TGON2_MOUSE
ID TGON2_MOUSE Reviewed; 363 AA.
AC Q62314;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Trans-Golgi network integral membrane protein 2 {ECO:0000305};
DE AltName: Full=TGN38B {ECO:0000303|PubMed:7540170};
DE Flags: Precursor;
GN Name=Tgoln2 {ECO:0000312|MGI:MGI:105079}; Synonyms=Ttgn2;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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: Not found in strains BALB/c, C57BL/6 and DBA/2.
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DR EMBL; D50032; BAA08758.1; -; mRNA.
DR PIR; A56940; A56940.
DR PIR; B56940; B56940.
DR RefSeq; NP_033470.1; NM_009444.1.
DR AlphaFoldDB; Q62314; -.
DR SMR; Q62314; -.
DR BioGRID; 204366; 2.
DR GlyGen; Q62314; 1 site.
DR iPTMnet; Q62314; -.
DR PhosphoSitePlus; Q62314; -.
DR jPOST; Q62314; -.
DR MaxQB; Q62314; -.
DR PRIDE; Q62314; -.
DR ProteomicsDB; 258868; -.
DR DNASU; 22135; -.
DR GeneID; 22135; -.
DR KEGG; mmu:22135; -.
DR UCSC; uc033isn.1; mouse.
DR CTD; 10618; -.
DR MGI; MGI:105079; Tgoln2.
DR InParanoid; Q62314; -.
DR PhylomeDB; Q62314; -.
DR BioGRID-ORCS; 22135; 1 hit in 16 CRISPR screens.
DR PRO; PR:Q62314; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62314; protein.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO: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; IDA:MGI.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..363
FT /note="Trans-Golgi network integral membrane protein 2"
FT /id="PRO_0000022487"
FT TOPO_DOM 18..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 133..140
FT /note="1"
FT REPEAT 141..148
FT /note="2"
FT REPEAT 149..156
FT /note="3"
FT REPEAT 157..164
FT /note="4"
FT REPEAT 165..172
FT /note="5"
FT REPEAT 173..180
FT /note="6"
FT REPEAT 181..188
FT /note="7"
FT REGION 23..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..188
FT /note="7 X 8 AA tandem repeats"
FT MOTIF 356..359
FT /note="Endocytosis signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 29..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43493"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43493"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43493"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 363 AA; 38821 MW; 2826FA9E958C5C27 CRC64;
MRFQVALLLL SVAVARALPP VYKRDADSGD SQNPPNQPSK QSSTPLPPES SNQVKTTRPT
DGQGQKSDKK DQDKTTLAAV SSKAESGPPT AATDHSLGDS RRQPEKTDAE LKETARPLSP
VNPKLEKSDQ SSTEDSGKPT GGNSGKPTGG DSGKPTGGDS DKPTEAGSNK ATEDDSGKST
KVDLDKPTSK IFPDTETSKT DKVQPTEKGQ KATLTSKTES GETLAGDSDF SLKPEKGDKS
SEPTEDVETK EIEEGDTEPE EGSPLEEENE KVSGPSSSEN QEGTLTDSMK NEKDDLYKDS
SGNTSAESSH FFAYLVTAAV LVAVLYIAYH NKRKIIAFAL EGKRSKVTRR PKASDYQRLN
LKL
