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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
 
 
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