ATG9B_MOUSE
ID ATG9B_MOUSE Reviewed; 922 AA.
AC Q6EBV9; F8VQL8; Q674R6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Autophagy-related protein 9B {ECO:0000305};
DE AltName: Full=APG9-like 2 {ECO:0000303|PubMed:15755735};
DE AltName: Full=Nitric oxide synthase 3-overlapping antisense gene protein {ECO:0000303|PubMed:15234981};
GN Name=Atg9b {ECO:0000312|MGI:MGI:2685420};
GN Synonyms=Apg9l2 {ECO:0000303|PubMed:15755735},
GN Nos3as {ECO:0000303|PubMed:15234981};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129S6/SvEvTac, and CD-1; TISSUE=Placenta;
RX PubMed=15234981; DOI=10.1074/jbc.m400271200;
RA Robb G.B., Carson A.R., Tai S.C., Fish J.E., Singh S., Yamada T.,
RA Scherer S.W., Nakabayashi K., Marsden P.A.;
RT "Post-transcriptional regulation of endothelial nitric-oxide synthase by an
RT overlapping antisense mRNA transcript.";
RL J. Biol. Chem. 279:37982-37996(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15755735; DOI=10.1074/jbc.m413957200;
RA Yamada T., Carson A.R., Caniggia I., Umebayashi K., Yoshimori T.,
RA Nakabayashi K., Scherer S.W.;
RT "Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes an
RT autophagy-related protein (APG9-like2) highly expressed in trophoblast.";
RL J. Biol. Chem. 280:18283-18290(2005).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy by mediating
CC autophagosomal membrane expansion (PubMed:15755735). Cycles between the
CC 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 (ATG2A or ATG2B) from the
CC cytoplasmic to the luminal leaflet of the bilayer, thereby driving
CC autophagosomal membrane expansion (By similarity). In addition to
CC autophagy, also plays a role in necrotic cell death (By similarity).
CC {ECO:0000250|UniProtKB:Q68FE2, ECO:0000250|UniProtKB:Q7Z3C6,
CC ECO:0000269|PubMed:15755735}.
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:Q7Z3C6};
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:Q7Z3C6};
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:Q7Z3C6};
CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms
CC a path between the two membrane leaflets.
CC {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:15755735}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15755735}. Note=Under amino acid starvation or
CC rapamycin treatment, redistributes from a juxtanuclear clustered pool
CC to a dispersed peripheral cytosolic pool. The starvation-induced
CC redistribution depends on ULK1 and ATG13.
CC {ECO:0000250|UniProtKB:Q674R7}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, and placenta and testis.
CC {ECO:0000269|PubMed:15234981, ECO:0000269|PubMed:15755735}.
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 ATG9B-containing vesicles, thereby
CC enabling growth into autophagosomes. {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- DOMAIN: The tyrosine-based sorting signal motif, also named YXX-psi
CC motif, promotes interaction with the AP-4 complex.
CC {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS87213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY495541; AAS72555.1; -; mRNA.
DR EMBL; AY515312; AAS87213.1; ALT_INIT; mRNA.
DR EMBL; AY515313; AAS87214.1; -; mRNA.
DR EMBL; AC113055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK004021; DAA05202.1; -; mRNA.
DR CCDS; CCDS39027.1; -.
DR RefSeq; NP_001002897.2; NM_001002897.3.
DR AlphaFoldDB; Q6EBV9; -.
DR SMR; Q6EBV9; -.
DR STRING; 10090.ENSMUSP00000051864; -.
DR iPTMnet; Q6EBV9; -.
DR PhosphoSitePlus; Q6EBV9; -.
DR PaxDb; Q6EBV9; -.
DR PRIDE; Q6EBV9; -.
DR ProteomicsDB; 277191; -.
DR Antibodypedia; 32933; 270 antibodies from 25 providers.
DR DNASU; 213948; -.
DR Ensembl; ENSMUST00000059401; ENSMUSP00000051864; ENSMUSG00000038295.
DR GeneID; 213948; -.
DR KEGG; mmu:213948; -.
DR UCSC; uc033ihy.1; mouse.
DR CTD; 285973; -.
DR MGI; MGI:2685420; Atg9b.
DR VEuPathDB; HostDB:ENSMUSG00000038295; -.
DR eggNOG; KOG2173; Eukaryota.
DR GeneTree; ENSGT00390000014839; -.
DR HOGENOM; CLU_006200_2_0_1; -.
DR InParanoid; Q6EBV9; -.
DR OMA; PSHQCPQ; -.
DR OrthoDB; 712239at2759; -.
DR PhylomeDB; Q6EBV9; -.
DR TreeFam; TF313665; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 213948; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q6EBV9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6EBV9; protein.
DR Bgee; ENSMUSG00000038295; Expressed in lip and 100 other tissues.
DR Genevisible; Q6EBV9; MM.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Autophagy; Lipid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..922
FT /note="Autophagy-related protein 9B"
FT /id="PRO_0000314868"
FT TOPO_DOM 1..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..275
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 438..458
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 459..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..550
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 625..645
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 646..922
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 150..153
FT /note="Tyrosine-based sorting signal"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT COMPBIAS 85..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 29
FT /note="P -> H (in Ref. 1; AAS72555/AAS87214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 101913 MW; 3E79390541C3DB9D CRC64;
MVRRTGWGGS RRQRGRWGDL GPSSVPLLPM ALPLPASPCR GTGGRRISVF SLSPAPRTRS
CSSSVFPPAS GSPCLVIQEA GASQTPHNVL PTPTTPSTQA HPTMIHTSAS PSWGSHSTPP
LASATPPPSC PRPQDHPGLR MGPLIPEQDY ERLEDCDPEG SQDSPIHGED HQPLLHVPEG
LRGSWHHIQN LDSFFTKIYS YHQRNGFACI LLEDVFQLGQ FIFIVTFTTF LLRCVDYNVL
FNNQPKNHTR RGPLHSKVTL SDAILPSAQC AEKIHDSPLL VFLLVLAAGF WLFQLLRSVC
NLFSYWDIQV FYREALHIPP EELSSVPWAE VQSRLLELQR SGGLCVQPRP LTELDVHHRI
LRYTNYQVAL ANKGLLPARC PLPWGSSAAF LSRGLALNVD LLLFRGPFSL FRGGWELPEA
YKRSDLRGVL ANRWRRTVLL LAAVNLALSP LVLAWQVLHA FYSHVELLRR EPGAFGARRW
SRLARLQLRH FNELPHELRA RLGRAYRPAA AFLRAAEPPA PLRALLARQL VFFSGALFAA
LLVLTIYDED VLAVEHVLTT MTALGVTATV ARSFIPEEQC QGRSSQLLLQ AALAHMHYLP
EEPGATGARA SSYWQMAQLL QYRAVSLLEE LLSPLLTPLF LLFWFRPRAL EIIDFFHHFT
VDVAGVGDIC SFALMDVKRH GHPQWLSEGQ TEASLSQRAE DGKTELSLMR FSLAHPQWQP
PGHSSKFLGH LRGRVQQDAA AWGAPSTRSP PTPGVLSDCT SPLPEAFLAN LLVNPRPPQR
DLSPTAPCPA AATASLLASI SRMVQDPSCV SPGGTGGQKL TQLPELVSAE MSLHAIYLHQ
LHQQQQQELW GEASASSPSR PWSSPSQPGS PDEEKPSWSS DGSSPASSPR QQWGTQRAQN
LFPKGFQENT DTQKEPLTGP LH
