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Autophagy-related protein 9A (APG9-like 1) (mATG9)

 ATG9A_HUMAN             Reviewed;         839 AA.
Q7Z3C6; Q3ZAQ6; Q6P0N7; Q7Z317; Q7Z320; Q8NDK6; Q8WU65; Q9BVL5;
Q9H6L1; Q9HAG7;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
27-SEP-2017, entry version 135.
RecName: Full=Autophagy-related protein 9A;
AltName: Full=APG9-like 1;
AltName: Full=mATG9;
Name=ATG9A; Synonyms=APG9L1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
GLY-592.
TISSUE=Fetal brain, Lung endothelial cell, Rectum tumor, and 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).
[2]
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).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain, and Lymph;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-839, AND VARIANT
GLY-592.
TISSUE=Embryo;
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).
[6]
IDENTIFICATION.
PubMed=15755735; DOI=10.1074/jbc.M413957200;
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION AT ASN-99.
PubMed=16940348; DOI=10.1242/jcs.03172;
Young A.R., Chan E.Y., Hu X.W., Kochl R., Crawshaw S.G., High S.,
Hailey D.W., Lippincott-Schwartz J., Tooze S.A.;
"Starvation and ULK1-dependent cycling of mammalian Atg9 between the
TGN and endosomes.";
J. Cell Sci. 119:3888-3900(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-656, 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).
[10]
SUBCELLULAR LOCATION.
PubMed=18936157; DOI=10.1128/MCB.01082-08;
Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.;
"Kinase-inactivated ULK proteins inhibit autophagy via their conserved
C-terminal domains using an Atg13-independent mechanism.";
Mol. Cell. Biol. 29:157-171(2009).
[11]
INTERACTION WITH SUPT20H.
PubMed=19893488; DOI=10.1038/emboj.2009.321;
Webber J.L., Tooze S.A.;
"Coordinated regulation of autophagy by p38alpha MAPK through mAtg9
and p38IP.";
EMBO J. 29:27-40(2010).
[12]
SUBCELLULAR LOCATION.
PubMed=19910472; DOI=10.1074/jbc.M109.054197;
Gao W., Kang J.H., Liao Y., Ding W.X., Gambotto A.A., Watkins S.C.,
Liu Y.J., Stolz D.B., Yin X.M.;
"Biochemical isolation and characterization of the tubulovesicular
LC3-positive autophagosomal compartment.";
J. Biol. Chem. 285:1371-1383(2010).
[13]
SUBCELLULAR LOCATION.
PubMed=20124090; DOI=10.1369/jhc.2010.955690;
Tamura H., Shibata M., Koike M., Sasaki M., Uchiyama Y.;
"Atg9A protein, an autophagy-related membrane protein, is localized in
the neurons of mouse brains.";
J. Histochem. Cytochem. 58:443-453(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, 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).
[15]
SUBCELLULAR LOCATION, AND TRAFFICKING.
PubMed=21068542; DOI=10.4161/auto.7.1.14015;
Takahashi Y., Meyerkord C.L., Hori T., Runkle K., Fox T.E., Kester M.,
Loughran T.P., Wang H.G.;
"Bif-1 regulates Atg9 trafficking by mediating the fission of Golgi
membranes during autophagy.";
Autophagy 7:61-73(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735; SER-738 AND
SER-741, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-18; SER-656;
SER-735 AND SER-828, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735 AND SER-828, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Involved in autophagy and cytoplasm to vacuole transport
(Cvt) vesicle formation. Plays a key role in the organization of
the preautophagosomal structure/phagophore assembly site (PAS),
the nucleating site for formation of the sequestering vesicle.
Cycles between a juxta-nuclear trans-Golgi network compartment and
late endosomes. Nutrient starvation induces accumulation on
autophagosomes. Starvation-dependent trafficking requires ULK1,
ATG13 and SUPT20H. {ECO:0000269|PubMed:16940348}.
-!- SUBUNIT: Interacts with SUPT20H. {ECO:0000269|PubMed:19893488}.
-!- INTERACTION:
Q8NEM7-2:-; NbExp=8; IntAct=EBI-727146, EBI-7568679;
A0PJX0:CIB4; NbExp=4; IntAct=EBI-12006308, EBI-12868028;
Q15323:KRT31; NbExp=3; IntAct=EBI-727146, EBI-948001;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-727146, EBI-10171774;
Q8IUC1:KRTAP11-1; NbExp=4; IntAct=EBI-12006308, EBI-1052037;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-727146, EBI-10172511;
P26371:KRTAP5-9; NbExp=3; IntAct=EBI-727146, EBI-3958099;
Q3LI66:KRTAP6-2; NbExp=4; IntAct=EBI-12006308, EBI-11962084;
Q17RB8:LONRF1; NbExp=3; IntAct=EBI-727146, EBI-2341787;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-727146, EBI-945833;
Q04864:REL; NbExp=3; IntAct=EBI-727146, EBI-307352;
Q9UHD2:TBK1; NbExp=2; IntAct=EBI-727146, EBI-356402;
Q05086-2:UBE3A; NbExp=3; IntAct=EBI-727146, EBI-10175863;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane;
Multi-pass membrane protein. Golgi apparatus, trans-Golgi network
membrane; Multi-pass membrane protein. Late endosome membrane;
Multi-pass membrane protein. Endoplasmic reticulum membrane;
Multi-pass membrane protein. Note=Under amino acid starvation or
rapamycin treatment, redistributes from a juxtanuclear clustered
pool to a dispersed peripheral cytosolic pool. The starvation-
induced redistribution depends on ULK1, ATG13, as well as SH3GLB1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q7Z3C6-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z3C6-2; Sequence=VSP_013396;
Name=3;
IsoId=Q7Z3C6-3; Sequence=VSP_013397, VSP_013398;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB13882.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15246.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB55119.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AL833865; CAD38723.1; -; mRNA.
EMBL; BX537984; CAD97944.1; -; mRNA.
EMBL; BX538192; CAD98061.1; -; mRNA.
EMBL; BX538198; CAD98064.1; -; mRNA.
EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471063; EAW70706.1; -; Genomic_DNA.
EMBL; BC001098; AAH01098.2; -; mRNA.
EMBL; BC021202; AAH21202.2; -; mRNA.
EMBL; BC065534; AAH65534.1; -; mRNA.
EMBL; AK021732; BAB13882.1; ALT_INIT; mRNA.
EMBL; AK027448; BAB55119.1; ALT_INIT; mRNA.
EMBL; AK025822; BAB15246.1; ALT_INIT; mRNA.
EMBL; BK004018; DAA05199.1; -; mRNA.
CCDS; CCDS42820.1; -. [Q7Z3C6-1]
RefSeq; NP_001070666.1; NM_001077198.2. [Q7Z3C6-1]
RefSeq; NP_076990.4; NM_024085.4. [Q7Z3C6-1]
UniGene; Hs.323363; -.
ProteinModelPortal; Q7Z3C6; -.
BioGrid; 122518; 52.
IntAct; Q7Z3C6; 63.
MINT; MINT-1422125; -.
STRING; 9606.ENSP00000355173; -.
iPTMnet; Q7Z3C6; -.
PhosphoSitePlus; Q7Z3C6; -.
BioMuta; ATG9A; -.
DMDM; 296439428; -.
EPD; Q7Z3C6; -.
MaxQB; Q7Z3C6; -.
PaxDb; Q7Z3C6; -.
PeptideAtlas; Q7Z3C6; -.
PRIDE; Q7Z3C6; -.
DNASU; 79065; -.
Ensembl; ENST00000361242; ENSP00000355173; ENSG00000198925. [Q7Z3C6-1]
Ensembl; ENST00000396761; ENSP00000379983; ENSG00000198925. [Q7Z3C6-1]
Ensembl; ENST00000409033; ENSP00000386482; ENSG00000198925. [Q7Z3C6-3]
Ensembl; ENST00000409422; ENSP00000386535; ENSG00000198925. [Q7Z3C6-2]
Ensembl; ENST00000409618; ENSP00000386710; ENSG00000198925. [Q7Z3C6-1]
GeneID; 79065; -.
KEGG; hsa:79065; -.
UCSC; uc002vke.3; human. [Q7Z3C6-1]
CTD; 79065; -.
DisGeNET; 79065; -.
EuPathDB; HostDB:ENSG00000198925.10; -.
GeneCards; ATG9A; -.
H-InvDB; HIX0002853; -.
H-InvDB; HIX0077803; -.
HGNC; HGNC:22408; ATG9A.
HPA; HPA059551; -.
MIM; 612204; gene.
neXtProt; NX_Q7Z3C6; -.
OpenTargets; ENSG00000198925; -.
PharmGKB; PA134931318; -.
eggNOG; KOG2173; Eukaryota.
eggNOG; ENOG410XQBE; LUCA.
GeneTree; ENSGT00390000014839; -.
HOVERGEN; HBG050539; -.
InParanoid; Q7Z3C6; -.
KO; K17907; -.
OMA; SCVDYDI; -.
OrthoDB; EOG091G01WQ; -.
PhylomeDB; Q7Z3C6; -.
TreeFam; TF313665; -.
Reactome; R-HSA-1632852; Macroautophagy.
ChiTaRS; ATG9A; human.
GeneWiki; ATG9A; -.
GenomeRNAi; 79065; -.
PRO; PR:Q7Z3C6; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000198925; -.
CleanEx; HS_ATG9A; -.
ExpressionAtlas; Q7Z3C6; baseline and differential.
Genevisible; Q7Z3C6; HS.
GO; GO:0005776; C:autophagosome; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005770; C:late endosome; IDA:MGI.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0000407; C:pre-autophagosomal structure; IDA:MGI.
GO; GO:0055037; C:recycling endosome; IDA:MGI.
GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
GO; GO:0000045; P:autophagosome assembly; IMP:MGI.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
GO; GO:0034497; P:protein localization to pre-autophagosomal structure; IBA:GO_Central.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
InterPro; IPR007241; Autophagy-rel_prot_9.
PANTHER; PTHR13038; PTHR13038; 1.
Pfam; PF04109; APG9; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Autophagy; Complete proteome;
Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Glycoprotein;
Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 839 Autophagy-related protein 9A.
/FTId=PRO_0000119820.
TOPO_DOM 2 66 Cytoplasmic. {ECO:0000250}.
TRANSMEM 67 87 Helical. {ECO:0000255}.
TOPO_DOM 88 131 Lumenal. {ECO:0000250}.
TRANSMEM 132 152 Helical. {ECO:0000255}.
TOPO_DOM 153 289 Cytoplasmic. {ECO:0000250}.
TRANSMEM 290 310 Helical. {ECO:0000255}.
TOPO_DOM 311 371 Lumenal. {ECO:0000250}.
TRANSMEM 372 392 Helical. {ECO:0000255}.
TOPO_DOM 393 400 Cytoplasmic. {ECO:0000250}.
TRANSMEM 401 421 Helical. {ECO:0000255}.
TOPO_DOM 422 473 Lumenal. {ECO:0000250}.
TRANSMEM 474 494 Helical. {ECO:0000255}.
TOPO_DOM 495 839 Cytoplasmic. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000250|UniProtKB:Q68FE2}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 656 656 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 741 741 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 828 828 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16940348}.
VAR_SEQ 1 61 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_013396.
VAR_SEQ 455 528 NAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLR
PRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQ -> VHFG
RVAEPHCHTPHPHLLPAPTGPGDYRLLPKLHRGGRWCGRYL
LLCSDGCSPAWSSPVAICWADRGLSVPAS (in isoform
3). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_013397.
VAR_SEQ 529 839 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013398.
VARIANT 592 592 S -> G (in dbSNP:rs2276635).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_021835.
VARIANT 659 659 Q -> H (in dbSNP:rs2276634).
/FTId=VAR_055534.
CONFLICT 39 39 H -> R (in Ref. 1; CAD97944).
{ECO:0000305}.
CONFLICT 300 300 L -> P (in Ref. 1; CAD97944).
{ECO:0000305}.
CONFLICT 381 381 A -> T (in Ref. 4; AAH65534).
{ECO:0000305}.
CONFLICT 519 519 C -> R (in Ref. 1; CAD98061).
{ECO:0000305}.
CONFLICT 567 567 W -> R (in Ref. 1; CAD98061).
{ECO:0000305}.
CONFLICT 669 669 H -> N (in Ref. 5; BAB15246).
{ECO:0000305}.
CONFLICT 765 765 A -> V (in Ref. 1; CAD97944).
{ECO:0000305}.
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


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