TPPC3_MOUSE
ID TPPC3_MOUSE Reviewed; 180 AA.
AC O55013;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Trafficking protein particle complex subunit 3;
DE AltName: Full=BET3 homolog;
GN Name=Trappc3 {ECO:0000312|MGI:MGI:1351486};
GN Synonyms=Bet3 {ECO:0000250|UniProtKB:O43617};
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].
RA Eva L., Subramaniam V.N., Hong W.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16828797; DOI=10.1016/j.jmb.2006.06.012;
RA Kummel D., Muller J.J., Roske Y., Henke N., Heinemann U.;
RT "Structure of the Bet3-Tpc6B core of TRAPP: two Tpc6 paralogs form trimeric
RT complexes with Bet3 and Mum2.";
RL J. Mol. Biol. 361:22-32(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, AND PALMITOYLATION AT
RP CYS-68.
RX PubMed=15608655; DOI=10.1038/nsmb871;
RA Kim Y.-G., Sohn E.J., Seo J., Lee K.-J., Lee H.-S., Hwang I., Whiteway M.,
RA Sacher M., Oh B.-H.;
RT "Crystal structure of bet3 reveals a novel mechanism for Golgi localization
RT of tethering factor TRAPP.";
RL Nat. Struct. Mol. Biol. 12:38-45(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of Bet3 homolog (13277653) from Mus musculus at 2.10 A
RT resolution.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC reticulum to Golgi.
CC -!- SUBUNIT: Homodimer. Component of the multisubunit transport protein
CC particle (TRAPP) complex, which includes at least TRAPPC2, TRAPPC2L,
CC TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10,
CC TRAPPC11 and TRAPPC12. Heterodimer with TRAPPC6A. The heterodimer
CC TRAPPC3-TRAPPC6A interacts with TRAPPC2L. Heterodimer with TRAPPC6b.
CC The heterodimer TRAPPC6B-TRAPPC3 interacts with TRAPPC1 likely
CC providing a core for TRAPP complex formation.
CC {ECO:0000250|UniProtKB:O43617}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in lung, heart, liver,
CC spleen, brain and kidney. {ECO:0000269|PubMed:16828797}.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF041433; AAB96937.1; -; mRNA.
DR EMBL; BC003736; AAH03736.1; -; mRNA.
DR CCDS; CCDS18647.1; -.
DR RefSeq; NP_038746.1; NM_013718.2.
DR PDB; 1WC8; X-ray; 1.90 A; A=1-180.
DR PDB; 1WC9; X-ray; 1.60 A; A=8-172.
DR PDB; 2J3R; X-ray; 2.60 A; A=1-180.
DR PDB; 2J3T; X-ray; 2.40 A; A=1-180.
DR PDB; 2J3W; X-ray; 2.10 A; D/E=1-180.
DR PDB; 2PWN; X-ray; 2.04 A; A=1-180.
DR PDBsum; 1WC8; -.
DR PDBsum; 1WC9; -.
DR PDBsum; 2J3R; -.
DR PDBsum; 2J3T; -.
DR PDBsum; 2J3W; -.
DR PDBsum; 2PWN; -.
DR AlphaFoldDB; O55013; -.
DR SMR; O55013; -.
DR BioGRID; 205122; 9.
DR ComplexPortal; CPX-4764; TRAPP II complex.
DR ComplexPortal; CPX-4766; TRAPP III complex.
DR IntAct; O55013; 6.
DR MINT; O55013; -.
DR STRING; 10090.ENSMUSP00000030660; -.
DR iPTMnet; O55013; -.
DR PhosphoSitePlus; O55013; -.
DR SwissPalm; O55013; -.
DR REPRODUCTION-2DPAGE; O55013; -.
DR UCD-2DPAGE; O55013; -.
DR EPD; O55013; -.
DR PaxDb; O55013; -.
DR PeptideAtlas; O55013; -.
DR PRIDE; O55013; -.
DR ProteomicsDB; 260731; -.
DR TopDownProteomics; O55013; -.
DR Antibodypedia; 31641; 224 antibodies from 28 providers.
DR DNASU; 27096; -.
DR Ensembl; ENSMUST00000030660; ENSMUSP00000030660; ENSMUSG00000028847.
DR GeneID; 27096; -.
DR KEGG; mmu:27096; -.
DR UCSC; uc008utc.1; mouse.
DR CTD; 27095; -.
DR MGI; MGI:1351486; Trappc3.
DR VEuPathDB; HostDB:ENSMUSG00000028847; -.
DR eggNOG; KOG3330; Eukaryota.
DR GeneTree; ENSGT00390000003880; -.
DR HOGENOM; CLU_087110_0_0_1; -.
DR InParanoid; O55013; -.
DR OMA; WTSDNKQ; -.
DR OrthoDB; 1334804at2759; -.
DR PhylomeDB; O55013; -.
DR TreeFam; TF300091; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 27096; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Trappc3; mouse.
DR EvolutionaryTrace; O55013; -.
DR PRO; PR:O55013; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O55013; protein.
DR Bgee; ENSMUSG00000028847; Expressed in vault of skull and 264 other tissues.
DR ExpressionAtlas; O55013; baseline and differential.
DR Genevisible; O55013; MM.
DR GO; GO:0033106; C:cis-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0030008; C:TRAPP complex; IDA:MGI.
DR GO; GO:1990071; C:TRAPPII protein complex; IC:ComplexPortal.
DR GO; GO:1990072; C:TRAPPIII protein complex; IC:ComplexPortal.
DR GO; GO:0048208; P:COPII vesicle coating; IC:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:MGI.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006901; P:vesicle coating; IC:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR CDD; cd14942; TRAPPC3_bet3; 1.
DR InterPro; IPR016721; Bet3.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR007194; TRAPP_component.
DR PANTHER; PTHR13048; PTHR13048; 1.
DR Pfam; PF04051; TRAPP; 1.
DR PIRSF; PIRSF018293; TRAPP_I_complex_Bet3; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Lipoprotein; Palmitate; Reference proteome; Transport.
FT CHAIN 1..180
FT /note="Trafficking protein particle complex subunit 3"
FT /id="PRO_0000211573"
FT LIPID 68
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:15608655"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2J3R"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:1WC9"
FT HELIX 37..61
FT /evidence="ECO:0007829|PDB:1WC9"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:1WC9"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:1WC9"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1WC9"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2J3R"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1WC9"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1WC9"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2J3W"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1WC9"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:1WC9"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1WC9"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:1WC9"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1WC9"
FT STRAND 159..170
FT /evidence="ECO:0007829|PDB:1WC9"
SQ SEQUENCE 180 AA; 20302 MW; B8D57A33D68C0D94 CRC64;
MSRQANRGTE SKKMSSELFT LTYGALVTQL CKDYENDEDV NKQLDRMGYN IGVRLIEDFL
ARSNVGRCHD FRETADVIAK VAFKMYLGIT PSITNWSPAG DEFSLILENN PLVDFVELPD
NHSALIYSNL LCGVLRGALE MVQMAVEAKF VQDTLKGDGV TEIRMRFIRR IEDNLPAGEE
