ID H7C1G6_HUMAN Unreviewed; 244 AA. AC H7C1G6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Autophagy-related protein 9 {ECO:0000256|RuleBase:RU364027}; DE Flags: Fragment; GN Name=ATG9A {ECO:0000313|Ensembl:ENSP00000400234.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000400234.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000400234.1, ECO:0000313|Proteomes:UP000005640} 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., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [2] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [3] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [4] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [5] {ECO:0000313|Ensembl:ENSP00000400234.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: Phospholipid scramblase involved in autophagy. Cycles between CC the preautophagosomal structure/phagophore assembly site (PAS) and the CC cytoplasmic vesicle pool and supplies membrane for the growing CC autophagosome. Lipid scramblase activity plays a key role in CC preautophagosomal structure/phagophore assembly by distributing the CC phospholipids that arrive through ATG2 from the cytoplasmic to the CC luminal leaflet of the bilayer, thereby driving autophagosomal membrane CC expansion. {ECO:0000256|RuleBase:RU364027}. CC -!- SUBCELLULAR LOCATION: Endosome membrane CC {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004337}. Late endosome membrane CC {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004107}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Preautophagosomal structure membrane CC {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004511, CC ECO:0000256|RuleBase:RU364027}. CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000256|ARBA:ARBA00006185, CC ECO:0000256|RuleBase:RU364027}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H7C1G6; -. DR SMR; H7C1G6; -. DR MassIVE; H7C1G6; -. DR MaxQB; H7C1G6; -. DR PeptideAtlas; H7C1G6; -. DR ProteomicsDB; 44636; -. DR Antibodypedia; 34308; 488 antibodies from 38 providers. DR Ensembl; ENST00000429920.1; ENSP00000400234.1; ENSG00000198925.12. DR UCSC; uc061ssr.1; human. DR HGNC; HGNC:22408; ATG9A. DR VEuPathDB; HostDB:ENSG00000198925; -. DR GeneTree; ENSGT00390000014839; -. DR HOGENOM; CLU_1140225_0_0_1; -. DR ChiTaRS; ATG9A; human. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000198925; Expressed in gastrocnemius and 97 other cell types or tissues. DR ExpressionAtlas; H7C1G6; baseline and differential. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR InterPro; IPR007241; Autophagy-rel_prot_9. DR PANTHER; PTHR13038; APG9 AUTOPHAGY 9; 1. DR PANTHER; PTHR13038:SF13; AUTOPHAGY-RELATED PROTEIN 9A; 1. DR Pfam; PF04109; ATG9; 1. PE 1: Evidence at protein level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU364027}; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Lipid transport {ECO:0000256|RuleBase:RU364027}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Proteomics identification {ECO:0007829|EPD:H7C1G6, KW ECO:0007829|MaxQB:H7C1G6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}; KW Transport {ECO:0000256|RuleBase:RU364027}. FT REGION 212..244 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 214..244 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000400234.1" FT NON_TER 244 FT /evidence="ECO:0000313|Ensembl:ENSP00000400234.1" SQ SEQUENCE 244 AA; 26759 MW; 71F9B0004318F3AA CRC64; LAHIHYMPDH WQGNAHRSQT RDEFAQLFQY KAVFILEELL SPIVTPLILI FCLRPRALEI IDFFRNFTVE VVGVGDTCSF AQMDVRQHGH PQWLSAGQTE ASVYQQAEDG KTELSLMHFA ITNPGWQPPR ESTAFLGFLK EQVQRDGAAA SLAQGGLLPE NALFTSIQSL QSESEPLSLI ANVVAGSSCR GPPLPRDLQG SRHRAEVASA LRSFSPLQPG QAPTGRAHST MTGSGSTSSR PRLN //