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TGON3_RAT
ID   TGON3_RAT               Reviewed;         357 AA.
AC   P19814; Q4G0B6;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Trans-Golgi network integral membrane protein TGN38;
DE   Flags: Precursor;
GN   Name=Ttgn1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=2204342; DOI=10.1042/bj2700097;
RA   Luzio J.P., Brake B., Banting G., Howell K.E., Braghetta P., Stanley K.K.;
RT   "Identification, sequencing and expression of an integral membrane protein
RT   of the trans-Golgi network (TGN38).";
RL   Biochem. J. 270:97-102(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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   [3]
RP   PROTEIN SEQUENCE OF 119-125, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   INTERACTION WITH NEURABIN-1 AND NEURABIN-2, AND MUTAGENESIS.
RX   PubMed=10514494; DOI=10.1074/jbc.274.42.30080;
RA   Stephens D.J., Banting G.;
RT   "Direct interaction of the trans-Golgi network membrane protein, TGN38,
RT   with the F-actin binding protein, neurabin.";
RL   J. Biol. Chem. 274:30080-30086(1999).
RN   [5]
RP   METHYLATION AT ARG-74, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15047867; DOI=10.1091/mbc.e04-02-0101;
RA   Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
RA   Yates J.R. III, Howell K.E.;
RT   "Organellar proteomics reveals Golgi arginine dimethylation.";
RL   Mol. Biol. Cell 15:2907-2919(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-235 AND SER-271, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBUNIT: Interacts with neurabin-1 and neurabin-2. Binds preferentially
CC       to the dimeric form of neurabin-1. {ECO:0000269|PubMed:10514494}.
CC   -!- INTERACTION:
CC       P19814; P84092: Ap2m1; NbExp=4; IntAct=EBI-541446, EBI-297693;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
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DR   EMBL; X53565; CAA37637.1; -; mRNA.
DR   EMBL; BC098512; AAH98512.1; -; mRNA.
DR   RefSeq; NP_620195.1; NM_138840.2.
DR   PDB; 4IKN; X-ray; 1.85 A; B=348-353.
DR   PDBsum; 4IKN; -.
DR   AlphaFoldDB; P19814; -.
DR   SMR; P19814; -.
DR   BioGRID; 251332; 2.
DR   ELM; P19814; -.
DR   IntAct; P19814; 7.
DR   MINT; P19814; -.
DR   STRING; 10116.ENSRNOP00000019713; -.
DR   GlyGen; P19814; 4 sites.
DR   iPTMnet; P19814; -.
DR   PhosphoSitePlus; P19814; -.
DR   PaxDb; P19814; -.
DR   PRIDE; P19814; -.
DR   Ensembl; ENSRNOT00000019713; ENSRNOP00000019713; ENSRNOG00000014617.
DR   GeneID; 192152; -.
DR   KEGG; rno:192152; -.
DR   UCSC; RGD:620445; rat.
DR   CTD; 10618; -.
DR   RGD; 620445; Ttgn1.
DR   eggNOG; ENOG502S6YU; Eukaryota.
DR   GeneTree; ENSGT00530000064712; -.
DR   HOGENOM; CLU_047350_0_0_1; -.
DR   InParanoid; P19814; -.
DR   OMA; MWRSRRI; -.
DR   OrthoDB; 1324458at2759; -.
DR   PhylomeDB; P19814; -.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR   Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:P19814; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000014617; Expressed in colon and 19 other tissues.
DR   Genevisible; P19814; RN.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005768; C:endosome; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; TAS:RGD.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Glycoprotein; Golgi apparatus;
KW   Membrane; Methylation; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..357
FT                   /note="Trans-Golgi network integral membrane protein TGN38"
FT                   /id="PRO_0000022488"
FT   TOPO_DOM        18..303
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..357
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   REGION          20..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..180
FT                   /note="6 X 8 AA tandem repeats of [PT]-[TS]-G-[GVS]-D-[SN]-
FT                   [DN]-[NK]"
FT   COMPBIAS        20..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..259
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         74
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000269|PubMed:15047867"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         348
FT                   /note="S->A,D: Abolishes neurabin-1 and neurabin-2
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:10514494"
FT   MUTAGEN         350
FT                   /note="Y->A: No effect on neurabin-1 and neurabin-2
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:10514494"
FT   MUTAGEN         354..357
FT                   /note="Missing: No effect on neurabin-1 and neurabin-2
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:10514494"
SQ   SEQUENCE   357 AA;  38305 MW;  173B64C51CAD593B CRC64;
     MQFLVALLLL SVAVARALPS ASKPNNTSSE NNPPIQPSTP LPPGVDISQQ VKTNRPTDQR
     LESDKEGQDK TVARTSASVS SGVESATNLN LDDSKKHPET ADAKLKETLQ QLLPVDPKQE
     KSGQKFTKDS GSPTGGDSDN TTGGDSNKTT GVDSDKTSGG DSNKPTGSDN DKPTGGDSNK
     PTSKVPSNTE TPKIDKVQLT EKGQKPTLIS KTESGEKLAG DSDFSLKPEK GDKSSEPTED
     VETKEIEEGD TEPEEGSPLE EENEKVLGPS SSENQEGTLT DSMKDEKDDH YKDNSGNTSA
     ESSHFFAYLV TAAVLVAVLY IAYHNKRKII AFALEGKRSK VTRRPKASDY QRLNLKL
 
 
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