ATG9A
entrez
79065
canonical
uniprot
Q7Z3C6
canonical
ensembl
ENSG00000198925
resolver
ensp
ENSP00000355173
resolver
ensp
ENSP00000379983
resolver
genesymbol
ATG9A
resolver
genesymbol_syn
APG9L1
resolver
hgnc
HGNC:22408
resolver
uniprot
Q3ZAQ6
resolver
uniprot
Q6P0N7
resolver
uniprot
Q7Z317
resolver
uniprot
Q7Z320
resolver
uniprot
Q8NDK6
resolver
uniprot
Q8WU65
resolver
uniprot
Q9BVL5
resolver
uniprot
Q9H6L1
resolver
uniprot
Q9HAG7
resolver
uniprot_entry
ATG9A_HUMAN
resolver
uniprot_sec
Q3ZAQ6
resolver
uniprot_sec
Q6P0N7
resolver
uniprot_sec
Q7Z317
resolver
uniprot_sec
Q7Z320
resolver
uniprot_sec
Q8NDK6
resolver
uniprot_sec
Q8WU65
resolver
uniprot_sec
Q9BVL5
resolver
uniprot_sec
Q9H6L1
resolver
uniprot_sec
Q9HAG7
resolver
amino_acid_sequence
MAQFDTEYQRLEASYSDSPPGEEDLLVHVAEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSAGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAASLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAHSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHVWHRRESDESGESAPDEGGEGARAPQSIPRSASYPCAAPRPGAPETTALHGGFQRRYGGITDPGTVPRVPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV
uniprot
proteins
function
FUNCTION: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion (PubMed:22456507, PubMed:27510922, PubMed:29437695, PubMed:32513819, PubMed:32610138, PubMed:33106659, PubMed:33468622, PubMed:33850023). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (PubMed:16940348, PubMed:22456507, PubMed:33106659). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (PubMed:33106659). Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (PubMed:30917996). In addition to autophagy, also plays a role in necrotic cell death (By similarity). {ECO:0000250|UniProtKB:Q68FE2, ECO:0000269|PubMed:16940348, ECO:0000269|PubMed:22456507, ECO:0000269|PubMed:27510922, ECO:0000269|PubMed:29437695, ECO:0000269|PubMed:30917996, ECO:0000269|PubMed:32513819, ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0000269|PubMed:33468622, ECO:0000269|PubMed:33850023}.
uniprot
proteins
mass_dalton
94447
uniprot
proteins
mutagenesis
MUTAGEN 8; /note="Y->A: Abolished interaction with the AP-4 complex."; /evidence="ECO:0000269|PubMed:29180427"; MUTAGEN 9; /note="Q->A: Abolished interaction with the AP-4 complex."; /evidence="ECO:0000269|PubMed:29180427"; MUTAGEN 10; /note="R->A: Does not affect interaction with the AP-4 complex."; /evidence="ECO:0000269|PubMed:29180427"; MUTAGEN 11; /note="L->A: Abolished interaction with the AP-4 complex."; /evidence="ECO:0000269|PubMed:29180427"; MUTAGEN 12; /note="E->A: Abolished interaction with the AP-4 complex."; /evidence="ECO:0000269|PubMed:29180427"; MUTAGEN 15; /note="Y->A: Does not affect interaction with the AP-4 complex."; /evidence="ECO:0000269|PubMed:29180427"; MUTAGEN 99; /note="N->D: Abolished N-glycosylation."; /evidence="ECO:0000269|PubMed:27316455"; MUTAGEN 265; /note="N->W: Impaired autophagy."; /evidence="ECO:0000269|PubMed:32610138"; MUTAGEN 321..323; /note="KRE->LLL: Reduced lipid scramblase activity and autophagy. Strongly reduced autophagy; when associated with W-412. Strongly reduced lipid scramblase activity and autophagy; when associated with W-419."; /evidence="ECO:0000269|PubMed:33106659"; MUTAGEN 412; /note="T->W: Does not affect lipid scramblase activity. Strongly reduced autophagy; when associated with L-321--L-323."; /evidence="ECO:0000269|PubMed:33106659"; MUTAGEN 419; /note="T->W: Strongly reduced lipid scramblase activity and autophagy; when associated with L-321--L-323."; /evidence="ECO:0000269|PubMed:33106659"; MUTAGEN 422; /note="R->W: Impaired autophagy."; /evidence="ECO:0000269|PubMed:32610138"; MUTAGEN 516..519; /note="GDTC->ADTA: Impaired transport from the endoplasmic reticulum to the Golgi apparatus without affecting homooligomerization."; /evidence="ECO:0000269|PubMed:27663665"; MUTAGEN 711..713; /note="LYM->AAA: Impaired transport through the Golgi apparatus."; /evidence="ECO:0000269|PubMed:27316455
uniprot
proteins
post_translational_modification
PTM: Ufmylated in a DDRGK1 dependent manner. {ECO:0000250|UniProtKB:Q68FE2}.
uniprot
proteins
protein_family
ATG9 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15755735
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16940348
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18936157
uniprot
proteins
pubmed
19893488
uniprot
proteins
pubmed
19910472
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20124090
uniprot
proteins
pubmed
21068542
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22456507
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27316455
uniprot
proteins
pubmed
27510922
uniprot
proteins
pubmed
27663665
uniprot
proteins
pubmed
28536105
uniprot
proteins
pubmed
29180427
uniprot
proteins
pubmed
29437695
uniprot
proteins
pubmed
30262884
uniprot
proteins
pubmed
30917996
uniprot
proteins
pubmed
32073997
uniprot
proteins
pubmed
32513819
uniprot
proteins
pubmed
32610138
uniprot
proteins
pubmed
33106659
uniprot
proteins
pubmed
33468622
uniprot
proteins
pubmed
33773106
uniprot
proteins
pubmed
33850023
uniprot
proteins
pubmed
34432599
uniprot
proteins
sequence_length
839
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:32073997, ECO:0000269|PubMed:33106659}; Multi-pass membrane protein {ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:19910472}; Multi-pass membrane protein {ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16940348, ECO:0000269|PubMed:20124090, ECO:0000269|PubMed:21068542, ECO:0000269|PubMed:27316455, ECO:0000269|PubMed:27663665, ECO:0000269|PubMed:29180427, ECO:0000269|PubMed:33468622, ECO:0000305|PubMed:34432599}; Multi-pass membrane protein {ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659}. Late endosome membrane {ECO:0000269|PubMed:16940348, ECO:0000269|PubMed:20124090, ECO:0000269|PubMed:22456507, ECO:0000269|PubMed:32513819, ECO:0000269|PubMed:33468622}; Multi-pass membrane protein {ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659}. Recycling endosome membrane {ECO:0000269|PubMed:22456507, ECO:0000269|PubMed:29437695}; Multi-pass membrane protein {ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20124090, ECO:0000269|PubMed:27316455, ECO:0000269|PubMed:27663665}; Multi-pass membrane protein {ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659}. Mitochondrion membrane {ECO:0000305|PubMed:34432599}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly localizes to the trans-Golgi network (TGN) and the endosomal system; cycles between them though vesicle trafficking (PubMed:27316455, PubMed:27663665). Export from the TGN to promote formation of autophagosomes is mediated by the AP-4 complex (PubMed:29180427, PubMed:30262884). Under amino acid starvation or rapamycin treatment, redistributes to preautophagosomal structure/phagophore assembly site (PAS) (PubMed:16940348). The starvation-induced redistribution depends on ULK1, ATG13, as well as SH3GLB1 (PubMed:16940348). Upon autophagy induction, a small portion transiently localizes to the autophagic membranes (PubMed:22456507). Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner (PubMed:34432599). {ECO:0000269|PubMed:16940348, ECO:0000269|PubMed:22456507, ECO:0000269|PubMed:27316455, ECO:0000269|PubMed:27663665, ECO:0000269|PubMed:29180427, ECO:0000269|PubMed:30262884, ECO:0000269|PubMed:34432599}.
uniprot
proteins
transmembrane_region
TRANSMEM 62..84; /note="Helical"; /evidence="ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0007744|PDB:6WQZ, ECO:0007744|PDB:6WR4, ECO:0007744|PDB:7JLO, ECO:0007744|PDB:7JLP, ECO:0007744|PDB:7JLQ"; TRANSMEM 129..154; /note="Helical"; /evidence="ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0007744|PDB:6WQZ, ECO:0007744|PDB:6WR4, ECO:0007744|PDB:7JLO, ECO:0007744|PDB:7JLP, ECO:0007744|PDB:7JLQ"; TRANSMEM 372..397; /note="Helical"; /evidence="ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0007744|PDB:6WQZ, ECO:0007744|PDB:6WR4, ECO:0007744|PDB:7JLO, ECO:0007744|PDB:7JLP, ECO:0007744|PDB:7JLQ"; TRANSMEM 407..424; /note="Helical"; /evidence="ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0007744|PDB:6WQZ, ECO:0007744|PDB:6WR4, ECO:0007744|PDB:7JLO, ECO:0007744|PDB:7JLP, ECO:0007744|PDB:7JLQ
uniprot
proteins