ATG9_PICAN
ID ATG9_PICAN Reviewed; 889 AA.
AC A7KAI7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm
CC to vacuole transport (Cvt) vesicle formation (PubMed:17204848). Cycles
CC between the preautophagosomal structure/phagophore assembly site (PAS)
CC and the 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. Required for mitophagy. Also involved in endoplasmic
CC reticulum-specific autophagic process and is essential for the survival
CC of cells subjected to severe ER stress. Different machineries are
CC required for anterograde trafficking to the PAS during either the Cvt
CC pathway or bulk autophagy and for retrograde trafficking (By
CC similarity). {ECO:0000250|UniProtKB:Q12142,
CC ECO:0000269|PubMed:17204848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-
CC 3-phosphate)(out); Xref=Rhea:RHEA:67920, ChEBI:CHEBI:58088;
CC Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms
CC a path between the two membrane leaflets.
CC {ECO:0000250|UniProtKB:O74312}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}.
CC -!- DOMAIN: Forms a homotrimer with a solvated central pore, which is
CC connected laterally to the cytosol through the cavity within each
CC protomer. Acts as a lipid scramblase that uses its central pore to
CC function: the central pore opens laterally to accommodate lipid
CC headgroups, thereby enabling lipid flipping and redistribution of
CC lipids added to the outer leaflet of ATG9-containing vesicles, thereby
CC enabling growth into autophagosomes. {ECO:0000250|UniProtKB:O74312}.
CC -!- PTM: Phosphorylated by ATG1. ATG1 phosphorylation is required for
CC preautophagosome elongation. {ECO:0000250|UniProtKB:Q12142}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
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DR EMBL; EF102888; ABO31292.1; -; Genomic_DNA.
DR AlphaFoldDB; A7KAI7; -.
DR SMR; A7KAI7; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; 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; PTHR13038; 1.
DR Pfam; PF04109; ATG9; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus;
KW Lipid transport; Membrane; Phosphoprotein; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..889
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000317913"
FT TOPO_DOM 1..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..299
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 396
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 397..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..549
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 652..672
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 673..889
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 41..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 102069 MW; 8927A7EC2EB1B394 CRC64;
MGDLNKHTFL SRVFGSASNP LLNDDNNDIE FSINNLQDTF EEHQVESPPR APHPINVNSE
DESSSETESA SNEDLLYDQK RELYQQVESE LRQDDYDTVP ESLMMERRRP HEGSTRTIGT
KIPPSPAEPP IGPNITQWGE KARGIASRTL DNIPKTIAKG ISFQLPANAS SKLPPPPLSY
RRETSVGGET EMAQNINEQR QLRGRLGLLS PMERALWLWS NVSNLDTFLE DVYGYYTGNG
YRCIILSRVS DLLIIVFVVW LTSFMGNCVD YNQLMNGNAT KYSDVVVDKC YSKISLSQKL
FFLVLFAILV LRIKSFYSHF KDLKEIKNFY NLLLGVSDEE LQTISWSTIV KKIKVLRDQN
TNALISGNQN LRGDDLKSKK RLSAHDIANR LMRKENYMIA IFNKNVLAPA LTIPFINHHF
LTKTLEWNLK LCIFDFVFNT DGQLKQAVLS EHKRLALATE MRKRFRLAGI LSIFLTPFLV
IYFLLYFFLK FFYDIKTNPS LVGSREYSPY ARWKLREFNE LPHMFDKRLK MSRARATEYI
NQFPKEATNI ILNFVAFVTG SLVTILVVLT VLGHENFLNF ELTEGRTVLF YISTLGAVFT
ICKGSVSEND TVFDPEASLR YVAQFTHYLP NSWNGRFHTE EVKNEFCKLF NLRLILVLKE
ITSLIMLPYI LYCRLPDVSE KVIDFFREFS VHVDGLGYVC TFAMFEFDSK DKPVRSQAAN
DDDDLKQEYY TADDDKMVKS YLYFLESYGN ESVRKTGKEP AVDRISRRPG KKNLLRSAMM
NNSMMDKSRG AQSTVRYPPQ FRSPNLAESV YTKRQNIDLM EDTTAGLSTD TRNYLQTLNN
STLLGESFQH GFPVEDTTHH EEDADSEDDD EAGVLGLINQ IYKHKEGVN
