GenomeNet

Database: UniProt
Entry: A16L2_MOUSE
LinkDB: A16L2_MOUSE
Original site: A16L2_MOUSE 
ID   A16L2_MOUSE             Reviewed;         623 AA.
AC   Q6KAU8; D3Z653; G9M4M8; Q6PAU0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Protein Atg16l2 {ECO:0000305};
DE   AltName: Full=APG16-like 2;
DE   AltName: Full=Autophagy-related protein 16-2;
GN   Name=Atg16l2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, SUBUNIT,
RP   INTERACTION WITH ATG5 AND RAB33B, AND SUBCELLULAR LOCATION.
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   [5]
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   [6]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=31451676; DOI=10.4049/jimmunol.1800419;
RA   Khor B., Conway K.L., Omar A.S., Biton M., Haber A.L., Rogel N., Baxt L.A.,
RA   Begun J., Kuballa P., Gagnon J.D., Lassen K.G., Regev A., Xavier R.J.;
RT   "Distinct Tissue-Specific Roles for the Disease-Associated Autophagy Genes
RT   ATG16L2 and ATG16L1.";
RL   J. Immunol. 203:1820-1829(2019).
CC   -!- FUNCTION: May play a role in regulating epithelial homeostasis in an
CC       ATG16L1-dependent manner. {ECO:0000269|PubMed:31451676}.
CC   -!- SUBUNIT: Homooligomer (PubMed:22082872). Heterooligomer with ATG16L2
CC       (PubMed:22082872). Interacts with ATG5 (PubMed:22082872). Self-
CC       oligomerizes to form a 800-kDa complex composed of ATG12-ATG5 and
CC       ATG16L2 (PubMed:22082872). Interacts with RAB33B (PubMed:22082872).
CC       {ECO:0000269|PubMed:22082872}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22082872}.
CC       Note=Localizes also to discrete punctae along the ciliary axoneme.
CC       {ECO:0000269|PubMed:24089209}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Atg16L2 beta {ECO:0000303|PubMed:22082872};
CC         IsoId=Q6KAU8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6KAU8-2; Sequence=VSP_033906, VSP_033907;
CC       Name=3; Synonyms=Atg16L2 alpha {ECO:0000303|PubMed:22082872};
CC         IsoId=Q6KAU8-3; Sequence=VSP_060643;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22082872}.
CC   -!- DISRUPTION PHENOTYPE: ATG16L2-deficient mice are viable and born at
CC       Mendelian proportions. Deficient mice exhibit intact canonical
CC       autophagy. {ECO:0000269|PubMed:31451676}.
CC   -!- MISCELLANEOUS: Although ATG16L2 is structurally similar to ATG16L1 and
CC       is likewise able to form a complex with the autophagy proteins ATG5 and
CC       ATG12, overexpression and knockdown studies suggest that ATG16L2 is not
CC       essential for canonical autophagy. {ECO:0000269|PubMed:22082872,
CC       ECO:0000269|PubMed:31451676}.
CC   -!- SIMILARITY: Belongs to the WD repeat ATG16 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD21359.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR   EMBL; AK131109; BAD21359.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AC107638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC060054; AAH60054.1; ALT_INIT; mRNA.
DR   EMBL; AB476648; BAL42360.1; -; mRNA.
DR   EMBL; AB476647; BAL42359.1; -; mRNA.
DR   CCDS; CCDS52329.1; -. [Q6KAU8-1]
DR   RefSeq; NP_001104581.1; NM_001111111.1. [Q6KAU8-1]
DR   AlphaFoldDB; Q6KAU8; -.
DR   SMR; Q6KAU8; -.
DR   BioGRID; 216189; 2.
DR   ComplexPortal; CPX-355; Atg12-Atg5-Atg16l2 complex.
DR   STRING; 10090.ENSMUSP00000112500; -.
DR   iPTMnet; Q6KAU8; -.
DR   PhosphoSitePlus; Q6KAU8; -.
DR   SwissPalm; Q6KAU8; -.
DR   EPD; Q6KAU8; -.
DR   jPOST; Q6KAU8; -.
DR   MaxQB; Q6KAU8; -.
DR   PaxDb; 10090-ENSMUSP00000112500; -.
DR   ProteomicsDB; 286033; -. [Q6KAU8-1]
DR   ProteomicsDB; 286034; -. [Q6KAU8-2]
DR   ProteomicsDB; 335064; -.
DR   Antibodypedia; 30896; 221 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000120267.9; ENSMUSP00000112500.2; ENSMUSG00000047767.18. [Q6KAU8-1]
DR   Ensembl; ENSMUST00000122116.8; ENSMUSP00000113320.2; ENSMUSG00000047767.18. [Q6KAU8-3]
DR   Ensembl; ENSMUST00000139609.8; ENSMUSP00000117387.2; ENSMUSG00000047767.18. [Q6KAU8-2]
DR   Ensembl; ENSMUST00000143630.8; ENSMUSP00000117029.2; ENSMUSG00000047767.18. [Q6KAU8-2]
DR   GeneID; 73683; -.
DR   KEGG; mmu:73683; -.
DR   UCSC; uc009iof.2; mouse. [Q6KAU8-1]
DR   UCSC; uc009iog.2; mouse.
DR   AGR; MGI:1920933; -.
DR   CTD; 89849; -.
DR   MGI; MGI:1920933; Atg16l2.
DR   VEuPathDB; HostDB:ENSMUSG00000047767; -.
DR   eggNOG; KOG0288; Eukaryota.
DR   GeneTree; ENSGT00940000153936; -.
DR   HOGENOM; CLU_000288_57_10_1; -.
DR   InParanoid; Q6KAU8; -.
DR   OMA; PHCAAIN; -.
DR   OrthoDB; 458014at2759; -.
DR   PhylomeDB; Q6KAU8; -.
DR   TreeFam; TF315541; -.
DR   BioGRID-ORCS; 73683; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Atg16l2; mouse.
DR   PRO; PR:Q6KAU8; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q6KAU8; Protein.
DR   Bgee; ENSMUSG00000047767; Expressed in granulocyte and 153 other cell types or tissues.
DR   ExpressionAtlas; Q6KAU8; baseline and differential.
DR   Genevisible; Q6KAU8; MM.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IDA:ComplexPortal.
DR   GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IDA:ComplexPortal.
DR   GO; GO:0000045; P:autophagosome assembly; IMP:ComplexPortal.
DR   GO; GO:0016236; P:macroautophagy; IMP:ComplexPortal.
DR   GO; GO:0039689; P:negative stranded viral RNA replication; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd22887; Atg16_CCD; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19878; AUTOPHAGY PROTEIN 16-LIKE; 1.
DR   PANTHER; PTHR19878:SF7; PROTEIN ATG16L2; 1.
DR   Pfam; PF08614; ATG16; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Protein transport;
KW   Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..623
FT                   /note="Protein Atg16l2"
FT                   /id="PRO_0000337111"
FT   REPEAT          338..377
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          382..421
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          424..458
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          459..502
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          504..543
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          550..589
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          593..623
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
FT   REGION          64..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          116..229
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        64..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         279..300
FT                   /note="RSASATSLTLSRCVDVVKGLLD -> S (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:22082872"
FT                   /id="VSP_060643"
FT   VAR_SEQ         396..403
FT                   /note="GSQVLAAT -> VRRLCPTA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033906"
FT   VAR_SEQ         404..623
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033907"
SQ   SEQUENCE   623 AA;  69241 MW;  0358F9B735BC44D6 CRC64;
     MAGPGAPCDP CAPAAVWKRH IVRQLRHRDR TQKALFLELV PAYNHLLEKA ELLAKFSEKL
     KSEPKDAIST RHEDWREEVS GTGPDQVSSP ASLRVKWQQE KKGLQLVCGE MAYQVVKKSA
     ALDTLQSQLE ERQDRLEALQ ACVVQLQEAR AQQSRQLEER QAENAAQREA YETLLQQAVH
     QEAALRRLQE EARDLLEQLV QRKARAAAER NLRNERRERA NQALVSQELK KAAKRTVSIS
     EIPNTLEDGT KEETVALAPA ALPEFSESET CEKWKRPFRS ASATSLTLSR CVDVVKGLLD
     FKKRRGHSVG GAPEQRYQSI PVCVSAQIPS QAQDVLDAHL SEVNAVCFGP NSSLLATGGA
     DRLIHLWNVV GGRLEANQTL EGAGGSITSV DFDPSGSQVL AATYNQAAQL WKVGETQSKE
     TLSGHKDKVT AAKFKLTRHQ AVTGSRDRTV KEWDLGRAYC SRTINVLSYC NDVVCGDHII
     ISGHNDQKIR FWDSRGPHCI QVIPVQGRVT SLHLSYDQLH LLSCSRDNTL KVIDLRISNI
     RQVFRADGFK CSSDWTKAVF SPDRSYALAG SSNGDLYIWD VNTGKLETSL QGPHCTAVNA
     VAWCFSGNHV VSVDQGRKVV LWH
//
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