TGON1_MOUSE
ID TGON1_MOUSE Reviewed; 353 AA.
AC Q62313;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Trans-Golgi network integral membrane protein 1;
DE AltName: Full=TGN38A;
DE Flags: Precursor;
GN Name=Tgoln1; Synonyms=Ttgn1;
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=ICR; TISSUE=Brain;
RX PubMed=7540170; DOI=10.1074/jbc.270.24.14471;
RA Kasai K., Takahashi S., Murakami K., Nakayama K.;
RT "Strain-specific presence of two TGN38 isoforms and absence of TGN41 in
RT mouse.";
RL J. Biol. Chem. 270:14471-14476(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Testis;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
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: May be involved in regulating membrane traffic to and from
CC trans-Golgi network.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Note=Primarily in trans-Golgi network. Cycles between
CC the trans-Golgi network and the cell surface returning via endosomes
CC (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- MISCELLANEOUS: Also found in strains BALB/c, C57BL/6 and DBA/2.
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DR EMBL; D50031; BAA08757.1; -; mRNA.
DR EMBL; AK041302; BAC30896.1; -; mRNA.
DR EMBL; AK076586; BAC36404.1; -; mRNA.
DR EMBL; BC009143; AAH09143.1; -; mRNA.
DR CCDS; CCDS51811.1; -.
DR PIR; B56940; B56940.
DR RefSeq; NP_033469.1; NM_009443.3.
DR AlphaFoldDB; Q62313; -.
DR SMR; Q62313; -.
DR IntAct; Q62313; 1.
DR STRING; 10090.ENSMUSP00000068487; -.
DR GlyConnect; 2778; 1 N-Linked glycan (1 site).
DR GlyGen; Q62313; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q62313; -.
DR PhosphoSitePlus; Q62313; -.
DR EPD; Q62313; -.
DR jPOST; Q62313; -.
DR MaxQB; Q62313; -.
DR PaxDb; Q62313; -.
DR PRIDE; Q62313; -.
DR ProteomicsDB; 263170; -.
DR Antibodypedia; 2516; 335 antibodies from 33 providers.
DR DNASU; 22134; -.
DR Ensembl; ENSMUST00000070524; ENSMUSP00000068487; ENSMUSG00000056429.
DR GeneID; 22134; -.
DR KEGG; mmu:22134; -.
DR CTD; 22134; -.
DR MGI; MGI:105080; Tgoln1.
DR VEuPathDB; HostDB:ENSMUSG00000056429; -.
DR eggNOG; ENOG502S6YU; Eukaryota.
DR GeneTree; ENSGT00530000064712; -.
DR HOGENOM; CLU_047350_0_0_1; -.
DR InParanoid; Q62313; -.
DR OMA; MWRSRRI; -.
DR OrthoDB; 1324458at2759; -.
DR PhylomeDB; Q62313; -.
DR TreeFam; TF332514; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 22134; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tgoln1; mouse.
DR PRO; PR:Q62313; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q62313; protein.
DR Bgee; ENSMUSG00000056429; Expressed in left colon and 254 other tissues.
DR ExpressionAtlas; Q62313; baseline and differential.
DR Genevisible; Q62313; MM.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Golgi apparatus; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..353
FT /note="Trans-Golgi network integral membrane protein 1"
FT /id="PRO_0000022485"
FT TOPO_DOM 18..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 131..138
FT /note="1"
FT REPEAT 139..146
FT /note="2"
FT REPEAT 147..154
FT /note="3"
FT REPEAT 155..162
FT /note="4"
FT REPEAT 163..170
FT /note="5"
FT REPEAT 171..178
FT /note="6"
FT REGION 23..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..178
FT /note="6 X 8 AA tandem repeats"
FT MOTIF 346..349
FT /note="Endocytosis signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 26..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 353 AA; 37848 MW; 95C340C2F4A21EB3 CRC64;
MRFQVALLLL SVAVARALPS VYKRDADSGD SQNPPNQPSK QSSTPLPSSN QVKTTRPTDG
QGQKSDKKDQ DKTTLAAVSS KAESGPRTAA TDHSLGDSRR QPEKTDAELN ETARPLSPVN
PKLEKSDQSS TEDSGKPTGG NSGKPTGGDS GKPTEAGSNK ATEDDSGKST KVDLDKPTSK
ISPDTETSKT DKVQPTEKGQ KPTLTSKTES GETLAGDSDF SLKPEKGDKS SEPTEDVETK
EIEEGDTEPE EGSPLEEENE KVPGPSSSEN QEGTLTDSMK NEKDDLYKDS SGNTSAESSH
FFAYLVTAAV LVAVLYIAYH NKRKIIAFAL EGKRSKVTRR PKASDYQRLN LKL
