Full text data of ATG9A
ATG9A
(APG9L1)
[Confidence: low (only semi-automatic identification from reviews)]
Autophagy-related protein 9A (APG9-like 1; mATG9)
Autophagy-related protein 9A (APG9-like 1; mATG9)
UniProt
Q7Z3C6
ID ATG9A_HUMAN Reviewed; 839 AA.
AC Q7Z3C6; Q3ZAQ6; Q6P0N7; Q7Z317; Q7Z320; Q8NDK6; Q8WU65; Q9BVL5;
read moreAC Q9H6L1; Q9HAG7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=Autophagy-related protein 9A;
DE AltName: Full=APG9-like 1;
DE AltName: Full=mATG9;
GN Name=ATG9A; Synonyms=APG9L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-592.
RC TISSUE=Fetal brain, Lung endothelial cell, Rectum tumor, and Testis;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain, and Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-839, AND VARIANT
RP GLY-592.
RC TISSUE=Embryo;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP IDENTIFICATION.
RX PubMed=15755735; DOI=10.1074/jbc.M413957200;
RA Yamada T., Carson A.R., Caniggia I., Umebayashi K., Yoshimori T.,
RA Nakabayashi K., Scherer S.W.;
RT "Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an
RT autophagy-related protein (APG9-like2) highly expressed in
RT trophoblast.";
RL J. Biol. Chem. 280:18283-18290(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION AT ASN-99.
RX PubMed=16940348; DOI=10.1242/jcs.03172;
RA Young A.R., Chan E.Y., Hu X.W., Kochl R., Crawshaw S.G., High S.,
RA Hailey D.W., Lippincott-Schwartz J., Tooze S.A.;
RT "Starvation and ULK1-dependent cycling of mammalian Atg9 between the
RT TGN and endosomes.";
RL J. Cell Sci. 119:3888-3900(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-656, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=18936157; DOI=10.1128/MCB.01082-08;
RA Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.;
RT "Kinase-inactivated ULK proteins inhibit autophagy via their conserved
RT C-terminal domains using an Atg13-independent mechanism.";
RL Mol. Cell. Biol. 29:157-171(2009).
RN [11]
RP INTERACTION WITH SUPT20H.
RX PubMed=19893488; DOI=10.1038/emboj.2009.321;
RA Webber J.L., Tooze S.A.;
RT "Coordinated regulation of autophagy by p38alpha MAPK through mAtg9
RT and p38IP.";
RL EMBO J. 29:27-40(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=19910472; DOI=10.1074/jbc.M109.054197;
RA Gao W., Kang J.H., Liao Y., Ding W.X., Gambotto A.A., Watkins S.C.,
RA Liu Y.J., Stolz D.B., Yin X.M.;
RT "Biochemical isolation and characterization of the tubulovesicular
RT LC3-positive autophagosomal compartment.";
RL J. Biol. Chem. 285:1371-1383(2010).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=20124090; DOI=10.1369/jhc.2010.955690;
RA Tamura H., Shibata M., Koike M., Sasaki M., Uchiyama Y.;
RT "Atg9A protein, an autophagy-related membrane protein, is localized in
RT the neurons of mouse brains.";
RL J. Histochem. Cytochem. 58:443-453(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=21068542; DOI=10.4161/auto.7.1.14015;
RA Takahashi Y., Meyerkord C.L., Hori T., Runkle K., Fox T.E., Kester M.,
RA Loughran T.P., Wang H.G.;
RT "Bif-1 regulates Atg9 trafficking by mediating the fission of Golgi
RT membranes during autophagy.";
RL Autophagy 7:61-73(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735; SER-738 AND
RP SER-741, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in autophagy and cytoplasm to vacuole transport
CC (Cvt) vesicle formation. Plays a key role in the organization of
CC the preautophagosomal structure/phagophore assembly site (PAS),
CC the nucleating site for formation of the sequestering vesicle.
CC Cycles between a juxta-nuclear trans-Golgi network compartment and
CC late endosomes. Nutrient starvation induces accumulation on
CC autophagosomes. Starvation-dependent trafficking requires ULK1,
CC ATG13 and SUPT20H.
CC -!- SUBUNIT: Interacts with SUPT20H.
CC -!- INTERACTION:
CC Q8NEM7-2:-; NbExp=8; IntAct=EBI-727146, EBI-7568679;
CC Q9UHD2:TBK1; NbExp=2; IntAct=EBI-727146, EBI-356402;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane;
CC Multi-pass membrane protein. Golgi apparatus, trans-Golgi network
CC membrane; Multi-pass membrane protein. Late endosome membrane;
CC Multi-pass membrane protein. Endoplasmic reticulum membrane;
CC Multi-pass membrane protein. Note=Under amino acid starvation or
CC rapamycin treatment, redistributes from a juxtanuclear clustered
CC pool to a dispersed peripheral cytosolic pool. The starvation-
CC induced redistribution depends on ULK1, ATG13, as well as SH3GLB1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z3C6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3C6-2; Sequence=VSP_013396;
CC Name=3;
CC IsoId=Q7Z3C6-3; Sequence=VSP_013397, VSP_013398;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC -!- SIMILARITY: Belongs to the ATG9 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13882.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB15246.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55119.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AL833865; CAD38723.1; -; mRNA.
DR EMBL; BX537984; CAD97944.1; -; mRNA.
DR EMBL; BX538192; CAD98061.1; -; mRNA.
DR EMBL; BX538198; CAD98064.1; -; mRNA.
DR EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW70706.1; -; Genomic_DNA.
DR EMBL; BC001098; AAH01098.2; -; mRNA.
DR EMBL; BC021202; AAH21202.2; -; mRNA.
DR EMBL; BC065534; AAH65534.1; -; mRNA.
DR EMBL; AK021732; BAB13882.1; ALT_INIT; mRNA.
DR EMBL; AK027448; BAB55119.1; ALT_INIT; mRNA.
DR EMBL; AK025822; BAB15246.1; ALT_INIT; mRNA.
DR EMBL; BK004018; DAA05199.1; -; mRNA.
DR RefSeq; NP_001070666.1; NM_001077198.2.
DR RefSeq; NP_076990.4; NM_024085.4.
DR RefSeq; XP_005246898.1; XM_005246841.1.
DR RefSeq; XP_005246899.1; XM_005246842.1.
DR RefSeq; XP_005246900.1; XM_005246843.1.
DR RefSeq; XP_005246901.1; XM_005246844.1.
DR RefSeq; XP_005246902.1; XM_005246845.1.
DR RefSeq; XP_005246903.1; XM_005246846.1.
DR RefSeq; XP_005246904.1; XM_005246847.1.
DR UniGene; Hs.323363; -.
DR ProteinModelPortal; Q7Z3C6; -.
DR IntAct; Q7Z3C6; 12.
DR MINT; MINT-1422125; -.
DR PhosphoSite; Q7Z3C6; -.
DR DMDM; 296439428; -.
DR PaxDb; Q7Z3C6; -.
DR PRIDE; Q7Z3C6; -.
DR DNASU; 79065; -.
DR Ensembl; ENST00000361242; ENSP00000355173; ENSG00000198925.
DR Ensembl; ENST00000396761; ENSP00000379983; ENSG00000198925.
DR Ensembl; ENST00000409033; ENSP00000386482; ENSG00000198925.
DR Ensembl; ENST00000409422; ENSP00000386535; ENSG00000198925.
DR Ensembl; ENST00000409618; ENSP00000386710; ENSG00000198925.
DR GeneID; 79065; -.
DR KEGG; hsa:79065; -.
DR UCSC; uc002vke.1; human.
DR CTD; 79065; -.
DR GeneCards; GC02M220074; -.
DR H-InvDB; HIX0002853; -.
DR H-InvDB; HIX0077803; -.
DR HGNC; HGNC:22408; ATG9A.
DR MIM; 612204; gene.
DR neXtProt; NX_Q7Z3C6; -.
DR PharmGKB; PA134931318; -.
DR eggNOG; NOG298729; -.
DR HOVERGEN; HBG050539; -.
DR InParanoid; Q7Z3C6; -.
DR OMA; EVVFFTR; -.
DR OrthoDB; EOG72C4ZM; -.
DR GeneWiki; ATG9A; -.
DR GenomeRNAi; 79065; -.
DR NextBio; 67835; -.
DR PRO; PR:Q7Z3C6; -.
DR ArrayExpress; Q7Z3C6; -.
DR Bgee; Q7Z3C6; -.
DR CleanEx; HS_ATG9A; -.
DR Genevestigator; Q7Z3C6; -.
DR GO; GO:0000421; C:autophagic vacuole membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagic vacuole assembly; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 1.
DR Pfam; PF04109; APG9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Autophagy; Complete proteome;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 839 Autophagy-related protein 9A.
FT /FTId=PRO_0000119820.
FT TOPO_DOM 2 66 Cytoplasmic (By similarity).
FT TRANSMEM 67 87 Helical; (Potential).
FT TOPO_DOM 88 131 Lumenal (By similarity).
FT TRANSMEM 132 152 Helical; (Potential).
FT TOPO_DOM 153 289 Cytoplasmic (By similarity).
FT TRANSMEM 290 310 Helical; (Potential).
FT TOPO_DOM 311 371 Lumenal (By similarity).
FT TRANSMEM 372 392 Helical; (Potential).
FT TOPO_DOM 393 400 Cytoplasmic (By similarity).
FT TRANSMEM 401 421 Helical; (Potential).
FT TOPO_DOM 422 473 Lumenal (By similarity).
FT TRANSMEM 474 494 Helical; (Potential).
FT TOPO_DOM 495 839 Cytoplasmic (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 18 18 Phosphoserine.
FT MOD_RES 656 656 Phosphoserine.
FT MOD_RES 735 735 Phosphoserine.
FT MOD_RES 738 738 Phosphoserine.
FT MOD_RES 741 741 Phosphoserine.
FT MOD_RES 828 828 Phosphoserine.
FT CARBOHYD 99 99 N-linked (GlcNAc...).
FT VAR_SEQ 1 61 Missing (in isoform 2).
FT /FTId=VSP_013396.
FT VAR_SEQ 455 528 NAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLR
FT PRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQ -> VHFG
FT RVAEPHCHTPHPHLLPAPTGPGDYRLLPKLHRGGRWCGRYL
FT LLCSDGCSPAWSSPVAICWADRGLSVPAS (in isoform
FT 3).
FT /FTId=VSP_013397.
FT VAR_SEQ 529 839 Missing (in isoform 3).
FT /FTId=VSP_013398.
FT VARIANT 592 592 S -> G (in dbSNP:rs2276635).
FT /FTId=VAR_021835.
FT VARIANT 659 659 Q -> H (in dbSNP:rs2276634).
FT /FTId=VAR_055534.
FT CONFLICT 39 39 H -> R (in Ref. 1; CAD97944).
FT CONFLICT 300 300 L -> P (in Ref. 1; CAD97944).
FT CONFLICT 381 381 A -> T (in Ref. 4; AAH65534).
FT CONFLICT 519 519 C -> R (in Ref. 1; CAD98061).
FT CONFLICT 567 567 W -> R (in Ref. 1; CAD98061).
FT CONFLICT 669 669 H -> N (in Ref. 5; BAB15246).
FT CONFLICT 765 765 A -> V (in Ref. 1; CAD97944).
SQ SEQUENCE 839 AA; 94447 MW; 69BE087CA550DC42 CRC64;
MAQFDTEYQR LEASYSDSPP GEEDLLVHVA EGSKSPWHHI ENLDLFFSRV YNLHQKNGFT
CMLIGEIFEL MQFLFVVAFT TFLVSCVDYD ILFANKMVNH SLHPTEPVKV TLPDAFLPAQ
VCSARIQENG SLITILVIAG VFWIHRLIKF IYNICCYWEI HSFYLHALRI PMSALPYCTW
QEVQARIVQT QKEHQICIHK RELTELDIYH RILRFQNYMV ALVNKSLLPL RFRLPGLGEA
VFFTRGLKYN FELILFWGPG SLFLNEWSLK AEYKRGGQRL ELAQRLSNRI LWIGIANFLL
CPLILIWQIL YAFFSYAEVL KREPGALGAR CWSLYGRCYL RHFNELEHEL QSRLNRGYKP
ASKYMNCFLS PLLTLLAKNG AFFAGSILAV LIALTIYDED VLAVEHVLTT VTLLGVTVTV
CRSFIPDQHM VFCPEQLLRV ILAHIHYMPD HWQGNAHRSQ TRDEFAQLFQ YKAVFILEEL
LSPIVTPLIL IFCLRPRALE IIDFFRNFTV EVVGVGDTCS FAQMDVRQHG HPQWLSAGQT
EASVYQQAED GKTELSLMHF AITNPGWQPP RESTAFLGFL KEQVQRDGAA ASLAQGGLLP
ENALFTSIQS LQSESEPLSL IANVVAGSSC RGPPLPRDLQ GSRHRAEVAS ALRSFSPLQP
GQAPTGRAHS TMTGSGVDAR TASSGSSVWE GQLQSLVLSE YASTEMSLHA LYMHQLHKQQ
AQAEPERHVW HRRESDESGE SAPDEGGEGA RAPQSIPRSA SYPCAAPRPG APETTALHGG
FQRRYGGITD PGTVPRVPSH FSRLPLGGWA EDGQSASRHP EPVPEEGSED ELPPQVHKV
//
ID ATG9A_HUMAN Reviewed; 839 AA.
AC Q7Z3C6; Q3ZAQ6; Q6P0N7; Q7Z317; Q7Z320; Q8NDK6; Q8WU65; Q9BVL5;
read moreAC Q9H6L1; Q9HAG7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=Autophagy-related protein 9A;
DE AltName: Full=APG9-like 1;
DE AltName: Full=mATG9;
GN Name=ATG9A; Synonyms=APG9L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-592.
RC TISSUE=Fetal brain, Lung endothelial cell, Rectum tumor, and Testis;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain, and Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-839, AND VARIANT
RP GLY-592.
RC TISSUE=Embryo;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP IDENTIFICATION.
RX PubMed=15755735; DOI=10.1074/jbc.M413957200;
RA Yamada T., Carson A.R., Caniggia I., Umebayashi K., Yoshimori T.,
RA Nakabayashi K., Scherer S.W.;
RT "Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an
RT autophagy-related protein (APG9-like2) highly expressed in
RT trophoblast.";
RL J. Biol. Chem. 280:18283-18290(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION AT ASN-99.
RX PubMed=16940348; DOI=10.1242/jcs.03172;
RA Young A.R., Chan E.Y., Hu X.W., Kochl R., Crawshaw S.G., High S.,
RA Hailey D.W., Lippincott-Schwartz J., Tooze S.A.;
RT "Starvation and ULK1-dependent cycling of mammalian Atg9 between the
RT TGN and endosomes.";
RL J. Cell Sci. 119:3888-3900(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-656, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=18936157; DOI=10.1128/MCB.01082-08;
RA Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.;
RT "Kinase-inactivated ULK proteins inhibit autophagy via their conserved
RT C-terminal domains using an Atg13-independent mechanism.";
RL Mol. Cell. Biol. 29:157-171(2009).
RN [11]
RP INTERACTION WITH SUPT20H.
RX PubMed=19893488; DOI=10.1038/emboj.2009.321;
RA Webber J.L., Tooze S.A.;
RT "Coordinated regulation of autophagy by p38alpha MAPK through mAtg9
RT and p38IP.";
RL EMBO J. 29:27-40(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=19910472; DOI=10.1074/jbc.M109.054197;
RA Gao W., Kang J.H., Liao Y., Ding W.X., Gambotto A.A., Watkins S.C.,
RA Liu Y.J., Stolz D.B., Yin X.M.;
RT "Biochemical isolation and characterization of the tubulovesicular
RT LC3-positive autophagosomal compartment.";
RL J. Biol. Chem. 285:1371-1383(2010).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=20124090; DOI=10.1369/jhc.2010.955690;
RA Tamura H., Shibata M., Koike M., Sasaki M., Uchiyama Y.;
RT "Atg9A protein, an autophagy-related membrane protein, is localized in
RT the neurons of mouse brains.";
RL J. Histochem. Cytochem. 58:443-453(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=21068542; DOI=10.4161/auto.7.1.14015;
RA Takahashi Y., Meyerkord C.L., Hori T., Runkle K., Fox T.E., Kester M.,
RA Loughran T.P., Wang H.G.;
RT "Bif-1 regulates Atg9 trafficking by mediating the fission of Golgi
RT membranes during autophagy.";
RL Autophagy 7:61-73(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735; SER-738 AND
RP SER-741, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in autophagy and cytoplasm to vacuole transport
CC (Cvt) vesicle formation. Plays a key role in the organization of
CC the preautophagosomal structure/phagophore assembly site (PAS),
CC the nucleating site for formation of the sequestering vesicle.
CC Cycles between a juxta-nuclear trans-Golgi network compartment and
CC late endosomes. Nutrient starvation induces accumulation on
CC autophagosomes. Starvation-dependent trafficking requires ULK1,
CC ATG13 and SUPT20H.
CC -!- SUBUNIT: Interacts with SUPT20H.
CC -!- INTERACTION:
CC Q8NEM7-2:-; NbExp=8; IntAct=EBI-727146, EBI-7568679;
CC Q9UHD2:TBK1; NbExp=2; IntAct=EBI-727146, EBI-356402;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane;
CC Multi-pass membrane protein. Golgi apparatus, trans-Golgi network
CC membrane; Multi-pass membrane protein. Late endosome membrane;
CC Multi-pass membrane protein. Endoplasmic reticulum membrane;
CC Multi-pass membrane protein. Note=Under amino acid starvation or
CC rapamycin treatment, redistributes from a juxtanuclear clustered
CC pool to a dispersed peripheral cytosolic pool. The starvation-
CC induced redistribution depends on ULK1, ATG13, as well as SH3GLB1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z3C6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3C6-2; Sequence=VSP_013396;
CC Name=3;
CC IsoId=Q7Z3C6-3; Sequence=VSP_013397, VSP_013398;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC -!- SIMILARITY: Belongs to the ATG9 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13882.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB15246.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB55119.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AL833865; CAD38723.1; -; mRNA.
DR EMBL; BX537984; CAD97944.1; -; mRNA.
DR EMBL; BX538192; CAD98061.1; -; mRNA.
DR EMBL; BX538198; CAD98064.1; -; mRNA.
DR EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW70706.1; -; Genomic_DNA.
DR EMBL; BC001098; AAH01098.2; -; mRNA.
DR EMBL; BC021202; AAH21202.2; -; mRNA.
DR EMBL; BC065534; AAH65534.1; -; mRNA.
DR EMBL; AK021732; BAB13882.1; ALT_INIT; mRNA.
DR EMBL; AK027448; BAB55119.1; ALT_INIT; mRNA.
DR EMBL; AK025822; BAB15246.1; ALT_INIT; mRNA.
DR EMBL; BK004018; DAA05199.1; -; mRNA.
DR RefSeq; NP_001070666.1; NM_001077198.2.
DR RefSeq; NP_076990.4; NM_024085.4.
DR RefSeq; XP_005246898.1; XM_005246841.1.
DR RefSeq; XP_005246899.1; XM_005246842.1.
DR RefSeq; XP_005246900.1; XM_005246843.1.
DR RefSeq; XP_005246901.1; XM_005246844.1.
DR RefSeq; XP_005246902.1; XM_005246845.1.
DR RefSeq; XP_005246903.1; XM_005246846.1.
DR RefSeq; XP_005246904.1; XM_005246847.1.
DR UniGene; Hs.323363; -.
DR ProteinModelPortal; Q7Z3C6; -.
DR IntAct; Q7Z3C6; 12.
DR MINT; MINT-1422125; -.
DR PhosphoSite; Q7Z3C6; -.
DR DMDM; 296439428; -.
DR PaxDb; Q7Z3C6; -.
DR PRIDE; Q7Z3C6; -.
DR DNASU; 79065; -.
DR Ensembl; ENST00000361242; ENSP00000355173; ENSG00000198925.
DR Ensembl; ENST00000396761; ENSP00000379983; ENSG00000198925.
DR Ensembl; ENST00000409033; ENSP00000386482; ENSG00000198925.
DR Ensembl; ENST00000409422; ENSP00000386535; ENSG00000198925.
DR Ensembl; ENST00000409618; ENSP00000386710; ENSG00000198925.
DR GeneID; 79065; -.
DR KEGG; hsa:79065; -.
DR UCSC; uc002vke.1; human.
DR CTD; 79065; -.
DR GeneCards; GC02M220074; -.
DR H-InvDB; HIX0002853; -.
DR H-InvDB; HIX0077803; -.
DR HGNC; HGNC:22408; ATG9A.
DR MIM; 612204; gene.
DR neXtProt; NX_Q7Z3C6; -.
DR PharmGKB; PA134931318; -.
DR eggNOG; NOG298729; -.
DR HOVERGEN; HBG050539; -.
DR InParanoid; Q7Z3C6; -.
DR OMA; EVVFFTR; -.
DR OrthoDB; EOG72C4ZM; -.
DR GeneWiki; ATG9A; -.
DR GenomeRNAi; 79065; -.
DR NextBio; 67835; -.
DR PRO; PR:Q7Z3C6; -.
DR ArrayExpress; Q7Z3C6; -.
DR Bgee; Q7Z3C6; -.
DR CleanEx; HS_ATG9A; -.
DR Genevestigator; Q7Z3C6; -.
DR GO; GO:0000421; C:autophagic vacuole membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagic vacuole assembly; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 1.
DR Pfam; PF04109; APG9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Autophagy; Complete proteome;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 839 Autophagy-related protein 9A.
FT /FTId=PRO_0000119820.
FT TOPO_DOM 2 66 Cytoplasmic (By similarity).
FT TRANSMEM 67 87 Helical; (Potential).
FT TOPO_DOM 88 131 Lumenal (By similarity).
FT TRANSMEM 132 152 Helical; (Potential).
FT TOPO_DOM 153 289 Cytoplasmic (By similarity).
FT TRANSMEM 290 310 Helical; (Potential).
FT TOPO_DOM 311 371 Lumenal (By similarity).
FT TRANSMEM 372 392 Helical; (Potential).
FT TOPO_DOM 393 400 Cytoplasmic (By similarity).
FT TRANSMEM 401 421 Helical; (Potential).
FT TOPO_DOM 422 473 Lumenal (By similarity).
FT TRANSMEM 474 494 Helical; (Potential).
FT TOPO_DOM 495 839 Cytoplasmic (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 18 18 Phosphoserine.
FT MOD_RES 656 656 Phosphoserine.
FT MOD_RES 735 735 Phosphoserine.
FT MOD_RES 738 738 Phosphoserine.
FT MOD_RES 741 741 Phosphoserine.
FT MOD_RES 828 828 Phosphoserine.
FT CARBOHYD 99 99 N-linked (GlcNAc...).
FT VAR_SEQ 1 61 Missing (in isoform 2).
FT /FTId=VSP_013396.
FT VAR_SEQ 455 528 NAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLR
FT PRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQ -> VHFG
FT RVAEPHCHTPHPHLLPAPTGPGDYRLLPKLHRGGRWCGRYL
FT LLCSDGCSPAWSSPVAICWADRGLSVPAS (in isoform
FT 3).
FT /FTId=VSP_013397.
FT VAR_SEQ 529 839 Missing (in isoform 3).
FT /FTId=VSP_013398.
FT VARIANT 592 592 S -> G (in dbSNP:rs2276635).
FT /FTId=VAR_021835.
FT VARIANT 659 659 Q -> H (in dbSNP:rs2276634).
FT /FTId=VAR_055534.
FT CONFLICT 39 39 H -> R (in Ref. 1; CAD97944).
FT CONFLICT 300 300 L -> P (in Ref. 1; CAD97944).
FT CONFLICT 381 381 A -> T (in Ref. 4; AAH65534).
FT CONFLICT 519 519 C -> R (in Ref. 1; CAD98061).
FT CONFLICT 567 567 W -> R (in Ref. 1; CAD98061).
FT CONFLICT 669 669 H -> N (in Ref. 5; BAB15246).
FT CONFLICT 765 765 A -> V (in Ref. 1; CAD97944).
SQ SEQUENCE 839 AA; 94447 MW; 69BE087CA550DC42 CRC64;
MAQFDTEYQR LEASYSDSPP GEEDLLVHVA EGSKSPWHHI ENLDLFFSRV YNLHQKNGFT
CMLIGEIFEL MQFLFVVAFT TFLVSCVDYD ILFANKMVNH SLHPTEPVKV TLPDAFLPAQ
VCSARIQENG SLITILVIAG VFWIHRLIKF IYNICCYWEI HSFYLHALRI PMSALPYCTW
QEVQARIVQT QKEHQICIHK RELTELDIYH RILRFQNYMV ALVNKSLLPL RFRLPGLGEA
VFFTRGLKYN FELILFWGPG SLFLNEWSLK AEYKRGGQRL ELAQRLSNRI LWIGIANFLL
CPLILIWQIL YAFFSYAEVL KREPGALGAR CWSLYGRCYL RHFNELEHEL QSRLNRGYKP
ASKYMNCFLS PLLTLLAKNG AFFAGSILAV LIALTIYDED VLAVEHVLTT VTLLGVTVTV
CRSFIPDQHM VFCPEQLLRV ILAHIHYMPD HWQGNAHRSQ TRDEFAQLFQ YKAVFILEEL
LSPIVTPLIL IFCLRPRALE IIDFFRNFTV EVVGVGDTCS FAQMDVRQHG HPQWLSAGQT
EASVYQQAED GKTELSLMHF AITNPGWQPP RESTAFLGFL KEQVQRDGAA ASLAQGGLLP
ENALFTSIQS LQSESEPLSL IANVVAGSSC RGPPLPRDLQ GSRHRAEVAS ALRSFSPLQP
GQAPTGRAHS TMTGSGVDAR TASSGSSVWE GQLQSLVLSE YASTEMSLHA LYMHQLHKQQ
AQAEPERHVW HRRESDESGE SAPDEGGEGA RAPQSIPRSA SYPCAAPRPG APETTALHGG
FQRRYGGITD PGTVPRVPSH FSRLPLGGWA EDGQSASRHP EPVPEEGSED ELPPQVHKV
//
MIM
612204
*RECORD*
*FIELD* NO
612204
*FIELD* TI
*612204 AUTOPHAGY 9, S. CEREVISIAE, HOMOLOG OF, A; ATG9A
;;APG9-LIKE 1; APG9L1
*FIELD* TX
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CLONING
Yamada et al. (2005) cloned mouse and human ATG9A, which they called
APG9L1. The deduced 839-amino acid human protein has an APG9-like domain
and predicted transmembrane domains. Northern blot and RT-PCR analysis
detected APG9L1 in all tissues examined. Mouse Apg9l1 was also widely
expressed. Time-lapse imaging showed that mouse Apg9l1 colocalized with
the autophagosome membrane marker Lc3 (MAP1LC3A; 601242) in transfected
COS-7 cells.
GENE FUNCTION
Using small interfering RNA, Yamada et al. (2005) found that knockdown
of APG9L1 in HeLa cells reduced starvation-induced autophagosome
formation and that mouse Apg9l2 (ATG9B; 612205) complemented the loss of
APG9L1. Yamada et al. (2005) concluded that APG9L1 is essential for
mammalian autophagy and that APG9L2 is complementary to APG9L1.
MAPPING
Yamada et al. (2005) stated that the ATG9A gene maps to chromosome 2q35.
EVOLUTION
Yamada et al. (2005) found that all lower eukaryotes have a single ATG9
gene, and all vertebrates they examined had 2 genes, ATG9A and ATG9B,
suggesting that a duplication of the ATG9 gene occurred before the
divergence of fish.
*FIELD* RF
1. Yamada, T.; Carson, A. R.; Caniggia, I.; Umebayashi, K.; Yoshimori,
T.; Nakabayashi, K.; Scherer, S. W.: Endothelial nitric-oxide synthase
antisense (NOS3AS) gene encodes an autophagy-related protein (APG9-like2)
highly expressed in trophoblast. J. Biol. Chem. 280: 18283-18290,
2005.
*FIELD* CD
Patricia A. Hartz: 7/30/2008
*FIELD* ED
wwang: 07/30/2008
*RECORD*
*FIELD* NO
612204
*FIELD* TI
*612204 AUTOPHAGY 9, S. CEREVISIAE, HOMOLOG OF, A; ATG9A
;;APG9-LIKE 1; APG9L1
*FIELD* TX
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CLONING
Yamada et al. (2005) cloned mouse and human ATG9A, which they called
APG9L1. The deduced 839-amino acid human protein has an APG9-like domain
and predicted transmembrane domains. Northern blot and RT-PCR analysis
detected APG9L1 in all tissues examined. Mouse Apg9l1 was also widely
expressed. Time-lapse imaging showed that mouse Apg9l1 colocalized with
the autophagosome membrane marker Lc3 (MAP1LC3A; 601242) in transfected
COS-7 cells.
GENE FUNCTION
Using small interfering RNA, Yamada et al. (2005) found that knockdown
of APG9L1 in HeLa cells reduced starvation-induced autophagosome
formation and that mouse Apg9l2 (ATG9B; 612205) complemented the loss of
APG9L1. Yamada et al. (2005) concluded that APG9L1 is essential for
mammalian autophagy and that APG9L2 is complementary to APG9L1.
MAPPING
Yamada et al. (2005) stated that the ATG9A gene maps to chromosome 2q35.
EVOLUTION
Yamada et al. (2005) found that all lower eukaryotes have a single ATG9
gene, and all vertebrates they examined had 2 genes, ATG9A and ATG9B,
suggesting that a duplication of the ATG9 gene occurred before the
divergence of fish.
*FIELD* RF
1. Yamada, T.; Carson, A. R.; Caniggia, I.; Umebayashi, K.; Yoshimori,
T.; Nakabayashi, K.; Scherer, S. W.: Endothelial nitric-oxide synthase
antisense (NOS3AS) gene encodes an autophagy-related protein (APG9-like2)
highly expressed in trophoblast. J. Biol. Chem. 280: 18283-18290,
2005.
*FIELD* CD
Patricia A. Hartz: 7/30/2008
*FIELD* ED
wwang: 07/30/2008