A16L2_HUMAN
ID A16L2_HUMAN Reviewed; 619 AA.
AC Q8NAA4; A5PL30; B2RPK5; Q658V4; Q6PID3; Q8NBG0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein Atg16l2 {ECO:0000305};
DE AltName: Full=APG16-like 2;
DE AltName: Full=Autophagy-related protein 16-2;
DE AltName: Full=WD repeat-containing protein 80;
GN Name=ATG16L2; Synonyms=WDR80;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Astrocyte, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Eye;
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 [LARGE SCALE MRNA] OF 297-619.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play a role in regulating epithelial homeostasis in an
CC ATG16L1-dependent manner. {ECO:0000250|UniProtKB:Q6KAU8}.
CC -!- SUBUNIT: Homooligomer. Heterooligomer with ATG16L1. Interacts with
CC ATG5. Self-oligomerizes to form a 800-kDa complex composed of ATG12-
CC ATG5 and ATG16L2. Interacts with RAB33B.
CC {ECO:0000250|UniProtKB:Q6KAU8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6KAU8}. Note=Localizes also to discrete punctae
CC along the ciliary axoneme. {ECO:0000250|UniProtKB:Q6KAU8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NAA4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NAA4-2; Sequence=VSP_033904;
CC Name=3;
CC IsoId=Q8NAA4-3; Sequence=VSP_033905;
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 in mouse suggest that
CC ATG16L2 is not essential for canonical autophagy.
CC {ECO:0000250|UniProtKB:Q6KAU8}.
CC -!- SIMILARITY: Belongs to the WD repeat ATG16 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; AK093017; BAC04021.1; -; mRNA.
DR EMBL; AK090597; BAC03485.1; -; mRNA.
DR EMBL; CH471076; EAW74876.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW74874.1; -; Genomic_DNA.
DR EMBL; BC036713; AAH36713.1; -; mRNA.
DR EMBL; BC137489; AAI37490.1; -; mRNA.
DR EMBL; BC137490; AAI37491.1; -; mRNA.
DR EMBL; BC142718; AAI42719.1; -; mRNA.
DR EMBL; BC146660; AAI46661.1; -; mRNA.
DR EMBL; AL832974; CAH56355.1; -; mRNA.
DR CCDS; CCDS31634.1; -. [Q8NAA4-1]
DR RefSeq; NP_001305695.1; NM_001318766.1. [Q8NAA4-2]
DR RefSeq; NP_203746.1; NM_033388.1. [Q8NAA4-1]
DR RefSeq; XP_011543635.1; XM_011545333.1. [Q8NAA4-2]
DR RefSeq; XP_011543636.1; XM_011545334.1. [Q8NAA4-2]
DR AlphaFoldDB; Q8NAA4; -.
DR SMR; Q8NAA4; -.
DR BioGRID; 124620; 41.
DR ComplexPortal; CPX-354; ATG12-ATG5-ATG16L2 complex.
DR IntAct; Q8NAA4; 6.
DR MINT; Q8NAA4; -.
DR STRING; 9606.ENSP00000326340; -.
DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; Q8NAA4; -.
DR PhosphoSitePlus; Q8NAA4; -.
DR BioMuta; ATG16L2; -.
DR DMDM; 189027648; -.
DR EPD; Q8NAA4; -.
DR jPOST; Q8NAA4; -.
DR MassIVE; Q8NAA4; -.
DR MaxQB; Q8NAA4; -.
DR PaxDb; Q8NAA4; -.
DR PeptideAtlas; Q8NAA4; -.
DR PRIDE; Q8NAA4; -.
DR ProteomicsDB; 72661; -. [Q8NAA4-1]
DR ProteomicsDB; 72662; -. [Q8NAA4-2]
DR ProteomicsDB; 72663; -. [Q8NAA4-3]
DR Antibodypedia; 30896; 198 antibodies from 26 providers.
DR DNASU; 89849; -.
DR Ensembl; ENST00000321297.10; ENSP00000326340.5; ENSG00000168010.11. [Q8NAA4-1]
DR GeneID; 89849; -.
DR KEGG; hsa:89849; -.
DR MANE-Select; ENST00000321297.10; ENSP00000326340.5; NM_033388.2; NP_203746.1.
DR UCSC; uc001otd.4; human. [Q8NAA4-1]
DR CTD; 89849; -.
DR DisGeNET; 89849; -.
DR GeneCards; ATG16L2; -.
DR HGNC; HGNC:25464; ATG16L2.
DR HPA; ENSG00000168010; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 618716; gene.
DR neXtProt; NX_Q8NAA4; -.
DR OpenTargets; ENSG00000168010; -.
DR PharmGKB; PA142672575; -.
DR VEuPathDB; HostDB:ENSG00000168010; -.
DR eggNOG; KOG0288; Eukaryota.
DR GeneTree; ENSGT00940000153936; -.
DR InParanoid; Q8NAA4; -.
DR OMA; PHCAAIN; -.
DR PhylomeDB; Q8NAA4; -.
DR TreeFam; TF315541; -.
DR PathwayCommons; Q8NAA4; -.
DR SignaLink; Q8NAA4; -.
DR BioGRID-ORCS; 89849; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; ATG16L2; human.
DR GenomeRNAi; 89849; -.
DR Pharos; Q8NAA4; Tbio.
DR PRO; PR:Q8NAA4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NAA4; protein.
DR Bgee; ENSG00000168010; Expressed in granulocyte and 143 other tissues.
DR ExpressionAtlas; Q8NAA4; baseline and differential.
DR Genevisible; Q8NAA4; HS.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IPI:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:Ensembl.
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:0006497; P:protein lipidation; IDA:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 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; 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; 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..619
FT /note="Protein Atg16l2"
FT /id="PRO_0000337110"
FT REPEAT 334..373
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 378..417
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 420..454
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 455..498
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 500..539
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 546..585
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 589..619
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 57..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..227
FT /evidence="ECO:0000255"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033904"
FT VAR_SEQ 276..619
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033905"
FT VARIANT 220
FT /note="R -> W (in dbSNP:rs11235604)"
FT /id="VAR_043605"
FT CONFLICT 124
FT /note="E -> G (in Ref. 1; BAC03485)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="A -> V (in Ref. 3; AAH36713)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="R -> G (in Ref. 1; BAC03485)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="G -> E (in Ref. 1; BAC04021)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="L -> R (in Ref. 4; CAH56355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 68998 MW; 7F2962AA3C6BB850 CRC64;
MAGPGVPGAP AARWKRHIVR QLRLRDRTQK ALFLELVPAY NHLLEKAELL DKFSKKLQPE
PNSVTPTTHQ GPWEESELDS DQVPSLVALR VKWQEEEEGL RLVCGEMAYQ VVEKGAALGT
LESELQQRQS RLAALEARVA QLREARAQQA QQVEEWRAQN AVQRAAYEAL RAHVGLREAA
LRRLQEEARD LLERLVQRKA RAAAERNLRN ERRERAKQAR VSQELKKAAK RTVSISEGPD
TLGDGMRERR ETLALAPEPE PLEKEACEKW KRPFRSASAT SLTLSHCVDV VKGLLDFKKR
RGHSIGGAPE QRYQIIPVCV AARLPTRAQD VLDAHLSEVN AVRFGPNSSL LATGGADRLI
HLWNVVGSRL EANQTLEGAG GSITSVDFDP SGYQVLAATY NQAAQLWKVG EAQSKETLSG
HKDKVTAAKF KLTRHQAVTG SRDRTVKEWD LGRAYCSRTI NVLSYCNDVV CGDHIIISGH
NDQKIRFWDS RGPHCTQVIP VQGRVTSLSL SHDQLHLLSC SRDNTLKVID LRVSNIRQVF
RADGFKCGSD WTKAVFSPDR SYALAGSCDG ALYIWDVDTG KLESRLQGPH CAAVNAVAWC
YSGSHMVSVD QGRKVVLWQ
