ID   PACER_HUMAN             Reviewed;         662 AA.
AC   Q9H714; A8KAG9; A8XR19; B3KS87; Q5W051; Q5W053; Q6PJ74; Q6PK94; Q86XH7;
AC   Q8N5J6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 3.
DT   28-JAN-2026, entry version 156.
DE   RecName: Full=Protein associated with UVRAG as autophagy enhancer {ECO:0000303|PubMed:28306502};
DE            Short=Pacer {ECO:0000303|PubMed:28306502};
DE   AltName: Full=Protein Rubicon-like {ECO:0000305};
GN   Name=RUBCNL {ECO:0000312|HGNC:HGNC:20420};
GN   Synonyms=C13orf18 {ECO:0000312|HGNC:HGNC:20420}, KIAA0226L
GN   {ECO:0000312|HGNC:HGNC:20420};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6), AND VARIANT
RP   ARG-152.
RC   TISSUE=Colon, Testis, and Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 234-662 (ISOFORMS 1/2), AND VARIANT ARG-152.
RC   TISSUE=B-cell, Leukocyte, and Skin;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [5]
RP   POSSIBLE FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23522960; DOI=10.1016/j.molonc.2013.02.017;
RA   Huisman C., Wisman G.B., Kazemier H.G., van Vugt M.A., van der Zee A.G.,
RA   Schuuring E., Rots M.G.;
RT   "Functional validation of putative tumor suppressor gene C13ORF18 in
RT   cervical cancer by artificial transcription factors.";
RL   Mol. Oncol. 7:669-679(2013).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UVRAG AND STX17,
RP   LIPID-BINDING, AND MUTAGENESIS OF 204-VAL--ASN-208.
RX   PubMed=28306502; DOI=10.1016/j.molcel.2017.02.010;
RA   Cheng X., Ma X., Ding X., Li L., Jiang X., Shen Z., Chen S., Liu W.,
RA   Gong W., Sun Q.;
RT   "Pacer mediates the function of class III PI3K and HOPS complexes in
RT   autophagosome maturation by engaging Stx17.";
RL   Mol. Cell 65:1029-1043(2017).
RN   [7]
RP   FUNCTION, INTERACTION WITH STX17, PHOSPHORYLATION AT SER-157, ACETYLATION
RP   AT LYS-483; LYS-523; LYS-533; LYS-573 AND LYS-633, AND MUTAGENESIS OF
RP   SER-157; LYS-483; LYS-523; LYS-533; LYS-573 AND LYS-633.
RX   PubMed=30704899; DOI=10.1016/j.molcel.2018.12.017;
RA   Cheng X., Ma X., Zhu Q., Song D., Ding X., Li L., Jiang X., Wang X.,
RA   Tian R., Su H., Shen Z., Chen S., Liu T., Gong W., Liu W., Sun Q.;
RT   "Pacer is a mediator of mTORC1 and GSK3-TIP60 signaling in regulation of
RT   autophagosome maturation and lipid metabolism.";
RL   Mol. Cell 73:1-15(2019).
CC   -!- FUNCTION: Regulator of autophagy that promotes autophagosome maturation
CC       by facilitating the biogenesis of phosphatidylinositol 3-phosphate
CC       (PtdIns(3)P) in late steps of autophagy (PubMed:28306502,
CC       PubMed:30704899). Acts by antagonizing RUBCN, thereby stimulating
CC       phosphatidylinositol 3-kinase activity of the PI3K/PI3KC3 complex
CC       (PubMed:28306502). Following anchorage to the autophagosomal SNARE
CC       STX17, promotes the recruitment of PI3K/PI3KC3 and HOPS complexes to
CC       the autophagosome to regulate the fusion specificity of autophagosomes
CC       with late endosomes/lysosomes (PubMed:28306502). Binds
CC       phosphoinositides phosphatidylinositol 3-phosphate (PtdIns(3)P), 4-
CC       phosphate (PtdIns(4)P) and 5-phosphate (PtdIns(5)P) (PubMed:28306502).
CC       In addition to its role in autophagy, acts as a regulator of lipid and
CC       glycogen homeostasis (By similarity). May act as a tumor suppressor
CC       (Probable). {ECO:0000250|UniProtKB:Q3TD16, ECO:0000269|PubMed:28306502,
CC       ECO:0000269|PubMed:30704899, ECO:0000305|PubMed:23522960}.
CC   -!- SUBUNIT: Interacts with UVRAG; the interaction is direct and promotes
CC       association with the PI3K/PI3KC3 and HOPS complexes (PubMed:28306502).
CC       Interacts with STX17 (PubMed:28306502, PubMed:30704899).
CC       {ECO:0000269|PubMed:28306502, ECO:0000269|PubMed:30704899}.
CC   -!- INTERACTION:
CC       Q9H714-3; Q14457: BECN1; NbExp=3; IntAct=EBI-9088146, EBI-949378;
CC       Q9H714-3; Q96T51-2: RUFY1; NbExp=2; IntAct=EBI-9088146, EBI-12192715;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC       {ECO:0000269|PubMed:28306502}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:28306502}. Note=Associates with late autophagic
CC       structure (PubMed:28306502). Recruitment to autophagosome membrane is
CC       promoted by autophagic stimuli (PubMed:28306502).
CC       {ECO:0000269|PubMed:28306502}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q9H714-5; Sequence=Displayed;
CC       Name=5;
CC         IsoId=Q9H714-4; Sequence=VSP_014713;
CC       Name=2;
CC         IsoId=Q9H714-3; Sequence=VSP_014708;
CC       Name=3;
CC         IsoId=Q9H714-1; Sequence=VSP_014711, VSP_014712;
CC       Name=4;
CC         IsoId=Q9H714-2; Sequence=VSP_014709, VSP_014710;
CC       Name=6;
CC         IsoId=Q9H714-6; Sequence=VSP_055260;
CC   -!- TISSUE SPECIFICITY: Expressed weakly in cervical carcinoma cell lines.
CC       {ECO:0000269|PubMed:23522960}.
CC   -!- INDUCTION: Up-regulated by epigenetic drugs, such as azacitidine, and
CC       artificial transcription factors (ATFs)-induced treatments in cervical
CC       carcinoma cell lines. {ECO:0000269|PubMed:23522960}.
CC   -!- PTM: Phosphorylated by MTOR at Ser-157 under nutrient-rich conditions
CC       (PubMed:30704899). Phosphorylation prevents acetylation by KAT5/TIP60
CC       and impairs RUBCNL/PACER function and autophagosome maturation
CC       (PubMed:30704899). Under autophagy induction, Phosphorylation by MTOR
CC       is repressed, enabling acetylation by KAT5/TIP60 (PubMed:30704899).
CC       {ECO:0000269|PubMed:30704899}.
CC   -!- PTM: Acetylated by KAT5/TIP60 under autophagy induction, promoting
CC       autophagosome maturation and lipid metabolism (PubMed:30704899).
CC       Acetylation is prevented by phosphorylation by MTOR (PubMed:30704899).
CC       Lys-483 and Lys-573 constitute the key sites for tuning function in
CC       autophagy (PubMed:30704899). {ECO:0000269|PubMed:30704899}.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
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DR   EMBL; AK025215; BAB15086.1; -; mRNA.
DR   EMBL; AK093073; BAG52649.1; -; mRNA.
DR   EMBL; AK293034; BAF85723.1; -; mRNA.
DR   EMBL; AL139801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004495; AAH04495.1; -; mRNA.
DR   EMBL; BC021097; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC032311; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC043488; AAH43488.1; -; mRNA.
DR   CCDS; CCDS31970.2; -. [Q9H714-5]
DR   CCDS; CCDS66542.1; -. [Q9H714-6]
DR   CCDS; CCDS66543.1; -. [Q9H714-4]
DR   CCDS; CCDS66545.1; -. [Q9H714-3]
DR   RefSeq; NP_001273690.1; NM_001286761.2. [Q9H714-5]
DR   RefSeq; NP_001273691.1; NM_001286762.3. [Q9H714-4]
DR   RefSeq; NP_001273692.1; NM_001286763.3. [Q9H714-3]
DR   RefSeq; NP_001273693.1; NM_001286764.3. [Q9H714-6]
DR   RefSeq; NP_001336701.1; NM_001349772.2. [Q9H714-5]
DR   RefSeq; NP_079389.2; NM_025113.5. [Q9H714-5]
DR   AlphaFoldDB; Q9H714; -.
DR   SMR; Q9H714; -.
DR   BioGRID; 123162; 11.
DR   FunCoup; Q9H714; 564.
DR   IntAct; Q9H714; 10.
DR   STRING; 9606.ENSP00000396935; -.
DR   iPTMnet; Q9H714; -.
DR   PhosphoSitePlus; Q9H714; -.
DR   BioMuta; RUBCNL; -.
DR   DMDM; 206729926; -.
DR   jPOST; Q9H714; -.
DR   MassIVE; Q9H714; -.
DR   PaxDb; 9606-ENSP00000396935; -.
DR   PeptideAtlas; Q9H714; -.
DR   ProteomicsDB; 1901; -.
DR   ProteomicsDB; 81072; -. [Q9H714-5]
DR   ProteomicsDB; 81073; -. [Q9H714-1]
DR   ProteomicsDB; 81074; -. [Q9H714-2]
DR   ProteomicsDB; 81075; -. [Q9H714-3]
DR   ProteomicsDB; 81076; -. [Q9H714-4]
DR   Antibodypedia; 23706; 147 antibodies from 20 providers.
DR   DNASU; 80183; -.
DR   Ensembl; ENST00000378784.8; ENSP00000368061.4; ENSG00000102445.21. [Q9H714-3]
DR   Ensembl; ENST00000378787.7; ENSP00000368064.3; ENSG00000102445.21. [Q9H714-4]
DR   Ensembl; ENST00000389908.7; ENSP00000374558.3; ENSG00000102445.21. [Q9H714-5]
DR   Ensembl; ENST00000417405.2; ENSP00000402357.2; ENSG00000102445.21. [Q9H714-4]
DR   Ensembl; ENST00000429979.6; ENSP00000396935.1; ENSG00000102445.21. [Q9H714-5]
DR   Ensembl; ENST00000631139.2; ENSP00000485932.1; ENSG00000102445.21. [Q9H714-6]
DR   Ensembl; ENST00000676051.1; ENSP00000501843.1; ENSG00000102445.21. [Q9H714-6]
DR   Ensembl; ENST00000676114.1; ENSP00000502252.1; ENSG00000102445.21. [Q9H714-5]
DR   Ensembl; ENST00000676307.1; ENSP00000502015.1; ENSG00000102445.21. [Q9H714-5]
DR   GeneID; 80183; -.
DR   KEGG; hsa:80183; -.
DR   MANE-Select; ENST00000429979.6; ENSP00000396935.1; NM_025113.5; NP_079389.2.
DR   UCSC; uc001vbe.6; human. [Q9H714-5]
DR   AGR; HGNC:20420; -.
DR   ClinPGx; PA134942431; -.
DR   CTD; 80183; -.
DR   DisGeNET; 80183; -.
DR   GeneCards; RUBCNL; -.
DR   HGNC; HGNC:20420; RUBCNL.
DR   HPA; ENSG00000102445; Tissue enhanced (lymphoid).
DR   MIM; 620175; gene.
DR   OpenTargets; ENSG00000102445; -.
DR   VEuPathDB; HostDB:ENSG00000102445; -.
DR   eggNOG; KOG1829; Eukaryota.
DR   GeneTree; ENSGT00940000160585; -.
DR   InParanoid; Q9H714; -.
DR   OMA; ILTMWDF; -.
DR   OrthoDB; 10067503at2759; -.
DR   PAN-GO; Q9H714; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9H714; -.
DR   PathwayCommons; Q9H714; -.
DR   SignaLink; Q9H714; -.
DR   SIGNOR; Q9H714; -.
DR   Agora; ENSG00000102445; -.
DR   BioGRID-ORCS; 80183; 12 hits in 1152 CRISPR screens.
DR   ChiTaRS; RUBCNL; human.
DR   GenomeRNAi; 80183; -.
DR   Pharos; Q9H714; Tbio.
DR   PRO; PR:Q9H714; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q9H714; protein.
DR   Bgee; ENSG00000102445; Expressed in periodontal ligament and 159 other cell types or tissues.
DR   ExpressionAtlas; Q9H714; baseline and differential.
DR   GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
DR   GO; GO:0097352; P:autophagosome maturation; IDA:UniProtKB.
DR   GO; GO:0061910; P:autophagosome-endosome fusion; IDA:UniProtKB.
DR   GO; GO:0061909; P:autophagosome-lysosome fusion; IDA:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0070873; P:regulation of glycogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR   InterPro; IPR052428; Autophagy_HostDef_Reg.
DR   InterPro; IPR025258; RH_dom.
DR   InterPro; IPR048569; RUBC_PIKBD.
DR   PANTHER; PTHR45971; PHOX (PX) DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45971:SF2; PROTEIN ASSOCIATED WITH UVRAG AS AUTOPHAGY ENHANCER; 1.
DR   Pfam; PF13901; RH_dom; 1.
DR   Pfam; PF21054; RUBC_PIKBD; 1.
DR   SMART; SM01175; DUF4206; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Autophagy; Cytoplasmic vesicle;
KW   Lipid metabolism; Lipid-binding; Membrane; Phosphoprotein;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..662
FT                   /note="Protein associated with UVRAG as autophagy enhancer"
FT                   /id="PRO_0000089880"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..235
FT                   /note="Interaction with UVRAG"
FT                   /evidence="ECO:0000269|PubMed:28306502"
FT   COMPBIAS        58..71
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..131
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         157
FT                   /note="Phosphoserine; by MTOR"
FT                   /evidence="ECO:0000269|PubMed:30704899"
FT   MOD_RES         483
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:30704899"
FT   MOD_RES         523
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:30704899"
FT   MOD_RES         533
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:30704899"
FT   MOD_RES         573
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:30704899"
FT   MOD_RES         633
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:30704899"
FT   VAR_SEQ         1..135
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055260"
FT   VAR_SEQ         1..88
FT                   /note="MVSQSTVRQDSPVEPWEGISDHSGIIDGSPRLLNTDHPPCQLDIRLMRHKAV
FT                   WINPQDVQQQPQDLQSQVPAAGNSGTHFVTDAASPS -> MVSNHYFLLCVNLPLREIH
FT                   TP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014708"
FT   VAR_SEQ         136..147
FT                   /note="MVRPGYSHRVSL -> KACMRKPRSWTE (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014709"
FT   VAR_SEQ         148..662
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014710"
FT   VAR_SEQ         309..321
FT                   /note="ELGDFNDITETCS -> VSLMSQTSILQNY (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014711"
FT   VAR_SEQ         322..662
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014712"
FT   VAR_SEQ         545..662
FT                   /note="ALKEFEQVPGHLTDELHLFSLEDLVRIKKGLLAPLLKDILKASLAHVAGCEL
FT                   CQGKGFICEFCQNTTVIFPFQTATCRRCSACRACFHKQCFQSSECPRCARITARRKLLE
FT                   SVASAAT -> CVKERALFVNFARIRLSSSHFRQQHVEDVQRAGLAFTNSASSPPSAPG
FT                   VRGSQRGENFWKVWPLQQHDAPEYCEKDCSTCLMITPICVYYW (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_014713"
FT   VARIANT         152
FT                   /note="G -> R (in dbSNP:rs1408184)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_022912"
FT   MUTAGEN         157
FT                   /note="S->A: Abolished phosphorylation by MTOR, leading to
FT                   promote interaction with STX17 and autophagosome
FT                   maturation."
FT                   /evidence="ECO:0000269|PubMed:30704899"
FT   MUTAGEN         157
FT                   /note="S->D: Phosphomimetic mutant; impaired interaction
FT                   with STX17 and abolished ability to promote autophagosome
FT                   maturation."
FT                   /evidence="ECO:0000269|PubMed:30704899"
FT   MUTAGEN         204..208
FT                   /note="VEKEN->AAAAA: Abolishes interaction with UVRAG."
FT                   /evidence="ECO:0000269|PubMed:28306502"
FT   MUTAGEN         483
FT                   /note="K->R: Abolished acetylation by KAT5/TIP60 and
FT                   abolished ability to promote autophagosome maturation; when
FT                   associated with R-523, R-533, R-573 and R-633."
FT   MUTAGEN         523
FT                   /note="K->R: Abolished acetylation by KAT5/TIP60 and
FT                   abolished ability to promote autophagosome maturation; when
FT                   associated with R-483, R-533, R-573 and R-633."
FT   MUTAGEN         533
FT                   /note="K->R: Abolished acetylation by KAT5/TIP60 and
FT                   abolished ability to promote autophagosome maturation; when
FT                   associated with R-483, R-523, R-573 and R-633."
FT   MUTAGEN         573
FT                   /note="K->R: Abolished acetylation by KAT5/TIP60 and
FT                   abolished ability to promote autophagosome maturation; when
FT                   associated with R-483, R-523, R-533 and R-633."
FT   MUTAGEN         633
FT                   /note="K->R: Abolished acetylation by KAT5/TIP60 and
FT                   abolished ability to promote autophagosome maturation; when
FT                   associated with R-483, R-523, R-533 and R-573."
FT   CONFLICT        234..236
FT                   /note="TES -> ARG (in Ref. 3; AAH04495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        469
FT                   /note="S -> P (in Ref. 1; BAG52649)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        549
FT                   /note="F -> L (in Ref. 1; BAG52649)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   662 AA;  73457 MW;  0AAA3C0F76CDAED8 CRC64;
     MVSQSTVRQD SPVEPWEGIS DHSGIIDGSP RLLNTDHPPC QLDIRLMRHK AVWINPQDVQ
     QQPQDLQSQV PAAGNSGTHF VTDAASPSGP SPSCLGDSLA ETTLSEDTTD SVGSASPHGS
     SEKSSSFSLS STEVHMVRPG YSHRVSLPTS PGILATSPYP ETDSAFFEPS HLTSAADEGA
     VQVSRRTISS NSFSPEVFVL PVDVEKENAH FYVADMIISA MEKMKCNILS QQQTESWSKE
     VSGLLGSDQP DSEMTFDTNI KQESGSSTSS YSGYEGCAVL QVSPVTETRT YHDVKEICKC
     DVDEFVILEL GDFNDITETC SCSCSSSKSV TYEPDFNSAE LLAKELYRVF QKCWILSVVN
     SQLAGSLSAA GSIVVNEECV RKDFESSMNV VQEIKFKSRI RGTEDWAPPR FQIIFNIHPP
     LKRDLVVAAQ NFFCAGCGTP VEPKFVKRLR YCEYLGKYFC DCCHSYAESC IPARILMMWD
     FKKYYVSNFS KQLLDSIWHQ PIFNLLSIGQ SLYAKAKELD RVKEIQEQLF HIKKLLKTCR
     FANSALKEFE QVPGHLTDEL HLFSLEDLVR IKKGLLAPLL KDILKASLAH VAGCELCQGK
     GFICEFCQNT TVIFPFQTAT CRRCSACRAC FHKQCFQSSE CPRCARITAR RKLLESVASA
     AT
//