TMM59_MOUSE
ID TMM59_MOUSE Reviewed; 323 AA.
AC Q9QY73; Q3TWB4; Q99LY8; Q9D1P9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Transmembrane protein 59;
DE AltName: Full=Thymic dendritic cell-derived factor 1;
DE Flags: Precursor;
GN Name=Tmem59; Synonyms=ORF18, Tdcf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Jin C.G., Chen W.F.;
RT "Isolation and molecular cloning of gene encoding a novel dendritic cell-
RT derived factor.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, Eye, Kidney, and Mammary gland;
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 PROTEIN SEQUENCE OF 316-323, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AF116911; AAF20283.1; -; mRNA.
DR EMBL; AK003252; BAB22668.2; -; mRNA.
DR EMBL; AK050162; BAC34103.1; -; mRNA.
DR EMBL; AK145644; BAE26561.1; -; mRNA.
DR EMBL; AK159761; BAE35352.1; -; mRNA.
DR EMBL; AK166772; BAE39008.1; -; mRNA.
DR EMBL; AK167058; BAE39221.1; -; mRNA.
DR EMBL; BC002164; AAH02164.1; -; mRNA.
DR EMBL; BC014732; AAH14732.1; -; mRNA.
DR EMBL; BC018379; AAH18379.1; -; mRNA.
DR EMBL; BC045145; AAH45145.1; -; mRNA.
DR EMBL; BC058273; AAH58273.1; -; mRNA.
DR CCDS; CCDS18432.1; -.
DR RefSeq; NP_083841.4; NM_029565.3.
DR AlphaFoldDB; Q9QY73; -.
DR STRING; 10090.ENSMUSP00000030361; -.
DR GlyGen; Q9QY73; 1 site.
DR iPTMnet; Q9QY73; -.
DR PhosphoSitePlus; Q9QY73; -.
DR SwissPalm; Q9QY73; -.
DR EPD; Q9QY73; -.
DR MaxQB; Q9QY73; -.
DR PaxDb; Q9QY73; -.
DR PeptideAtlas; Q9QY73; -.
DR PRIDE; Q9QY73; -.
DR ProteomicsDB; 259430; -.
DR Antibodypedia; 46893; 99 antibodies from 28 providers.
DR DNASU; 56374; -.
DR Ensembl; ENSMUST00000030361; ENSMUSP00000030361; ENSMUSG00000028618.
DR GeneID; 56374; -.
DR KEGG; mmu:56374; -.
DR UCSC; uc008tzj.2; mouse.
DR CTD; 9528; -.
DR MGI; MGI:1929278; Tmem59.
DR VEuPathDB; HostDB:ENSMUSG00000028618; -.
DR eggNOG; ENOG502QUIS; Eukaryota.
DR GeneTree; ENSGT00390000008279; -.
DR HOGENOM; CLU_059747_1_0_1; -.
DR InParanoid; Q9QY73; -.
DR OMA; INSSWIL; -.
DR OrthoDB; 1102891at2759; -.
DR PhylomeDB; Q9QY73; -.
DR TreeFam; TF331226; -.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 56374; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Tmem59; mouse.
DR PRO; PR:Q9QY73; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9QY73; protein.
DR Bgee; ENSMUSG00000028618; Expressed in cortex of kidney and 152 other tissues.
DR ExpressionAtlas; Q9QY73; baseline and differential.
DR GO; GO:0000137; C:Golgi cis cisterna; ISO:MGI.
DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; ISO:MGI.
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:0004175; F:endopeptidase activity; IDA:MGI.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0010955; P:negative regulation of protein processing; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:Ensembl.
DR InterPro; IPR022065; Uncharacterised_TMEM59.
DR PANTHER; PTHR28652; PTHR28652; 1.
DR Pfam; PF12280; BSMAP; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cell membrane; Direct protein sequencing; Endosome;
KW Glycoprotein; Golgi apparatus; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..323
FT /note="Transmembrane protein 59"
FT /id="PRO_0000003004"
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:0007744|PubMed:21183079"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 48
FT /note="C -> V (in Ref. 1; AAF20283)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="A -> T (in Ref. 1; AAF20283)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="L -> W (in Ref. 1; AAF20283)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="H -> Q (in Ref. 1; AAF20283)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..222
FT /note="YL -> DR (in Ref. 1; AAF20283)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="L -> F (in Ref. 3; AAH45145)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> G (in Ref. 1; AAF20283)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..300
FT /note="YGDLEFMNEQKLSRYPAPSLVIVR -> IGHFQFINQQNLTTYPPPPLLIVK
FT (in Ref. 1; AAF20283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36314 MW; 0E9BF6B6E07C7D96 CRC64;
MAAPKGKLWV QAQLGLPPLL LLTMALAGGS GTAAAEAFDS VLGDTASCHR ACQLTYPLHT
YPKEEELYAC QRGCRLFSIC QFVDDGLDLN RTKLECESAC TEAYSQPDEQ YACHLGCQDQ
LPFAELRQEQ LMSLMPRMHL LFPLTLVRSF WSDMMDSAQS FITSSWTFYL QADDGKIVIF
QSKPEIQYAP QLEQEPTNLR ESSLSKMSYL QMRNSQAHRN YLEEEESDGF LRCLSLNSGW
ILTTTLVLSV MVLLWICCAA VATAVEQYVP PEKLSIYGDL EFMNEQKLSR YPAPSLVIVR
SQTEEHEEAG PLPTKVNLAH SEI
