ATG9_SCHPO
ID ATG9_SCHPO Reviewed; 702 AA.
AC O74312;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Autophagy-related protein 9 {ECO:0000303|PubMed:19778961};
GN Name=atg9 {ECO:0000303|PubMed:19778961}; Synonyms=apg9;
GN ORFNames=SPBC15D4.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=19778961; DOI=10.1099/mic.0.034389-0;
RA Mukaiyama H., Kajiwara S., Hosomi A., Giga-Hama Y., Tanaka N., Nakamura T.,
RA Takegawa K.;
RT "Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial
RT sporulation during nitrogen starvation.";
RL Microbiology 155:3816-3826(2009).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CTL1.
RX PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA Du L.L.;
RT "Global analysis of fission yeast mating genes reveals new autophagy
RT factors.";
RL PLoS Genet. 9:E1003715-E1003715(2013).
RN [4] {ECO:0007744|PDB:7D0I}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), SUBUNIT, TOPOLOGY, AND
RP DOMAIN.
RX PubMed=33106658; DOI=10.1038/s41594-020-00518-w;
RA Matoba K., Kotani T., Tsutsumi A., Tsuji T., Mori T., Noshiro D.,
RA Sugita Y., Nomura N., Iwata S., Ohsumi Y., Fujimoto T., Nakatogawa H.,
RA Kikkawa M., Noda N.N.;
RT "Atg9 is a lipid scramblase that mediates autophagosomal membrane
RT expansion.";
RL Nat. Struct. Mol. Biol. 27:1185-1193(2020).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm
CC to vacuole transport (Cvt) vesicle formation (PubMed:23950735). Cycles
CC between the preautophagosomal structure/phagophore assembly site (PAS)
CC and the cytoplasmic vesicle pool and supplies membrane for the growing
CC autophagosome (By similarity). Lipid scramblase activity plays a key
CC role in preautophagosomal structure/phagophore assembly by distributing
CC the phospholipids that arrive through atg2 from the cytoplasmic to the
CC luminal leaflet of the bilayer, thereby driving autophagosomal membrane
CC expansion (By similarity). Also involved in endoplasmic reticulum-
CC specific autophagic process and is essential for the survival of cells
CC subjected to severe ER stress (By similarity). Different machineries
CC are required for anterograde trafficking to the PAS during either the
CC Cvt pathway or bulk autophagy and for retrograde trafficking (By
CC similarity). Has a role in meiosis and sporulation (PubMed:19778961).
CC {ECO:0000250|UniProtKB:Q12142, ECO:0000269|PubMed:19778961,
CC ECO:0000269|PubMed:23950735}.
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 (PubMed:33106658). Interacts
CC with ctl1 (PubMed:23950735). {ECO:0000269|PubMed:23950735,
CC ECO:0000269|PubMed:33106658}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:23950735}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23950735}. 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 (PubMed:33106658). Acts as a lipid scramblase that uses its
CC central pore to function: the central pore opens laterally to
CC accommodate lipid headgroups, thereby enabling lipid flipping and
CC redistribution of lipids added to the outer leaflet of atg9-containing
CC vesicles, thereby enabling growth into autophagosomes
CC (PubMed:33106658). {ECO:0000269|PubMed:33106658}.
CC -!- PTM: Phosphorylated by atg1. Atg1 phosphorylation is required for
CC preautophagosome elongation. {ECO:0000250|UniProtKB:Q12142}.
CC -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA20482.1; -; Genomic_DNA.
DR PIR; T39483; T39483.
DR RefSeq; NP_596247.1; NM_001022166.2.
DR PDB; 7D0I; EM; 3.00 A; B/D/F/H/J/L=1-702.
DR PDBsum; 7D0I; -.
DR AlphaFoldDB; O74312; -.
DR SMR; O74312; -.
DR BioGRID; 276398; 20.
DR STRING; 4896.SPBC15D4.07c.1; -.
DR iPTMnet; O74312; -.
DR MaxQB; O74312; -.
DR PaxDb; O74312; -.
DR PRIDE; O74312; -.
DR EnsemblFungi; SPBC15D4.07c.1; SPBC15D4.07c.1:pep; SPBC15D4.07c.
DR GeneID; 2539850; -.
DR KEGG; spo:SPBC15D4.07c; -.
DR PomBase; SPBC15D4.07c; atg9.
DR VEuPathDB; FungiDB:SPBC15D4.07c; -.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_006200_3_1_1; -.
DR InParanoid; O74312; -.
DR OMA; ELMTISW; -.
DR PhylomeDB; O74312; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR PRO; PR:O74312; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
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:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
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:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:PomBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 1.
DR Pfam; PF04109; ATG9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..702
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119837"
FT TOPO_DOM 1..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..223
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33106658,
FT ECO:0007744|PDB:7D0I"
FT TOPO_DOM 224..251
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 252..270
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33106658,
FT ECO:0007744|PDB:7D0I"
FT TOPO_DOM 271..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 422..446
FT /evidence="ECO:0000269|PubMed:33106658,
FT ECO:0007744|PDB:7D0I"
FT TOPO_DOM 447..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 497..522
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33106658,
FT ECO:0007744|PDB:7D0I"
FT TOPO_DOM 523..537
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 538..555
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33106658,
FT ECO:0007744|PDB:7D0I"
FT TOPO_DOM 556..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 604..624
FT /evidence="ECO:0000305|PubMed:33106658"
FT TOPO_DOM 625..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 35..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 198..223
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 253..287
FT /evidence="ECO:0007829|PDB:7D0I"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:7D0I"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:7D0I"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 427..447
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:7D0I"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 472..480
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 483..489
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 496..520
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 538..555
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 565..576
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 591..599
FT /evidence="ECO:0007829|PDB:7D0I"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 603..623
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:7D0I"
FT HELIX 629..638
FT /evidence="ECO:0007829|PDB:7D0I"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:7D0I"
FT TURN 644..646
FT /evidence="ECO:0007829|PDB:7D0I"
FT STRAND 647..650
FT /evidence="ECO:0007829|PDB:7D0I"
FT TURN 651..655
FT /evidence="ECO:0007829|PDB:7D0I"
SQ SEQUENCE 702 AA; 81705 MW; 6FC67C2F75530FF5 CRC64;
MFYQPAQNKK QYDDLADIEA QNNVPNTQEV LEAWQESLDS DEDESSPLEE SNGFTISEHD
DFVKSVPRKN NPTDLLYSGK LLDSDEPPSV HGNSSKVPSK HPSPSFPETT SLRNLQNGSK
QKPALPNFND PHFYNEDVTR SGHPNRSIYT QLPRNEFSNA RVLWNRLSAR DRVLWRWANV
ENLDSFLQQV YTYYTGKGLS CIIVHRLFQI LTVSFVIGFT TFITSCIDWP AVTPHGSLAG
VTKSQCIAQM SPITYLVLWL FLSFLLALWI YYLTDIPRLW QMREFYIHAL KIATADMPTV
SWQRVLYRLL KLKNVNALTA EDGRVVSLHN MKRLDAYAIA NRIMRKDNYF IALINNGIIN
IELPLLHRRI LTHTTEWNIN WCIFNFVFDE QGQLRSAFRN PNSRKRLSEE LRRRFIVAGF
LNCLFAPIVA IYLVIHNFFR YFNEYHKNPG ALSTRRYTPL ALWTFREYNE LQHFFDERIN
DSYAAASHYV SQFPDFNMIR LFKYISFILG SFTAILVIIT VFDPELMVTF EITKDRSVLF
YLGLFGSLIA VSRSIIPDET LVFAPEKALR RVITFTHYMP GWWSDNMHSK AVQQEFCSLY
SYRIVNLLWE ILGILLTPVL LFFTFPSCSQ DIVDFFREHT INVEGVGYVC SYAVFQDNPP
YESVASLVQS RKISPLIQNK PELSRISFYE QFNTEAPRRD LR
