ID   TMM59_MACFA             Reviewed;         323 AA.
AC   Q4R8C8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Transmembrane protein 59;
DE   Flags: Precursor;
GN   Name=TMEM59; ORFNames=QtsA-12783;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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}.
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; AB168526; BAE00644.1; -; mRNA.
DR   RefSeq; NP_001270198.1; NM_001283269.1.
DR   AlphaFoldDB; Q4R8C8; -.
DR   STRING; 9541.XP_005543351.1; -.
DR   GeneID; 101865500; -.
DR   CTD; 9528; -.
DR   eggNOG; ENOG502QUIS; Eukaryota.
DR   Proteomes; UP000233100; 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_0000282917"
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;  36197 MW;  3D998413233814B5 CRC64;
     MAAPKESLWV RTQLGLPPLL LLTMALAGGS GTASAEAFDS VLGDTASCHR ACQLTYPLHT
     YPKEEELYAC QRGCRLFSIC QFVDDGIDLN RTKLECESAC TEAYSQSDEQ YACHLGCQNQ
     LPFAELRQEQ LMSLMPKMHL LFPLTLVRSF WSDMMDSAQS FITSSWTFYL QADDGKIVIF
     QSKPEIQYAP HLEQESTNLR ESSLSKMSYL QMRNSQAHRN FLEDGESDGF LRCLSLNSGW
     ILTTTLVLSV MVLLWICCAT VATAVEQYVP SEKLSICGDL EFMNEQKLNK YPASSLVVVR
     SKTEDHEEAG PLPTKVNLAH SEI