ID   TMM59_PONAB             Reviewed;         323 AA.
AC   Q5R800;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Transmembrane protein 59;
DE   Flags: Precursor;
GN   Name=TMEM59;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a regulator of autophagy in response to S.aureus
CC       infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or
CC       MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a
CC       functional complex between LC3 and ATG16L1 and promoting LC3 lipidation
CC       and subsequent activation of autophagy. Modulates the O-glycosylation
CC       and complex N-glycosylation steps occurring during the Golgi maturation
CC       of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP
CC       transport to the cell surface and further shedding.
CC       {ECO:0000250|UniProtKB:Q9BXS4}.
CC   -!- SUBUNIT: Interacts with ATG16L1 (via WD repeats).
CC       {ECO:0000250|UniProtKB:Q9BXS4}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein
CC       {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9BXS4};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9BXS4}; Single-pass type I membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9BXS4};
CC       Single-pass type I membrane protein {ECO:0000255}. Note=Mainly
CC       localizes to late endosomes/lysosomes. Probably first exported to the
CC       cell surface and then actively endocytosed to transiently localize in
CC       early endosomes on its way to the late endosomal/lysosomal compartment
CC       where it becomes quickly degraded. {ECO:0000250|UniProtKB:Q9BXS4}.
CC   -!- DOMAIN: The ATG16L1-binding motif mediates interaction with ATG16L1 and
CC       promotes autophagy. {ECO:0000250|UniProtKB:Q9BXS4}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9BXS4}.
CC   -!- SIMILARITY: Belongs to the TMEM59 family. {ECO:0000305}.
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DR   EMBL; CR859956; CAH92110.1; -; mRNA.
DR   RefSeq; NP_001126232.1; NM_001132760.1.
DR   AlphaFoldDB; Q5R800; -.
DR   STRING; 9601.ENSPPYP00000001540; -.
DR   GeneID; 100173202; -.
DR   KEGG; pon:100173202; -.
DR   CTD; 9528; -.
DR   eggNOG; ENOG502QUIS; Eukaryota.
DR   InParanoid; Q5R800; -.
DR   OrthoDB; 1102891at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR   InterPro; IPR022065; Uncharacterised_TMEM59.
DR   PANTHER; PTHR28652; PTHR28652; 1.
DR   Pfam; PF12280; BSMAP; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cell membrane; Endosome; Glycoprotein; Golgi apparatus;
KW   Lysosome; Membrane; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..323
FT                   /note="Transmembrane protein 59"
FT                   /id="PRO_0000282919"
FT   TOPO_DOM        36..238
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..323
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           263..281
FT                   /note="ATG16L1-binding motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXS4"
FT   MOD_RES         303
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY73"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   323 AA;  36219 MW;  ADB8857680D5F436 CRC64;
     MAAPKGSLWV RTQLGLPPLL LLTMALAGGS GTASAEAFDS VLGDTASCHR ACQLTYPLHT
     YPKEEELYAC QRGCRLFSIC QFVDDGIDLN RTKLECESAC TEAYSQSDEQ YACHLGCQNQ
     LPFAELRQEQ LMSLMPKMHL LFPLTLVRSF WSDVMDSAQS FITSSWTFYL QADDGKIVIF
     QSKPEIQYAP HLEQEPTNLR ESSLSKMSYL QMRNSQVHRN FLEDGESDGF LRCLSLNSGW
     ILTTTLVLSV MVLLWICCAT VATAVEQYVP SEKLSIYGDL EFMNEQKLNR YPASSLVVVR
     SKTEDHEEAG PLPTKVNLAH SEI