 6ZAY; X-ray; 2.40 A; C/D=141-265.
DR PDBsum; 6SUR; -.
DR PDBsum; 6Y09; -.
DR PDBsum; 6ZAY; -.
DR AlphaFoldDB; Q8C0J2; -.
DR SMR; Q8C0J2; -.
DR BioGRID; 218476; 679.
DR ComplexPortal; CPX-328; Atg12-Atg5-Atg16l1 complex.
DR CORUM; Q8C0J2; -.
DR DIP; DIP-31966N; -.
DR IntAct; Q8C0J2; 14.
DR MINT; Q8C0J2; -.
DR STRING; 10090.ENSMUSP00000027512; -.
DR iPTMnet; Q8C0J2; -.
DR PhosphoSitePlus; Q8C0J2; -.
DR REPRODUCTION-2DPAGE; Q8C0J2; -.
DR EPD; Q8C0J2; -.
DR jPOST; Q8C0J2; -.
DR MaxQB; Q8C0J2; -.
DR PaxDb; Q8C0J2; -.
DR PeptideAtlas; Q8C0J2; -.
DR PRIDE; Q8C0J2; -.
DR ProteomicsDB; 286000; -. [Q8C0J2-1]
DR ProteomicsDB; 286001; -. [Q8C0J2-2]
DR ProteomicsDB; 286002; -. [Q8C0J2-3]
DR ProteomicsDB; 286003; -. [Q8C0J2-4]
DR ProteomicsDB; 286004; -. [Q8C0J2-5]
DR Antibodypedia; 1969; 878 antibodies from 43 providers.
DR DNASU; 77040; -.
DR Ensembl; ENSMUST00000027512; ENSMUSP00000027512; ENSMUSG00000026289. [Q8C0J2-1]
DR Ensembl; ENSMUST00000113186; ENSMUSP00000108811; ENSMUSG00000026289. [Q8C0J2-2]
DR Ensembl; ENSMUST00000113190; ENSMUSP00000108815; ENSMUSG00000026289. [Q8C0J2-3]
DR GeneID; 77040; -.
DR KEGG; mmu:77040; -.
DR UCSC; uc007bxl.2; mouse. [Q8C0J2-1]
DR CTD; 55054; -.
DR MGI; MGI:1924290; Atg16l1.
DR VEuPathDB; HostDB:ENSMUSG00000026289; -.
DR eggNOG; KOG0288; Eukaryota.
DR GeneTree; ENSGT00940000153936; -.
DR HOGENOM; CLU_000288_57_10_1; -.
DR InParanoid; Q8C0J2; -.
DR OMA; LFVWEVN; -.
DR PhylomeDB; Q8C0J2; -.
DR TreeFam; TF315541; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 77040; 15 hits in 76 CRISPR screens.
DR ChiTaRS; Atg16l1; mouse.
DR PRO; PR:Q8C0J2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C0J2; protein.
DR Bgee; ENSMUSG00000026289; Expressed in retinal neural layer and 249 other tissues.
DR ExpressionAtlas; Q8C0J2; baseline and differential.
DR Genevisible; Q8C0J2; MM.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IDA:ComplexPortal.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0000421; C:autophagosome membrane; IDA:MGI.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0036020; C:endolysosome membrane; ISS:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:ComplexPortal.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; ISS:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000045; P:autophagosome assembly; IMP:ComplexPortal.
DR GO; GO:0006501; P:C-terminal protein lipidation; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0016237; P:lysosomal microautophagy; IMP:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IMP:ComplexPortal.
DR GO; GO:0039689; P:negative stranded viral RNA replication; IMP:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:ARUK-UCL.
DR GO; GO:0006497; P:protein lipidation; ISO:MGI.
DR GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; IDA:MGI.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IPI:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0098792; P:xenophagy; IPI:MGI.
DR Gene3D; 2.130.10.10; -; 2.
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; 4.
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; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Coiled coil; Cytoplasm;
KW Endosome; Lysosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..607
FT /note="Autophagy-related protein 16-1"
FT /id="PRO_0000050849"
FT REPEAT 320..359
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 364..403
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 406..445
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 447..484
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 486..525
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 532..573
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 575..607
FT /note="WD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 13..43
FT /note="Interaction with ATG5"
FT /evidence="ECO:0000250|UniProtKB:Q676U5"
FT REGION 207..230
FT /note="WIPI2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q676U5"
FT REGION 230..242
FT /note="RB1CC1-binding"
FT /evidence="ECO:0000269|PubMed:23262492"
FT COILED 79..230
FT /evidence="ECO:0000255"
FT MOTIF 296..299
FT /note="Caspase cleavage"
FT /evidence="ECO:0000269|PubMed:24553140"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q676U5"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 266..284
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12665549,
FT ECO:0000303|PubMed:15449545"
FT /id="VSP_013391"
FT VAR_SEQ 284
FT /note="G -> GLSESPLLGHHSSDAAR (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12665549,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_013392"
FT VAR_SEQ 442
FT /note="C -> CEEMQSLCVLMVFGFLSG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15449545"
FT /id="VSP_013393"
FT VAR_SEQ 443..452
FT /note="IKTVFAGSSC -> EEMQSLCVFM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013394"
FT VAR_SEQ 453..607
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013395"
FT MUTAGEN 231..607
FT /note="Missing: Impaired non-canonical autophagy, leading
FT to susceptibility to influenza A virus (IAV) infection in
FT mice."
FT /evidence="ECO:0000269|PubMed:33586810"
FT MUTAGEN 299
FT /note="D->E: Prevents cleavage by activated CASP3."
FT /evidence="ECO:0000269|PubMed:24553140"
FT MUTAGEN 300
FT /note="T->A: No effect on the stability of the protein
FT under normal conditions. Enhances cleavage and degradation
FT mediated by activated CASP3 and CASP7. Results in reduced
FT autophagy and defective clearance of intestinal pathogens.
FT Increases secretion of pro-inflammatory cytokine IL1B and
FT type I IFN."
FT /evidence="ECO:0000269|PubMed:24553140,
FT ECO:0000269|PubMed:24821797"
FT CONFLICT 83
FT /note="Q -> H (in Ref. 1; BAC55090/BAC55091/BAC55092 and 2;
FT BAB23866)"
FT /evidence="ECO:0000305"
FT HELIX 145..167
FT /evidence="ECO:0007829|PDB:6Y09"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:6Y09"
FT HELIX 172..224
FT /evidence="ECO:0007829|PDB:6Y09"
SQ SEQUENCE 607 AA; 68172 MW; 63920320883A69DF CRC64;
MSSGLRAADF PRWKRHIAEE LRRRDRLQRQ AFEEIILQYT KLLEKSDLHS VLTQKLQAEK
HDMPNRHEIS PGHDGAWNDS QLQEMAQLRI KHQEELTELH KKRGELAQLV IDLNNQMQQK
DKEIQMNEAK ISEYLQTISD LETNCLDLRT KLQDLEVANQ TLKDEYDALQ ITFTALEEKL
RKTTEENQEL VTRWMAEKAQ EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI
EVIVDETSDH TEETSPVRAV SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS IPVPQDIMDT
HPASGKDVRV PTTASYVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE AFGDKCEFKG
SLSGSNAGIT SIEFDSAGAY LLAASNDFAS RIWTVDDYRL RHTLTGHSGK VLSAKFLLDN
ARIVSGSHDR TLKLWDLRSK VCIKTVFAGS SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES
VVREMELLGK ITALDLNPER TELLSCSRDD LLKVIDLRTN AVKQTFSAPG FKCGSDWTRV
VFSPDGSYVA AGSAEGSLYV WSVLTGKVEK VLSKQHSSSI NAVAWAPSGL HVVSVDKGSR
AVLWAQP
