PACER_HUMAN
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 03-AUG-2022, entry version 139.
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},
GN KIAA0226L {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_001286761.1. [Q9H714-5]
DR RefSeq; NP_001273691.1; NM_001286762.1. [Q9H714-4]
DR RefSeq; NP_001273692.1; NM_001286763.1. [Q9H714-3]
DR RefSeq; NP_001273693.1; NM_001286764.1. [Q9H714-6]
DR RefSeq; NP_079389.2; NM_025113.3. [Q9H714-5]
DR AlphaFoldDB; Q9H714; -.
DR SMR; Q9H714; -.
DR BioGRID; 123162; 11.
DR IntAct; Q9H714; 9.
DR STRING; 9606.ENSP00000396935; -.
DR iPTMnet; Q9H714; -.
DR PhosphoSitePlus; Q9H714; -.
DR BioMuta; RUBCNL; -.
DR DMDM; 206729926; -.
DR jPOST; Q9H714; -.
DR MassIVE; Q9H714; -.
DR MaxQB; Q9H714; -.
DR PaxDb; Q9H714; -.
DR PeptideAtlas; Q9H714; -.
DR PRIDE; 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 22 providers.
DR DNASU; 80183; -.
DR Ensembl; ENST00000378784.8; ENSP00000368061.4; ENSG00000102445.20. [Q9H714-3]
DR Ensembl; ENST00000378787.7; ENSP00000368064.3; ENSG00000102445.20. [Q9H714-4]
DR Ensembl; ENST00000389908.7; ENSP00000374558.3; ENSG00000102445.20. [Q9H714-5]
DR Ensembl; ENST00000417405.2; ENSP00000402357.2; ENSG00000102445.20. [Q9H714-4]
DR Ensembl; ENST00000429979.6; ENSP00000396935.1; ENSG00000102445.20. [Q9H714-5]
DR Ensembl; ENST00000631139.2; ENSP00000485932.1; ENSG00000102445.20. [Q9H714-6]
DR Ensembl; ENST00000676051.1; ENSP00000501843.1; ENSG00000102445.20. [Q9H714-6]
DR Ensembl; ENST00000676114.1; ENSP00000502252.1; ENSG00000102445.20. [Q9H714-5]
DR Ensembl; ENST00000676307.1; ENSP00000502015.1; ENSG00000102445.20. [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 CTD; 80183; -.
DR DisGeNET; 80183; -.
DR GeneCards; RUBCNL; -.
DR HGNC; HGNC:20420; RUBCNL.
DR HPA; ENSG00000102445; Tissue enhanced (lymphoid).
DR neXtProt; NX_Q9H714; -.
DR OpenTargets; ENSG00000102445; -.
DR PharmGKB; PA134942431; -.
DR VEuPathDB; HostDB:ENSG00000102445; -.
DR eggNOG; KOG1829; Eukaryota.
DR GeneTree; ENSGT00940000160585; -.
DR InParanoid; Q9H714; -.
DR OMA; TSHVDGC; -.
DR OrthoDB; 177737at2759; -.
DR PhylomeDB; Q9H714; -.
DR TreeFam; TF317067; -.
DR PathwayCommons; Q9H714; -.
DR SignaLink; Q9H714; -.
DR BioGRID-ORCS; 80183; 12 hits in 1074 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 157 other tissues.
DR ExpressionAtlas; Q9H714; baseline and differential.
DR Genevisible; Q9H714; HS.
DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; IPR025258; Zf-RING_9.
DR Pfam; PF13901; zf-RING_9; 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 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 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
