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 02-OCT-2024, entry version 128. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR RefSeq; XP_011236990.1; XM_011238688.2. DR AlphaFoldDB; Q68FE2; -. DR SMR; Q68FE2; -. DR BioGRID; 232841; 3. DR IntAct; Q68FE2; 4. DR MINT; Q68FE2; -. DR STRING; 10090.ENSMUSP00000139641; -. DR ChEMBL; CHEMBL4879478; -. DR GlyCosmos; Q68FE2; 1 site, No reported glycans. DR GlyGen; Q68FE2; 1 site. DR iPTMnet; Q68FE2; -. DR PhosphoSitePlus; Q68FE2; -. DR SwissPalm; Q68FE2; -. DR PaxDb; 10090-ENSMUSP00000139608; -. DR PeptideAtlas; Q68FE2; -. DR ProteomicsDB; 277065; -. DR ProteomicsDB; 332895; -. DR Pumba; Q68FE2; -. DR DNASU; 245860; -. DR Ensembl; ENSMUST00000040689.15; ENSMUSP00000047449.9; ENSMUSG00000033124.17. [Q68FE2-1] DR Ensembl; ENSMUST00000188347.7; ENSMUSP00000139731.2; ENSMUSG00000033124.17. [Q68FE2-1] DR Ensembl; ENSMUST00000189702.7; ENSMUSP00000139641.2; ENSMUSG00000033124.17. [Q68FE2-1] DR Ensembl; ENSMUST00000239085.2; ENSMUSP00000159170.2; ENSMUSG00000033124.17. [Q68FE2-2] DR GeneID; 245860; -. DR KEGG; mmu:245860; -. DR UCSC; uc007bob.2; mouse. DR AGR; MGI:2138446; -. 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; FLPPNEC; -. DR OrthoDB; 5481548at2759; -. DR TreeFam; TF313665; -. DR Reactome; R-MMU-1632852; Macroautophagy. DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy. DR BioGRID-ORCS; 245860; 26 hits in 80 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 60 other cell types or 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:0000139; C:Golgi membrane; IDA:UniProtKB. 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:0097060; C:synaptic membrane; IDA:SynGO. 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: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:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central. DR GO; GO:0097300; P:programmed 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 GO; GO:0061709; P:reticulophagy; IBA:GO_Central. DR InterPro; IPR007241; Autophagy-rel_prot_9. DR PANTHER; PTHR13038; APG9 AUTOPHAGY 9; 1. DR PANTHER; PTHR13038:SF13; AUTOPHAGY-RELATED PROTEIN 9A; 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 //