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Protein

Transmembrane protein 59

Gene

Tmem59

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy. Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP transport to the cell surface and further shedding.By similarity

GO - Molecular functioni

  • endopeptidase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Autophagy

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane protein 59
Alternative name(s):
Thymic dendritic cell-derived factor 1
Gene namesi
Name:Tmem59
Synonyms:ORF18, Tdcf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1929278. Tmem59.

Subcellular locationi

  • Late endosome membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Lysosome membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Cell membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Golgi apparatus membrane By similarity; Single-pass type I membrane protein Sequence analysis

  • Note: Mainly localizes to late endosomes/lysosomes. Probably first exported to the cell surface and then actively endocytosed to transiently localize in early endosomes on its way to the late endosomal/lysosomal compartment where it becomes quickly degraded.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 238203ExtracellularSequence analysisAdd
BLAST
Transmembranei239 – 25921HelicalSequence analysisAdd
BLAST
Topological domaini260 – 32364CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Golgi apparatus, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence analysisAdd
BLAST
Chaini36 – 323288Transmembrane protein 59PRO_0000003004Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence analysis
Modified residuei303 – 3031PhosphothreonineCombined sources

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9QY73.
MaxQBiQ9QY73.
PaxDbiQ9QY73.
PRIDEiQ9QY73.

PTM databases

iPTMnetiQ9QY73.
PhosphoSiteiQ9QY73.
SwissPalmiQ9QY73.

Expressioni

Gene expression databases

BgeeiQ9QY73.
CleanExiMM_TMEM59.
ExpressionAtlasiQ9QY73. baseline and differential.

Interactioni

Subunit structurei

Interacts with ATG16L1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030361.

Structurei

3D structure databases

ProteinModelPortaliQ9QY73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi263 – 28119ATG16L1-binding motifAdd
BLAST

Domaini

The ATG16L1-binding motif mediates interaction with ATG16L1 and promotes autophagy.By similarity

Sequence similaritiesi

Belongs to the TMEM59 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IIST. Eukaryota.
ENOG410XTCW. LUCA.
GeneTreeiENSGT00390000008279.
HOGENOMiHOG000015759.
HOVERGENiHBG018206.
InParanoidiQ9QY73.
OMAiYGDLEYM.
OrthoDBiEOG75TMCG.
PhylomeDBiQ9QY73.
TreeFamiTF331226.

Family and domain databases

InterProiIPR022065. Uncharacterised_TMEM59.
[Graphical view]
PfamiPF12280. BSMAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QY73-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPKGKLWV QAQLGLPPLL LLTMALAGGS GTAAAEAFDS VLGDTASCHR
60 70 80 90 100
ACQLTYPLHT YPKEEELYAC QRGCRLFSIC QFVDDGLDLN RTKLECESAC
110 120 130 140 150
TEAYSQPDEQ YACHLGCQDQ LPFAELRQEQ LMSLMPRMHL LFPLTLVRSF
160 170 180 190 200
WSDMMDSAQS FITSSWTFYL QADDGKIVIF QSKPEIQYAP QLEQEPTNLR
210 220 230 240 250
ESSLSKMSYL QMRNSQAHRN YLEEEESDGF LRCLSLNSGW ILTTTLVLSV
260 270 280 290 300
MVLLWICCAA VATAVEQYVP PEKLSIYGDL EFMNEQKLSR YPAPSLVIVR
310 320
SQTEEHEEAG PLPTKVNLAH SEI
Length:323
Mass (Da):36,314
Last modified:September 26, 2001 - v2
Checksum:i0E9BF6B6E07C7D96
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481C → V in AAF20283 (Ref. 1) Curated
Sequence conflicti103 – 1031A → T in AAF20283 (Ref. 1) Curated
Sequence conflicti121 – 1211L → W in AAF20283 (Ref. 1) Curated
Sequence conflicti139 – 1391H → Q in AAF20283 (Ref. 1) Curated
Sequence conflicti221 – 2222YL → DR in AAF20283 (Ref. 1) Curated
Sequence conflicti248 – 2481L → F in AAH45145 (PubMed:15489334).Curated
Sequence conflicti264 – 2641A → G in AAF20283 (Ref. 1) Curated
Sequence conflicti277 – 30024YGDLE…LVIVR → IGHFQFINQQNLTTYPPPPL LIVK in AAF20283 (Ref. 1) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF116911 mRNA. Translation: AAF20283.1.
AK003252 mRNA. Translation: BAB22668.2.
AK050162 mRNA. Translation: BAC34103.1.
AK145644 mRNA. Translation: BAE26561.1.
AK159761 mRNA. Translation: BAE35352.1.
AK166772 mRNA. Translation: BAE39008.1.
AK167058 mRNA. Translation: BAE39221.1.
BC002164 mRNA. Translation: AAH02164.1.
BC014732 mRNA. Translation: AAH14732.1.
BC018379 mRNA. Translation: AAH18379.1.
BC045145 mRNA. Translation: AAH45145.1.
BC058273 mRNA. Translation: AAH58273.1.
CCDSiCCDS18432.1.
RefSeqiNP_083841.4. NM_029565.3.
UniGeneiMm.291192.

Genome annotation databases

EnsembliENSMUST00000030361; ENSMUSP00000030361; ENSMUSG00000028618.
GeneIDi56374.
KEGGimmu:56374.
UCSCiuc008tzj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF116911 mRNA. Translation: AAF20283.1.
AK003252 mRNA. Translation: BAB22668.2.
AK050162 mRNA. Translation: BAC34103.1.
AK145644 mRNA. Translation: BAE26561.1.
AK159761 mRNA. Translation: BAE35352.1.
AK166772 mRNA. Translation: BAE39008.1.
AK167058 mRNA. Translation: BAE39221.1.
BC002164 mRNA. Translation: AAH02164.1.
BC014732 mRNA. Translation: AAH14732.1.
BC018379 mRNA. Translation: AAH18379.1.
BC045145 mRNA. Translation: AAH45145.1.
BC058273 mRNA. Translation: AAH58273.1.
CCDSiCCDS18432.1.
RefSeqiNP_083841.4. NM_029565.3.
UniGeneiMm.291192.

3D structure databases

ProteinModelPortaliQ9QY73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030361.

PTM databases

iPTMnetiQ9QY73.
PhosphoSiteiQ9QY73.
SwissPalmiQ9QY73.

Proteomic databases

EPDiQ9QY73.
MaxQBiQ9QY73.
PaxDbiQ9QY73.
PRIDEiQ9QY73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030361; ENSMUSP00000030361; ENSMUSG00000028618.
GeneIDi56374.
KEGGimmu:56374.
UCSCiuc008tzj.2. mouse.

Organism-specific databases

CTDi9528.
MGIiMGI:1929278. Tmem59.

Phylogenomic databases

eggNOGiENOG410IIST. Eukaryota.
ENOG410XTCW. LUCA.
GeneTreeiENSGT00390000008279.
HOGENOMiHOG000015759.
HOVERGENiHBG018206.
InParanoidiQ9QY73.
OMAiYGDLEYM.
OrthoDBiEOG75TMCG.
PhylomeDBiQ9QY73.
TreeFamiTF331226.

Miscellaneous databases

NextBioi312436.
PROiQ9QY73.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QY73.
CleanExiMM_TMEM59.
ExpressionAtlasiQ9QY73. baseline and differential.

Family and domain databases

InterProiIPR022065. Uncharacterised_TMEM59.
[Graphical view]
PfamiPF12280. BSMAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and molecular cloning of gene encoding a novel dendritic cell-derived factor."
    Jin C.G., Chen W.F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Thymus.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Colon, Eye, Kidney and Mammary gland.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 316-323, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart and Lung.

Entry informationi

Entry nameiTMM59_MOUSE
AccessioniPrimary (citable) accession number: Q9QY73
Secondary accession number(s): Q3TWB4, Q99LY8, Q9D1P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: March 16, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.