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Autophagy-related protein 16-1 (APG16-like 1)

 A16L1_HUMAN             Reviewed;         607 AA.
Q676U5; A3EXK9; A3EXL0; B6ZDH0; Q6IPN1; Q6UXW4; Q6ZVZ5; Q8NCY2;
Q96JV5; Q9H619;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 2.
22-NOV-2017, entry version 146.
RecName: Full=Autophagy-related protein 16-1;
AltName: Full=APG16-like 1;
Name=ATG16L1; Synonyms=APG16L; ORFNames=UNQ9393/PRO34307;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-300.
TISSUE=Fetal brain;
PubMed=15620219; DOI=10.1080/10425170400004104;
Zheng H., Ji C., Li J., Jiang H., Ren M., Lu Q., Gu S., Mao Y.,
Xie Y.;
"Cloning and analysis of human Apg16L.";
DNA Seq. 15:303-305(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), INVOLVEMENT IN
SUSCEPTIBILITY TO IBD10, AND VARIANT IBD10 ALA-300.
PubMed=17200669; DOI=10.1038/ng1954;
Hampe J., Franke A., Rosenstiel P., Till A., Teuber M., Huse K.,
Albrecht M., Mayr G., De La Vega F.M., Briggs J., Guenther S.,
Prescott N.J., Onnie C.M., Haesler R., Sipos B., Foelsch U.R.,
Lengauer T., Platzer M., Mathew C.G., Krawczak M., Schreiber S.;
"A genome-wide association scan of nonsynonymous SNPs identifies a
susceptibility variant for Crohn disease in ATG16L1.";
Nat. Genet. 39:207-211(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 55-607 (ISOFORM 2).
TISSUE=Brain, Placenta, and Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-607 (ISOFORM 2).
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 513-607.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
FUNCTION.
PubMed=18849966; DOI=10.1038/nature07416;
Cadwell K., Liu J.Y., Brown S.L., Miyoshi H., Loh J., Lennerz J.K.,
Kishi C., Kc W., Carrero J.A., Hunt S., Stone C.D., Brunt E.M.,
Xavier R.J., Sleckman B.P., Li E., Mizushima N., Stappenbeck T.S.,
Virgin H.W. IV;
"A key role for autophagy and the autophagy gene Atg16l1 in mouse and
human intestinal Paneth cells.";
Nature 456:259-263(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
INTERACTION WITH CLTC, AND SUBCELLULAR LOCATION.
PubMed=20639872; DOI=10.1038/ncb2078;
Ravikumar B., Moreau K., Jahreiss L., Puri C., Rubinsztein D.C.;
"Plasma membrane contributes to the formation of pre-autophagosomal
structures.";
Nat. Cell Biol. 12:747-757(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-287, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
INTERACTION WITH RAB33B.
PubMed=21808068; DOI=10.1074/jbc.M111.261115;
Nottingham R.M., Ganley I.G., Barr F.A., Lambright D.G., Pfeffer S.R.;
"RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by
Rab32 and Rab33B proteins.";
J. Biol. Chem. 286:33213-33222(2011).
[14]
FUNCTION, AND INTERACTION WITH TMEM59; TLR2 AND NOD2.
PubMed=23376921; DOI=10.1038/emboj.2013.8;
Boada-Romero E., Letek M., Fleischer A., Pallauf K., Ramon-Barros C.,
Pimentel-Muinos F.X.;
"TMEM59 defines a novel ATG16L1-binding motif that promotes local
activation of LC3.";
EMBO J. 32:566-582(2013).
[15]
FUNCTION, INTERACTION WITH RB1CC1, AND SUBCELLULAR LOCATION.
PubMed=23392225; DOI=10.1038/embor.2013.6;
Nishimura T., Kaizuka T., Cadwell K., Sahani M.H., Saitoh T.,
Akira S., Virgin H.W., Mizushima N.;
"FIP200 regulates targeting of Atg16L1 to the isolation membrane.";
EMBO Rep. 14:284-291(2013).
[16]
FUNCTION.
PubMed=24238340; DOI=10.1016/j.immuni.2013.10.013;
Sorbara M.T., Ellison L.K., Ramjeet M., Travassos L.H., Jones N.L.,
Girardin S.E., Philpott D.J.;
"The protein ATG16L1 suppresses inflammatory cytokines induced by the
intracellular sensors Nod1 and Nod2 in an autophagy-independent
manner.";
Immunity 39:858-873(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
INTERACTION WITH RB1CC1.
PubMed=23262492; DOI=10.1038/nsmb.2475;
Gammoh N., Florey O., Overholtzer M., Jiang X.;
"Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-
dependent and -independent autophagy.";
Nat. Struct. Mol. Biol. 20:144-149(2013).
[19]
INTERACTION WITH ATG5-ATG12 COMPLEX AND PPP1CA, PHOSPHORYLATION AT
SER-139, AND MUTAGENESIS OF SER-139; VAL-540 AND PHE-542.
PubMed=26083323; DOI=10.1080/15548627.2015.1060386;
Song H., Pu J., Wang L., Wu L., Xiao J., Liu Q., Chen J., Zhang M.,
Liu Y., Ni M., Mo J., Zheng Y., Wan D., Cai X., Cao Y., Xiao W.,
Ye L., Tu E., Lin Z., Wen J., Lu X., He J., Peng Y., Su J., Zhang H.,
Zhao Y., Lin M., Zhang Z.;
"ATG16L1 phosphorylation is oppositely regulated by CSNK2/casein
kinase 2 and PPP1/protein phosphatase 1 which determines the fate of
cardiomyocytes during hypoxia/reoxygenation.";
Autophagy 11:1308-1325(2015).
[20]
INTERACTION WITH MEFV.
PubMed=26347139; DOI=10.1083/jcb.201503023;
Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
Deretic V.;
"TRIM-mediated precision autophagy targets cytoplasmic regulators of
innate immunity.";
J. Cell Biol. 210:973-989(2015).
[21]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 11-43 IN COMPLEX WITH ATG5
AND ATG12, AND INTERACTION WITH ATG5.
PubMed=23202584; DOI=10.1038/nsmb.2431;
Otomo C., Metlagel Z., Takaesu G., Otomo T.;
"Structure of the human ATG12-ATG5 conjugate required for LC3
lipidation in autophagy.";
Nat. Struct. Mol. Biol. 20:59-66(2013).
[22]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 11-43 IN COMPLEX WITH ATG5
AND ATG12, AND INTERACTION WITH ATG5.
PubMed=24191030; DOI=10.1073/pnas.1314755110;
Metlagel Z., Otomo C., Takaesu G., Otomo T.;
"Structural basis of ATG3 recognition by the autophagic ubiquitin-like
protein ATG12.";
Proc. Natl. Acad. Sci. U.S.A. 110:18844-18849(2013).
[23]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-69, SUBUNIT, INTERACTION
WITH ATG5, AND MUTAGENESIS OF ILE-17; LEU-21; ARG-24 AND ILE-36.
PubMed=25484072; DOI=10.4161/15548627.2014.984276;
Kim J.H., Hong S.B., Lee J.K., Han S., Roh K.H., Lee K.E., Kim Y.K.,
Choi E.J., Song H.K.;
"Insights into autophagosome maturation revealed by the structures of
ATG5 with its interacting partners.";
Autophagy 11:75-87(2015).
[24]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-69, AND INTERACTION WITH
ATG5.
PubMed=26812546; DOI=10.7554/eLife.12245;
Kim M., Sandford E., Gatica D., Qiu Y., Liu X., Zheng Y.,
Schulman B.A., Xu J., Semple I., Ro S.H., Kim B., Mavioglu R.N.,
Tolun A., Jipa A., Takats S., Karpati M., Li J.Z., Yapici Z.,
Juhasz G., Lee J.H., Klionsky D.J., Burmeister M.;
"Mutation in ATG5 reduces autophagy and leads to ataxia with
developmental delay.";
Elife 5:0-0(2016).
[25]
VARIANT IBD10 ALA-300.
PubMed=17484864; DOI=10.1053/j.gastro.2007.03.034;
Prescott N.J., Fisher S.A., Franke A., Hampe J., Onnie C.M., Soars D.,
Bagnall R., Mirza M.M., Sanderson J., Forbes A., Mansfield J.C.,
Lewis C.M., Schreiber S., Mathew C.G.;
"A nonsynonymous SNP in ATG16L1 predisposes to ileal Crohn's disease
and is independent of CARD15 and IBD5.";
Gastroenterology 132:1665-1671(2007).
[26]
INVOLVEMENT IN SUSCEPTIBILITY TO IBD10, AND VARIANT IBD10 ALA-300.
PubMed=17435756; DOI=10.1038/ng2032;
Rioux J.D., Xavier R.J., Taylor K.D., Silverberg M.S., Goyette P.,
Huett A., Green T., Kuballa P., Barmada M.M., Datta L.W.,
Shugart Y.Y., Griffiths A.M., Targan S.R., Ippoliti A.F.,
Bernard E.-J., Mei L., Nicolae D.L., Regueiro M., Schumm L.P.,
Steinhart A.H., Rotter J.I., Duerr R.H., Cho J.H., Daly M.J.,
Brant S.R.;
"Genome-wide association study identifies new susceptibility loci for
Crohn disease and implicates autophagy in disease pathogenesis.";
Nat. Genet. 39:596-604(2007).
[27]
VARIANT IBD10 ALA-300.
PubMed=18047540; DOI=10.1111/j.1572-0241.2007.01660.x;
Weersma R.K., Zhernakova A., Nolte I.M., Lefebvre C., Rioux J.D.,
Mulder F., van Dullemen H.M., Kleibeuker J.H., Wijmenga C.,
Dijkstra G.;
"ATG16L1 and IL23R are associated with inflammatory bowel diseases but
not with celiac disease in the Netherlands.";
Am. J. Gastroenterol. 103:621-627(2008).
[28]
VARIANT IBD10 ALA-300.
PubMed=18499543; DOI=10.1016/j.dld.2008.03.022;
Hungarian IBD Study Group;
Lakatos P.L., Szamosi T., Szilvasi A., Molnar E., Lakatos L.,
Kovacs A., Molnar T., Altorjay I., Papp M., Tulassay Z., Miheller P.,
Papp J., Tordai A., Andrikovics H.;
"ATG16L1 and IL23 receptor (IL23R) genes are associated with disease
susceptibility in Hungarian CD patients.";
Dig. Liver Dis. 40:867-873(2008).
[29]
VARIANT IBD10 ALA-300.
PubMed=19659808; DOI=10.1111/j.1651-2227.2009.01438.x;
Lacher M., Schroepf S., Ballauff A., Lohse P., von Schweinitz D.,
Kappler R., Koletzko S.;
"Autophagy 16-like 1 rs2241880 G allele is associated with Crohn's
disease in German children.";
Acta Paediatr. 98:1835-1840(2009).
[30]
VARIANT IBD10 ALA-300.
PubMed=18985712; DOI=10.1002/ibd.20785;
Amre D.K., Mack D.R., Morgan K., Krupoves A., Costea I., Lambrette P.,
Grimard G., Dong J., Feguery H., Bucionis V., Deslandres C., Levy E.,
Seidman E.G.;
"Autophagy gene ATG16L1 but not IRGM is associated with Crohn's
disease in Canadian children.";
Inflamm. Bowel Dis. 15:501-507(2009).
[31]
VARIANT IBD10 ALA-300.
PubMed=24656308; DOI=10.1016/j.dld.2014.02.016;
Strisciuglio C., Auricchio R., Martinelli M., Staiano A.,
Giugliano F.P., Andreozzi M., De Rosa M., Giannetti E., Gianfrani C.,
Izzo P., Troncone R., Miele E.;
"Autophagy genes variants and paediatric Crohn's disease phenotype: a
single-centre experience.";
Dig. Liver Dis. 46:512-517(2014).
[32]
FUNCTION IN AUTOPHAGY, CLEAVAGE BY CASP3, CHARACTERIZATION OF VARIANT
IBD10 ALA-300, AND MUTAGENESIS OF ASP-299.
PubMed=24553140; DOI=10.1038/nature13044;
Murthy A., Li Y., Peng I., Reichelt M., Katakam A.K., Noubade R.,
Roose-Girma M., Devoss J., Diehl L., Graham R.R.,
van Lookeren Campagne M.;
"A Crohn's disease variant in Atg16l1 enhances its degradation by
caspase 3.";
Nature 506:456-462(2014).
[33]
FUNCTION, INTERACTION WITH WIPI2 AND RB1CC1, DOMAIN, AND MUTAGENESIS
OF GLU-226 AND GLU-230.
PubMed=24954904; DOI=10.1016/j.molcel.2014.05.021;
Dooley H.C., Razi M., Polson H.E., Girardin S.E., Wilson M.I.,
Tooze S.A.;
"WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and
pathogen clearance by recruiting Atg12-5-16L1.";
Mol. Cell 55:238-252(2014).
[34]
CHARACTERIZATION OF VARIANT IBD10 ALA-300, AND FUNCTION.
PubMed=25645662; DOI=10.1136/gutjnl-2014-308735;
Grimm W.A., Messer J.S., Murphy S.F., Nero T., Lodolce J.P.,
Weber C.R., Logsdon M.F., Bartulis S., Sylvester B.E., Springer A.,
Dougherty U., Niewold T.B., Kupfer S.S., Ellis N., Huo D.,
Bissonnette M., Boone D.L.;
"The Thr300Ala variant in ATG16L1 is associated with improved survival
in human colorectal cancer and enhanced production of type I
interferon.";
Gut 65:456-464(2016).
[35]
CHARACTERIZATION OF VARIANT IBD10 ALA-300, FUNCTION, AND INTERACTION
WITH TMEM59.
PubMed=27273576; DOI=10.1038/ncomms11821;
Boada-Romero E., Serramito-Gomez I., Sacristan M.P., Boone D.L.,
Xavier R.J., Pimentel-Muinos F.X.;
"The T300A Crohn's disease risk polymorphism impairs function of the
WD40 domain of ATG16L1.";
Nat. Commun. 7:11821-11821(2016).
-!- FUNCTION: Plays an essential role in autophagy: interacts with
ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine
(PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a
membrane-bound activated form of LC3 named LC3-II. Thereby,
controls the elongation of the nascent autophagosomal membrane
(PubMed:24553140, PubMed:23376921, PubMed:24954904,
PubMed:27273576, PubMed:23392225). Regulates mitochondrial
antiviral signaling (MAVS)-dependent type I interferon (IFN-I)
production (PubMed:25645662). Negatively regulates NOD1- and NOD2-
driven inflammatory cytokine response (PubMed:24238340). Plays a
role in regulating morphology and function of Paneth cell
(PubMed:18849966). {ECO:0000269|PubMed:18849966,
ECO:0000269|PubMed:23376921, ECO:0000269|PubMed:23392225,
ECO:0000269|PubMed:24238340, ECO:0000269|PubMed:24553140,
ECO:0000269|PubMed:24954904, ECO:0000269|PubMed:25645662,
ECO:0000269|PubMed:27273576}.
-!- SUBUNIT: Homodimer (PubMed:25484072). Homooligomer (By
similarity). Interacts with WIPI2 (PubMed:24954904). Interacts
with RB1CC1; the interaction is required for ULK1 complex-
dependent autophagy (PubMed:23262492, PubMed:24954904,
PubMed:23392225). Interacts with ATG5 (PubMed:23202584,
PubMed:24191030, PubMed:25484072, PubMed:26812546). Part of either
the minor and major complexes respectively composed of 4 sets of
ATG12-ATG5 and ATG16L1 (400 kDa) or 8 sets of ATG12-ATG5 and
ATG16L1 (800 kDa) (PubMed:26083323, PubMed:23202584,
PubMed:24191030). Interacts with RAB33B (PubMed:21808068).
Interacts (via WD repeats) with TMEM59; the interaction mediates
unconventional autophagic activity of TMEM59 (PubMed:23376921,
PubMed:27273576). Interacts with TLR2 and NOD2 (PubMed:23376921).
Interacts (via WD repeats) with MEFV (PubMed:26347139). Interacts
with PPP1CA; the interaction dephosphorylates ATG16L1 causing
dissociation of ATG12-ATG5-ATG16L1 complex (PubMed:26083323).
Interacts (via N-terminal) with CLTC (PubMed:20639872).
{ECO:0000250|UniProtKB:Q8C0J2, ECO:0000269|PubMed:20639872,
ECO:0000269|PubMed:21808068, ECO:0000269|PubMed:23202584,
ECO:0000269|PubMed:23262492, ECO:0000269|PubMed:23376921,
ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:24191030,
ECO:0000269|PubMed:24954904, ECO:0000269|PubMed:25484072,
ECO:0000269|PubMed:26083323, ECO:0000269|PubMed:26347139,
ECO:0000269|PubMed:26812546, ECO:0000269|PubMed:27273576}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-535909, EBI-535909;
Q9H1Y0:ATG5; NbExp=7; IntAct=EBI-535909, EBI-1047414;
P60520:GABARAPL2; NbExp=2; IntAct=EBI-535909, EBI-720116;
Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-535909, EBI-373144;
Q9BXW4:MAP1LC3C; NbExp=4; IntAct=EBI-535909, EBI-2603996;
Q8TDY2:RB1CC1; NbExp=6; IntAct=EBI-535909, EBI-1047793;
Q9BXS4:TMEM59; NbExp=6; IntAct=EBI-535909, EBI-7054441;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23392225}.
Preautophagosomal structure membrane {ECO:0000269|PubMed:20639872,
ECO:0000269|PubMed:23392225}; Peripheral membrane protein
{ECO:0000250}. Note=Recruited to omegasomes membranes by WIPI2.
Omegasomes are endoplasmic reticulum connected strutures at the
origin of preautophagosomal structures. Localized to
preautophagosomal structure (PAS) where it is involved in the
membrane targeting of ATG5. Localizes also to discrete punctae
along the ciliary axoneme. {ECO:0000250|UniProtKB:Q8C0J2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=APG16L beta;
IsoId=Q676U5-1; Sequence=Displayed;
Name=2;
IsoId=Q676U5-2; Sequence=VSP_013386;
Name=3;
IsoId=Q676U5-3; Sequence=VSP_013387, VSP_013388;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=Q676U5-4; Sequence=VSP_013389, VSP_013390;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q676U5-5; Sequence=VSP_013389, VSP_013386;
Note=No experimental confirmation available.;
-!- PTM: Proteolytic cleavage by activated CASP3 leads to degradation
and may regulate autophagy upon cellular stress and apoptotic
stimuli. {ECO:0000269|PubMed:24553140}.
-!- PTM: Phosphorylation at Ser-139 promotes association with the
ATG12-ATG5 conjugate to form the ATG12-ATG5-ATG16L1 complex.
{ECO:0000269|PubMed:26083323}.
-!- DISEASE: Inflammatory bowel disease 10 (IBD10) [MIM:611081]: A
chronic, relapsing inflammation of the gastrointestinal tract with
a complex etiology. It is subdivided into Crohn disease and
ulcerative colitis phenotypes. Crohn disease may affect any part
of the gastrointestinal tract from the mouth to the anus, but most
frequently it involves the terminal ileum and colon. Bowel
inflammation is transmural and discontinuous; it may contain
granulomas or be associated with intestinal or perianal fistulas.
In contrast, in ulcerative colitis, the inflammation is continuous
and limited to rectal and colonic mucosal layers; fistulas and
granulomas are not observed. Both diseases include extraintestinal
inflammation of the skin, eyes, or joints.
{ECO:0000269|PubMed:17200669, ECO:0000269|PubMed:17435756,
ECO:0000269|PubMed:17484864, ECO:0000269|PubMed:18047540,
ECO:0000269|PubMed:18499543, ECO:0000269|PubMed:18985712,
ECO:0000269|PubMed:19659808, ECO:0000269|PubMed:24553140,
ECO:0000269|PubMed:24656308, ECO:0000269|PubMed:25645662,
ECO:0000269|PubMed:27273576}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the WD repeat ATG16 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15448.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
Sequence=BAB55412.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY398617; AAR32130.1; -; mRNA.
EMBL; EF079889; ABN48554.1; -; mRNA.
EMBL; EF079890; ABN48555.1; -; mRNA.
EMBL; AY358182; AAQ88549.1; -; mRNA.
EMBL; AK026330; BAB15448.1; ALT_SEQ; mRNA.
EMBL; AK027854; BAB55412.1; ALT_INIT; mRNA.
EMBL; AK123876; BAC85713.1; -; mRNA.
EMBL; AC013726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471063; EAW71034.1; -; Genomic_DNA.
EMBL; BC071846; AAH71846.1; -; mRNA.
EMBL; AL834526; CAD39182.1; -; mRNA.
CCDS; CCDS2502.2; -. [Q676U5-2]
CCDS; CCDS2503.2; -. [Q676U5-1]
CCDS; CCDS54438.1; -. [Q676U5-5]
RefSeq; NP_001177195.1; NM_001190266.1.
RefSeq; NP_001177196.1; NM_001190267.1.
RefSeq; NP_060444.3; NM_017974.3. [Q676U5-2]
RefSeq; NP_110430.5; NM_030803.6. [Q676U5-1]
RefSeq; NP_942593.2; NM_198890.2. [Q676U5-5]
UniGene; Hs.529322; -.
PDB; 4GDK; X-ray; 2.70 A; C/F=11-43.
PDB; 4GDL; X-ray; 2.88 A; C=11-43.
PDB; 4NAW; X-ray; 2.20 A; C/G/K/O=11-43.
PDB; 4TQ0; X-ray; 2.70 A; B/D/F=1-69.
PDB; 5D7G; X-ray; 3.00 A; B/D/F/H=1-69.
PDB; 5NPV; X-ray; 3.10 A; B/D=11-307.
PDB; 5NPW; X-ray; 3.10 A; B/D/F/H=11-307.
PDB; 5NUV; X-ray; 1.55 A; A=303-607.
PDBsum; 4GDK; -.
PDBsum; 4GDL; -.
PDBsum; 4NAW; -.
PDBsum; 4TQ0; -.
PDBsum; 5D7G; -.
PDBsum; 5NPV; -.
PDBsum; 5NPW; -.
PDBsum; 5NUV; -.
ProteinModelPortal; Q676U5; -.
SMR; Q676U5; -.
BioGrid; 120375; 51.
CORUM; Q676U5; -.
DIP; DIP-27552N; -.
DIP; DIP-50290N; -.
IntAct; Q676U5; 37.
MINT; MINT-1141152; -.
STRING; 9606.ENSP00000375872; -.
iPTMnet; Q676U5; -.
PhosphoSitePlus; Q676U5; -.
SwissPalm; Q676U5; -.
BioMuta; ATG16L1; -.
DMDM; 62510482; -.
EPD; Q676U5; -.
MaxQB; Q676U5; -.
PaxDb; Q676U5; -.
PeptideAtlas; Q676U5; -.
PRIDE; Q676U5; -.
DNASU; 55054; -.
Ensembl; ENST00000347464; ENSP00000318259; ENSG00000085978. [Q676U5-5]
Ensembl; ENST00000373525; ENSP00000362625; ENSG00000085978. [Q676U5-4]
Ensembl; ENST00000392017; ENSP00000375872; ENSG00000085978. [Q676U5-1]
Ensembl; ENST00000392020; ENSP00000375875; ENSG00000085978. [Q676U5-2]
Ensembl; ENST00000625501; ENSP00000487542; ENSG00000281089. [Q676U5-1]
Ensembl; ENST00000626623; ENSP00000487298; ENSG00000281089. [Q676U5-5]
Ensembl; ENST00000630066; ENSP00000487446; ENSG00000281089. [Q676U5-2]
Ensembl; ENST00000630204; ENSP00000487455; ENSG00000281089. [Q676U5-4]
GeneID; 55054; -.
KEGG; hsa:55054; -.
UCSC; uc002vtx.3; human. [Q676U5-1]
CTD; 55054; -.
DisGeNET; 55054; -.
EuPathDB; HostDB:ENSG00000085978.21; -.
GeneCards; ATG16L1; -.
HGNC; HGNC:21498; ATG16L1.
HPA; HPA012577; -.
HPA; HPA063900; -.
MalaCards; ATG16L1; -.
MIM; 610767; gene.
MIM; 611081; phenotype.
neXtProt; NX_Q676U5; -.
OpenTargets; ENSG00000085978; -.
Orphanet; 206; Crohn disease.
PharmGKB; PA134902949; -.
eggNOG; KOG0288; Eukaryota.
eggNOG; ENOG410XQYA; LUCA.
GeneTree; ENSGT00810000125363; -.
HOGENOM; HOG000112569; -.
HOVERGEN; HBG050534; -.
InParanoid; Q676U5; -.
KO; K17890; -.
PhylomeDB; Q676U5; -.
TreeFam; TF315541; -.
Reactome; R-HSA-1632852; Macroautophagy.
SignaLink; Q676U5; -.
SIGNOR; Q676U5; -.
GeneWiki; ATG16L1; -.
GenomeRNAi; 55054; -.
PRO; PR:Q676U5; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000085978; -.
CleanEx; HS_ATG16L1; -.
ExpressionAtlas; Q676U5; baseline and differential.
Genevisible; Q676U5; HS.
GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
GO; GO:0005930; C:axoneme; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0034045; C:pre-autophagosomal structure membrane; IEA:UniProtKB-SubCell.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019787; F:ubiquitin-like protein transferase activity; TAS:Reactome.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0039689; P:negative stranded viral RNA replication; IBA:GO_Central.
GO; GO:0051260; P:protein homooligomerization; NAS:UniProtKB.
GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; IEA:Ensembl.
GO; GO:0034497; P:protein localization to pre-autophagosomal structure; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0098792; P:xenophagy; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR013923; Autophagy-rel_prot_16.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF08614; ATG16; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Autophagy; Coiled coil;
Complete proteome; Cytoplasm; Membrane; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Repeat; Transport; WD repeat.
CHAIN 1 607 Autophagy-related protein 16-1.
/FTId=PRO_0000050848.
REPEAT 320 359 WD 1. {ECO:0000255|PROSITE-
ProRule:PRU00221}.
REPEAT 364 403 WD 2. {ECO:0000255|PROSITE-
ProRule:PRU00221}.
REPEAT 406 445 WD 3. {ECO:0000255|PROSITE-
ProRule:PRU00221}.
REPEAT 447 484 WD 4. {ECO:0000255|PROSITE-
ProRule:PRU00221}.
REPEAT 486 525 WD 5. {ECO:0000255|PROSITE-
ProRule:PRU00221}.
REPEAT 532 573 WD 6. {ECO:0000255|PROSITE-
ProRule:PRU00221}.
REPEAT 575 607 WD 7. {ECO:0000255|PROSITE-
ProRule:PRU00221}.
REGION 13 43 Interaction with ATG5.
{ECO:0000269|PubMed:25484072}.
REGION 207 230 WIPI2-binding.
{ECO:0000269|PubMed:24954904}.
REGION 230 242 RB1CC1-binding.
{ECO:0000269|PubMed:23392225,
ECO:0000269|PubMed:24954904}.
COILED 78 230 {ECO:0000255}.
MOTIF 296 299 Caspase cleavage.
MOD_RES 139 139 Phosphoserine; by CK2.
{ECO:0000269|PubMed:26083323}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 70 213 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17200669}.
/FTId=VSP_013389.
VAR_SEQ 266 284 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17200669}.
/FTId=VSP_013386.
VAR_SEQ 334 368 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_013390.
VAR_SEQ 443 470 IKTVFAGSSCNDIVCTEQCVMSGHFDKK -> EEIQSLCLC
ICLDVSVEVCVCTSEPAFM (in isoform 3).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_013387.
VAR_SEQ 471 607 Missing (in isoform 3).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_013388.
VARIANT 300 300 T -> A (in IBD10; has no effect on the
stability of the protein under normal
conditions; enhances the cleavage and the
degradation mediated by activated CASP3;
results in reduced autophagy and
defective clearance of intestinal
pathogens; impairs interaction with
TMEM59; slows TMEM59 intracellular
trafficking; increases production of type
I IFNs; dbSNP:rs2241880).
{ECO:0000269|PubMed:15620219,
ECO:0000269|PubMed:17200669,
ECO:0000269|PubMed:17484864,
ECO:0000269|PubMed:18047540,
ECO:0000269|PubMed:18499543,
ECO:0000269|PubMed:18985712,
ECO:0000269|PubMed:19659808,
ECO:0000269|PubMed:24553140,
ECO:0000269|PubMed:24656308,
ECO:0000269|PubMed:25645662,
ECO:0000269|PubMed:27273576}.
/FTId=VAR_021834.
VARIANT 307 307 E -> K (in dbSNP:rs1866878).
/FTId=VAR_053386.
MUTAGEN 17 17 I->W: Abolishes interaction with ATG5.
{ECO:0000269|PubMed:25484072}.
MUTAGEN 21 21 L->W: Abolishes interaction with ATG5.
{ECO:0000269|PubMed:25484072}.
MUTAGEN 24 24 R->D: Abolishes interaction with ATG5.
{ECO:0000269|PubMed:25484072}.
MUTAGEN 36 36 I->W: Reduces interaction with ATG5.
{ECO:0000269|PubMed:25484072}.
MUTAGEN 139 139 S->A: Abolishes phosphorylation. Impairs
interaction with ATG12-ATG5 complex.
{ECO:0000269|PubMed:26083323}.
MUTAGEN 226 226 E->R: Impairs interaction with WIPI2.
{ECO:0000269|PubMed:24954904}.
MUTAGEN 230 230 E->R: Impairs interaction with WIPI2.
{ECO:0000269|PubMed:24954904}.
MUTAGEN 299 299 D->E: Prevents cleavage by activated
CASP3. {ECO:0000269|PubMed:24553140}.
MUTAGEN 540 540 V->A: Impairs interaction with PPP1CA;
when associated with A-542.
{ECO:0000269|PubMed:26083323}.
MUTAGEN 542 542 F->A: Impairs interaction with PPP1CA;
when associated with A-540.
{ECO:0000269|PubMed:26083323}.
CONFLICT 151 151 K -> R (in Ref. 6; BAB55412).
{ECO:0000305}.
CONFLICT 328 328 V -> A (in Ref. 6; BAB55412).
{ECO:0000305}.
CONFLICT 529 529 P -> T (in Ref. 6; BAB55412).
{ECO:0000305}.
HELIX 12 28 {ECO:0000244|PDB:4NAW}.
HELIX 30 42 {ECO:0000244|PDB:4NAW}.
STRAND 313 319 {ECO:0000244|PDB:5NUV}.
STRAND 321 323 {ECO:0000244|PDB:5NUV}.
STRAND 325 330 {ECO:0000244|PDB:5NUV}.
STRAND 334 341 {ECO:0000244|PDB:5NUV}.
STRAND 346 351 {ECO:0000244|PDB:5NUV}.
STRAND 356 362 {ECO:0000244|PDB:5NUV}.
STRAND 369 374 {ECO:0000244|PDB:5NUV}.
STRAND 378 385 {ECO:0000244|PDB:5NUV}.
STRAND 390 394 {ECO:0000244|PDB:5NUV}.
TURN 395 398 {ECO:0000244|PDB:5NUV}.
STRAND 399 404 {ECO:0000244|PDB:5NUV}.
STRAND 411 416 {ECO:0000244|PDB:5NUV}.
STRAND 422 427 {ECO:0000244|PDB:5NUV}.
STRAND 430 436 {ECO:0000244|PDB:5NUV}.
TURN 437 440 {ECO:0000244|PDB:5NUV}.
STRAND 441 447 {ECO:0000244|PDB:5NUV}.
STRAND 452 457 {ECO:0000244|PDB:5NUV}.
STRAND 459 466 {ECO:0000244|PDB:5NUV}.
STRAND 469 475 {ECO:0000244|PDB:5NUV}.
TURN 476 479 {ECO:0000244|PDB:5NUV}.
STRAND 480 486 {ECO:0000244|PDB:5NUV}.
STRAND 491 496 {ECO:0000244|PDB:5NUV}.
STRAND 502 507 {ECO:0000244|PDB:5NUV}.
TURN 508 510 {ECO:0000244|PDB:5NUV}.
STRAND 511 516 {ECO:0000244|PDB:5NUV}.
TURN 517 520 {ECO:0000244|PDB:5NUV}.
STRAND 521 526 {ECO:0000244|PDB:5NUV}.
STRAND 540 542 {ECO:0000244|PDB:5NUV}.
STRAND 546 552 {ECO:0000244|PDB:5NUV}.
STRAND 558 562 {ECO:0000244|PDB:5NUV}.
TURN 563 565 {ECO:0000244|PDB:5NUV}.
STRAND 568 572 {ECO:0000244|PDB:5NUV}.
STRAND 580 585 {ECO:0000244|PDB:5NUV}.
STRAND 592 596 {ECO:0000244|PDB:5NUV}.
STRAND 599 605 {ECO:0000244|PDB:5NUV}.
SEQUENCE 607 AA; 68265 MW; 5A5816AE2CF03CA0 CRC64;
MSSGLRAADF PRWKRHISEQ LRRRDRLQRQ AFEEIILQYN KLLEKSDLHS VLAQKLQAEK
HDVPNRHEIS PGHDGTWNDN QLQEMAQLRI KHQEELTELH KKRGELAQLV IDLNNQMQRK
DREMQMNEAK IAECLQTISD LETECLDLRT KLCDLERANQ TLKDEYDALQ ITFTALEGKL
RKTTEENQEL VTRWMAEKAQ EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI
EVIVDETSDH TEETSPVRAI SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS FPVPQDNVDT
HPGSGKEVRV PATALCVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE VFGEKCEFKG
SLSGSNAGIT SIEFDSAGSY LLAASNDFAS RIWTVDDYRL RHTLTGHSGK VLSAKFLLDN
ARIVSGSHDR TLKLWDLRSK VCIKTVFAGS SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES
IVREMELLGK ITALDLNPER TELLSCSRDD LLKVIDLRTN AIKQTFSAPG FKCGSDWTRV
VFSPDGSYVA AGSAEGSLYI WSVLTGKVEK VLSKQHSSSI NAVAWSPSGS HVVSVDKGCK
AVLWAQY


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