ATG9A_MOUSE
ID ATG9A_MOUSE Reviewed; 839 AA.
AC Q68FE2; Q3ZAQ4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Autophagy-related protein 9A {ECO:0000303|PubMed:27587839};
DE AltName: Full=APG9-like 1 {ECO:0000303|PubMed:15755735};
GN Name=Atg9a {ECO:0000303|PubMed:27587839, ECO:0000312|MGI:MGI:2138446};
GN Synonyms=Apg9l1 {ECO:0000303|PubMed:15755735};
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] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Botti J., Djavaheri-Mergny M., Codogno P., Oriol R.;
RT "Phylogeny and biochemistry of the autophagy protein beclin 1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION (ISOFORM 1), AND SUBCELLULAR LOCATION.
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19926846; DOI=10.1073/pnas.0911267106;
RA Saitoh T., Fujita N., Hayashi T., Takahara K., Satoh T., Lee H.,
RA Matsunaga K., Kageyama S., Omori H., Noda T., Yamamoto N., Kawai T.,
RA Ishii K., Takeuchi O., Yoshimori T., Akira S.;
RT "Atg9a controls dsDNA-driven dynamic translocation of STING and the innate
RT immune response.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20842-20846(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-18, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION.
RX PubMed=23402761; DOI=10.1016/j.bbrc.2013.02.010;
RA Chen D., Chen X., Li M., Zhang H., Ding W.X., Yin X.M.;
RT "CCCP-Induced LC3 lipidation depends on Atg9 whereas FIP200/Atg13 and
RT Beclin 1/Atg14 are dispensable.";
RL Biochem. Biophys. Res. Commun. 432:226-230(2013).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=26370455; DOI=10.1016/j.repbio.2015.05.001;
RA Kojima T., Yamada T., Akaishi R., Furuta I., Saitoh T., Nakabayashi K.,
RA Nakayama K.I., Nakayama K., Akira S., Minakami H.;
RT "Role of the Atg9a gene in intrauterine growth and survival of fetal
RT mice.";
RL Reprod. Biol. 15:131-138(2015).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 8-TYR--LEU-11 AND
RP 22-GLU--VAL-27.
RX PubMed=27587839; DOI=10.1242/jcs.196196;
RA Imai K., Hao F., Fujita N., Tsuji Y., Oe Y., Araki Y., Hamasaki M.,
RA Noda T., Yoshimori T.;
RT "Atg9A trafficking through the recycling endosomes is required for
RT autophagosome formation.";
RL J. Cell Sci. 129:3781-3791(2016).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27811852; DOI=10.1038/ncomms13391;
RA Imagawa Y., Saitoh T., Tsujimoto Y.;
RT "Vital staining for cell death identifies Atg9a-dependent necrosis in
RT developmental bone formation in mouse.";
RL Nat. Commun. 7:13391-13391(2016).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=28513333; DOI=10.1080/15548627.2017.1314897;
RA Yamaguchi J., Suzuki C., Nanao T., Kakuta S., Ozawa K., Tanida I.,
RA Saitoh T., Sunabori T., Komatsu M., Tanaka K., Aoki S., Sakimura K.,
RA Uchiyama Y.;
RT "Atg9a deficiency causes axon-specific lesions including neuronal circuit
RT dysgenesis.";
RL Autophagy 14:764-777(2018).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy by mediating
CC autophagosomal membrane expansion (PubMed:23402761, PubMed:27587839).
CC Cycles between the preautophagosomal structure/phagophore assembly site
CC (PAS) and the cytoplasmic vesicle pool and supplies membrane for the
CC growing autophagosome (By similarity). Lipid scramblase activity plays
CC a key role in preautophagosomal structure/phagophore assembly by
CC distributing the phospholipids that arrive through ATG2 (ATG2A or
CC ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer,
CC thereby driving autophagosomal membrane expansion (By similarity). Also
CC required to supply phosphatidylinositol 4-phosphate to the
CC autophagosome initiation site by recruiting the phosphatidylinositol 4-
CC kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1
CC (By similarity). In addition to autophagy, also plays a role in
CC necrotic cell death (PubMed:27811852). {ECO:0000250|UniProtKB:Q7Z3C6,
CC ECO:0000269|PubMed:23402761, ECO:0000269|PubMed:27587839,
CC ECO:0000269|PubMed:27811852}.
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 (By similarity). Interacts
CC (via cytoplasmic its C-terminus) with ATG2A (By similarity). Interacts
CC with SUPT20H (By similarity). Interacts (via the tyrosine-based sorting
CC signal motif) with AP4M1; promoting association with the AP-4 complex
CC (By similarity). Interacts with ARFIP1 and ARFIP2 (By similarity).
CC Interacts with ATG4A; the interaction is direct and promotes ATG9A
CC trafficking (By similarity). {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q7Z3C6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7Z3C6}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000269|PubMed:15755735}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7Z3C6}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:27587839}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7Z3C6}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q7Z3C6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7Z3C6}. Recycling endosome membrane
CC {ECO:0000269|PubMed:27587839}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7Z3C6}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q7Z3C6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7Z3C6}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q7Z3C6}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Mainly localizes to the trans-Golgi network (TGN)
CC and the endosomal system; cycles between them though vesicle
CC trafficking (PubMed:27587839). Export from the TGN to promote formation
CC of autophagosomes is mediated by the AP-4 complex. Under amino acid
CC starvation or rapamycin treatment, redistributes to preautophagosomal
CC structure/phagophore assembly site (PAS). The starvation-induced
CC redistribution depends on ULK1, ATG13, as well as SH3GLB1. Upon
CC autophagy induction, a portion of transiently localizes to the
CC autophagic membranes (By similarity). Recruited to damaged mitochondria
CC during mitophagy in a RIMOC1-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z3C6, ECO:0000269|PubMed:27587839}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68FE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68FE2-2; Sequence=VSP_061206, VSP_061207;
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 ATG9A-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 -!- DISRUPTION PHENOTYPE: Lethality; mice die within one day after birth
CC caused by impaired autophagy (PubMed:19926846). Mice also show aberrant
CC activation of the innate immune response (PubMed:19926846). Fetal mice
CC display significantly retarded growth (PubMed:26370455). Conditional
CC deletion in brain causes axon-specific degeneration: mice were born
CC normally, but half of them die within one week, and none live beyond 4
CC weeks of age (PubMed:28513333). Defects are caused by impaired
CC autophagy in neurons, leading to progressive degeneration in the axons
CC and their terminals, but not in neuronal cell bodies (PubMed:28513333).
CC In addition to defects in autophagy, mice also display impaired
CC necrotic cell death during bone morphogenesis: the bone surface is
CC rougher and bones are more porous due to defects in necrotic cell death
CC in bone surface formation (PubMed:27811852).
CC {ECO:0000269|PubMed:19926846, ECO:0000269|PubMed:26370455,
CC ECO:0000269|PubMed:27811852, ECO:0000269|PubMed:28513333}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
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DR EMBL; AM085510; CAJ30208.1; -; mRNA.
DR EMBL; BC079884; AAH79884.1; -; mRNA.
DR EMBL; BK004020; DAA05201.1; -; mRNA.
DR CCDS; CCDS35622.1; -. [Q68FE2-1]
DR RefSeq; NP_001003917.2; NM_001003917.4. [Q68FE2-1]
DR RefSeq; NP_001275541.1; NM_001288612.1. [Q68FE2-1]
DR RefSeq; XP_011236989.1; XM_011238687.2. [Q68FE2-1]
DR RefSeq; XP_011236990.1; XM_011238688.2. [Q68FE2-1]
DR AlphaFoldDB; Q68FE2; -.
DR SMR; Q68FE2; -.
DR BioGRID; 232841; 3.
DR IntAct; Q68FE2; 4.
DR MINT; Q68FE2; -.
DR STRING; 10090.ENSMUSP00000139608; -.
DR GlyGen; Q68FE2; 1 site.
DR iPTMnet; Q68FE2; -.
DR PhosphoSitePlus; Q68FE2; -.
DR SwissPalm; Q68FE2; -.
DR MaxQB; Q68FE2; -.
DR PaxDb; Q68FE2; -.
DR PeptideAtlas; Q68FE2; -.
DR PRIDE; Q68FE2; -.
DR ProteomicsDB; 277065; -.
DR ProteomicsDB; 332895; -.
DR DNASU; 245860; -.
DR Ensembl; ENSMUST00000040689; ENSMUSP00000047449; ENSMUSG00000033124. [Q68FE2-1]
DR Ensembl; ENSMUST00000188347; ENSMUSP00000139731; ENSMUSG00000033124. [Q68FE2-1]
DR Ensembl; ENSMUST00000189702; ENSMUSP00000139641; ENSMUSG00000033124. [Q68FE2-1]
DR Ensembl; ENSMUST00000239085; ENSMUSP00000159170; ENSMUSG00000033124. [Q68FE2-2]
DR GeneID; 245860; -.
DR KEGG; mmu:245860; -.
DR UCSC; uc007bob.2; mouse.
DR CTD; 79065; -.
DR MGI; MGI:2138446; Atg9a.
DR VEuPathDB; HostDB:ENSMUSG00000033124; -.
DR eggNOG; KOG2173; Eukaryota.
DR GeneTree; ENSGT00390000014839; -.
DR HOGENOM; CLU_006200_2_1_1; -.
DR InParanoid; Q68FE2; -.
DR OMA; MAHFETE; -.
DR OrthoDB; 712239at2759; -.
DR TreeFam; TF313665; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 245860; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Atg9a; mouse.
DR PRO; PR:Q68FE2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q68FE2; protein.
DR Bgee; ENSMUSG00000033124; Expressed in hindlimb stylopod muscle and 59 other tissues.
DR ExpressionAtlas; Q68FE2; baseline and differential.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; ISO:MGI.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0060349; P:bone morphogenesis; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:MGI.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:MGI.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IMP:UniProtKB.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:MGI.
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 Acetylation; Alternative splicing; Autophagy; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus;
KW Lipid transport; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT CHAIN 2..839
FT /note="Autophagy-related protein 9A"
FT /id="PRO_0000119821"
FT TOPO_DOM 2..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 85..128
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..154
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 155..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 291..301
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 302..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 320..328
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 329..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 372..397
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 398..406
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 407..424
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 425..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 471..480
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 481..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 484..492
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 493..839
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 657..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 8..11
FT /note="Tyrosine-based sorting signal"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT COMPBIAS 666..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 455..551
FT /note="NAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFR
FT NFTVEVVGVGDTCSFAQMDVRQHGHPQWLSGGQTEASVYQQAEDG -> VHLGGVAESH
FT RHTPHSHLLPPPSGPGDHRLLPQLYGRGRGCGRHLLLCSDGRSPAWPSSVAVWRADRGL
FT SVPASRGREDRVVAHALCHHQSRLAAPS (in isoform 2)"
FT /id="VSP_061206"
FT VAR_SEQ 552..839
FT /note="Missing (in isoform 2)"
FT /id="VSP_061207"
FT MUTAGEN 8..11
FT /note="YQRL->AAAA: Decreased localization to the Golgi
FT apparatus; when associated with 22-A--A-27."
FT /evidence="ECO:0000269|PubMed:27587839"
FT MUTAGEN 22..27
FT /note="EEDLLV->AAAAA: Decreased localization to the Golgi
FT apparatus; when associated with 8-A--A-11."
FT /evidence="ECO:0000269|PubMed:27587839"
SQ SEQUENCE 839 AA; 94425 MW; 1294E3B9231F1973 CRC64;
MAQFDTEYQR LEASYSDSPP GEEDLLVHVA EGSKSPWHHI ENLDLFFSRV YNLHQKNGFT
CMLIGEMFEL MQFLFVVAFT TFLVSCVDYD ILFANKMVNH SLHPTEPVKV TLPDAFLPAQ
VCSARIQENG SLITILVIAG VFWIHRLIKF IYNICCYWEI HSFYLHALRI PMSALPYCTW
QEVQARIVQT QKEHQICIHK RELTELDIYH RILRFQNYMV ALVNKSLLPL RFRLPGLGEV
VFFTRGLKYN FELILFWGPG SLFLNEWSLK AEYKRGGQRL ELAQRLSNRI LWIGIANFLL
CPLILIWQIL YAFFSYAEVL KREPGALGAR CWSLYGRCYL RHFNELEHEL QSRLNRGYKP
ASKYMNCFLS PLLTLLAKNG AFFAGSILAV LIALTIYDED VLAVEHVLTT VTLLGVTVTV
CRSFIPDQHM VFCPEQLLRV ILAHIHYMPD HWQGNAHRSQ TRDEFAQLFQ YKAVFILEEL
LSPIVTPLIL IFCLRPRALE IIDFFRNFTV EVVGVGDTCS FAQMDVRQHG HPQWLSGGQT
EASVYQQAED GKTELSLMHF AITNPGWQPP RESTAFLGFL KEQVQRDGAA AGLAQGGLLP
ENALFTSIQS LQSESEPLSL IANVVAGSSC RGPSLSRDLQ GSRHRADVAS ALRSFSPLQP
GAAPQGRVPS TMTGSGVDAR TASSGSSVWE GQLQSLVLSE YASTEMSLHA LYMHQLHKQQ
TQAEPERHVW HRRESDESGE SAPEEGGEGA RAPQPIPRSA SYPCATPRPG APETTALHGG
FQRRYGGITD PGTVPRGPSH FSRLPLGGWA EDGQPASRHP EPVPEEGSED ELPPQVHKV
