TMM59_BOVIN
ID TMM59_BOVIN Reviewed; 323 AA.
AC Q3T0Q2; F1MBR3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Transmembrane protein 59;
DE Flags: Precursor;
GN Name=TMEM59;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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}.
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DR EMBL; DAAA02008837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC102302; AAI02303.1; -; mRNA.
DR RefSeq; NP_001030248.1; NM_001035076.2.
DR AlphaFoldDB; Q3T0Q2; -.
DR STRING; 9913.ENSBTAP00000012534; -.
DR PaxDb; Q3T0Q2; -.
DR PRIDE; Q3T0Q2; -.
DR Ensembl; ENSBTAT00000012534; ENSBTAP00000012534; ENSBTAG00000009526.
DR GeneID; 509775; -.
DR KEGG; bta:509775; -.
DR CTD; 9528; -.
DR VEuPathDB; HostDB:ENSBTAG00000009526; -.
DR VGNC; VGNC:36099; TMEM59.
DR eggNOG; ENOG502QUIS; Eukaryota.
DR GeneTree; ENSGT00390000008279; -.
DR HOGENOM; CLU_059747_1_0_1; -.
DR InParanoid; Q3T0Q2; -.
DR OMA; INSSWIL; -.
DR OrthoDB; 1102891at2759; -.
DR TreeFam; TF331226; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000009526; Expressed in prostate gland and 105 other tissues.
DR ExpressionAtlas; Q3T0Q2; baseline and differential.
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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..323
FT /note="Transmembrane protein 59"
FT /id="PRO_0000282916"
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 CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 289
FT /note="N -> S (in Ref. 2; AAI02303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36065 MW; 122B28D4A265F61E CRC64;
MAVPKGSLWL RAQLGIPPLL LLAMALAGGS GTASAEAFDS VLGDTASCHR ACQLTYPLHT
YPKEEELYAC QRGCRLFSIC QFVDDGIDLN RTKLECESAC TEAYSQSDEQ YACHLGCQNQ
LPYAELRQEQ LMSLMPKMHL LFPLTLVRSF WSDMVDSAQS FITSSWTFYL QADDGKIVIF
QSKPEIQYAP QLEQEPTNLK DSSLSKMSYL QMRSSQAHRN YLEDGESDGF LRCLSLNSGW
ILTVTLVLSV MVLLWICCAT VATAVEQYVP SEKLSIYGDL EFMNEQKLNR YPASSLVVVR
SKAEDHEEAG PLPAKVNLAH SEI
