Full text data of TRAPPC3
TRAPPC3
(BET3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Trafficking protein particle complex subunit 3 (BET3 homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Trafficking protein particle complex subunit 3 (BET3 homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43617
ID TPPC3_HUMAN Reviewed; 180 AA.
AC O43617; A6NDN0; B2RDN2; D3DPS2;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Trafficking protein particle complex subunit 3;
DE AltName: Full=BET3 homolog;
GN Name=TRAPPC3; Synonyms=BET3; ORFNames=CDABP0066;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9564032; DOI=10.1093/emboj/17.9.2494;
RA Sacher M., Jiang Y., Barrowman J., Scarpa A., Burston J., Zhang L.,
RA Schieltz D., Yates J.R. III, Abeliovich H., Ferro-Novick S.;
RT "TRAPP, a highly conserved novel complex on the cis-Golgi that
RT mediates vesicle docking and fusion.";
RL EMBO J. 17:2494-2503(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Eva L., Subramaniam V.N., Hong W.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=11805826; DOI=10.1038/415141a;
RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A.,
RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M.,
RA Hoefert C., Schelder M., Brajenovic M., Ruffner H., Merino A.,
RA Klein K., Hudak M., Dickson D., Rudi T., Gnau V., Bauch A.,
RA Bastuck S., Huhse B., Leutwein C., Heurtier M.-A., Copley R.R.,
RA Edelmann A., Querfurth E., Rybin V., Drewes G., Raida M.,
RA Bouwmeester T., Bork P., Seraphin B., Kuster B., Neubauer G.,
RA Superti-Furga G.;
RT "Functional organization of the yeast proteome by systematic analysis
RT of protein complexes.";
RL Nature 415:141-147(2002).
RN [9]
RP IDENTIFICATION IN TRAPP COMPLEX, AND INTERACTION WITH TRAPPC2L.
RX PubMed=19416478; DOI=10.1111/j.1600-0854.2009.00906.x;
RA Scrivens P.J., Shahrzad N., Moores A., Morin A., Brunet S., Sacher M.;
RT "TRAPPC2L is a novel, highly conserved TRAPP-interacting protein.";
RL Traffic 10:724-736(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=21525244; DOI=10.1091/mbc.E10-11-0873;
RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
RT early stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-180, SUBUNIT, MUTAGENESIS
RP OF CYS-68, AND PALMITOYLATION AT CYS-68.
RX PubMed=15692564; DOI=10.1038/sj.emboj.7600565;
RA Turnbull A.P., Kummel D., Prinz B., Holz C., Schultchen J., Lang C.,
RA Niesen F.H., Hofmann K.P., Delbruck H., Behlke J., Muller E.C.,
RA Jarosch E., Sommer T., Heinemann U.;
RT "Structure of palmitoylated BET3: insights into TRAPP complex assembly
RT and membrane localization.";
RL EMBO J. 24:875-884(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-175 IN COMPLEX WITH
RP TRAPPC6A.
RX PubMed=16262728; DOI=10.1111/j.1600-0854.2005.00352.x;
RA Kim M.-S., Yi M.-J., Lee K.-H., Wagner J., Munger C., Kim Y.-G.,
RA Whiteway M., Cygler M., Oh B.-H., Sacher M.;
RT "Biochemical and crystallographic studies reveal a specific
RT interaction between TRAPP subunits Trs33p and Bet3p.";
RL Traffic 6:1183-1195(2005).
CC -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC reticulum to Golgi.
CC -!- SUBUNIT: Homodimer. Component of the multisubunit TRAPP (transport
CC protein particle) complex, which includes at least TRAPPC2,
CC TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9,
CC TRAPPC10, TRAPPC11 and TRAPPC12. Heterodimer with TRAPPC6A. The
CC heterodimer TRAPPC3-TRAPPC6A interacts with TRAPPC2L.
CC -!- INTERACTION:
CC O75865:TRAPPC6A; NbExp=2; IntAct=EBI-743566, EBI-743573;
CC O75865-2:TRAPPC6A; NbExp=3; IntAct=EBI-743566, EBI-8451480;
CC Q86SZ2:TRAPPC6B; NbExp=2; IntAct=EBI-743566, EBI-6160531;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network (By
CC similarity). Endoplasmic reticulum (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43617-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43617-2; Sequence=VSP_047015;
CC Note=Gene prediction based on EST data;
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3
CC subfamily.
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DR EMBL; AJ224335; CAA11902.1; -; mRNA.
DR EMBL; AF041432; AAB96936.1; -; mRNA.
DR EMBL; AY007139; AAG02000.1; -; mRNA.
DR EMBL; AK315610; BAG37979.1; -; mRNA.
DR EMBL; AC114484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07385.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07386.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07387.1; -; Genomic_DNA.
DR EMBL; BC007662; AAH07662.1; -; mRNA.
DR RefSeq; NP_001257823.1; NM_001270894.1.
DR RefSeq; NP_001257824.1; NM_001270895.1.
DR RefSeq; NP_001257825.1; NM_001270896.1.
DR RefSeq; NP_001257826.1; NM_001270897.1.
DR RefSeq; NP_055223.1; NM_014408.4.
DR UniGene; Hs.523131; -.
DR PDB; 1SZ7; X-ray; 1.55 A; A=2-180.
DR PDB; 2C0J; X-ray; 2.20 A; A=15-175.
DR PDB; 2CFH; X-ray; 2.30 A; A/B=1-180.
DR PDB; 3KXC; X-ray; 2.00 A; A=1-180.
DR PDBsum; 1SZ7; -.
DR PDBsum; 2C0J; -.
DR PDBsum; 2CFH; -.
DR PDBsum; 3KXC; -.
DR ProteinModelPortal; O43617; -.
DR SMR; O43617; 13-171.
DR DIP; DIP-47627N; -.
DR IntAct; O43617; 10.
DR MINT; MINT-5002244; -.
DR STRING; 9606.ENSP00000362261; -.
DR PhosphoSite; O43617; -.
DR PaxDb; O43617; -.
DR PRIDE; O43617; -.
DR Ensembl; ENST00000373162; ENSP00000362256; ENSG00000054116.
DR Ensembl; ENST00000373163; ENSP00000362257; ENSG00000054116.
DR Ensembl; ENST00000373166; ENSP00000362261; ENSG00000054116.
DR GeneID; 27095; -.
DR KEGG; hsa:27095; -.
DR UCSC; uc031pls.1; human.
DR CTD; 27095; -.
DR GeneCards; GC01M036602; -.
DR HGNC; HGNC:19942; TRAPPC3.
DR HPA; HPA028408; -.
DR MIM; 610955; gene.
DR neXtProt; NX_O43617; -.
DR PharmGKB; PA134972272; -.
DR eggNOG; NOG286899; -.
DR HOGENOM; HOG000186184; -.
DR HOVERGEN; HBG055045; -.
DR InParanoid; O43617; -.
DR OMA; VGFKMFL; -.
DR OrthoDB; EOG73JKWX; -.
DR PhylomeDB; O43617; -.
DR ChiTaRS; TRAPPC3; human.
DR EvolutionaryTrace; O43617; -.
DR GeneWiki; TRAPPC3; -.
DR GenomeRNAi; 27095; -.
DR NextBio; 35462482; -.
DR PRO; PR:O43617; -.
DR ArrayExpress; O43617; -.
DR Bgee; O43617; -.
DR CleanEx; HS_TRAPPC3; -.
DR Genevestigator; O43617; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0030008; C:TRAPP complex; IEA:Ensembl.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:Ensembl.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR007194; TRAPP_component.
DR InterPro; IPR016721; TRAPP_I_complex_Bet3.
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; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Lipoprotein; Palmitate; Reference proteome; Transport.
FT CHAIN 1 180 Trafficking protein particle complex
FT subunit 3.
FT /FTId=PRO_0000211572.
FT LIPID 68 68 S-palmitoyl cysteine.
FT VAR_SEQ 1 46 Missing (in isoform 2).
FT /FTId=VSP_047015.
FT MUTAGEN 68 68 C->S: Loss of palmitoylation.
FT HELIX 17 34
FT HELIX 37 62
FT HELIX 71 80
FT HELIX 82 87
FT STRAND 92 94
FT STRAND 102 109
FT HELIX 120 122
FT TURN 127 129
FT HELIX 130 140
FT TURN 141 143
FT STRAND 144 152
FT HELIX 154 156
FT STRAND 159 170
SQ SEQUENCE 180 AA; 20274 MW; B5E2D92BE8A39599 CRC64;
MSRQANRGTE SKKMSSELFT LTYGALVTQL CKDYENDEDV NKQLDKMGFN IGVRLIEDFL
ARSNVGRCHD FRETADVIAK VAFKMYLGIT PSITNWSPAG DEFSLILENN PLVDFVELPD
NHSSLIYSNL LCGVLRGALE MVQMAVEAKF VQDTLKGDGV TEIRMRFIRR IEDNLPAGEE
//
ID TPPC3_HUMAN Reviewed; 180 AA.
AC O43617; A6NDN0; B2RDN2; D3DPS2;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Trafficking protein particle complex subunit 3;
DE AltName: Full=BET3 homolog;
GN Name=TRAPPC3; Synonyms=BET3; ORFNames=CDABP0066;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9564032; DOI=10.1093/emboj/17.9.2494;
RA Sacher M., Jiang Y., Barrowman J., Scarpa A., Burston J., Zhang L.,
RA Schieltz D., Yates J.R. III, Abeliovich H., Ferro-Novick S.;
RT "TRAPP, a highly conserved novel complex on the cis-Golgi that
RT mediates vesicle docking and fusion.";
RL EMBO J. 17:2494-2503(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Eva L., Subramaniam V.N., Hong W.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=11805826; DOI=10.1038/415141a;
RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A.,
RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M.,
RA Hoefert C., Schelder M., Brajenovic M., Ruffner H., Merino A.,
RA Klein K., Hudak M., Dickson D., Rudi T., Gnau V., Bauch A.,
RA Bastuck S., Huhse B., Leutwein C., Heurtier M.-A., Copley R.R.,
RA Edelmann A., Querfurth E., Rybin V., Drewes G., Raida M.,
RA Bouwmeester T., Bork P., Seraphin B., Kuster B., Neubauer G.,
RA Superti-Furga G.;
RT "Functional organization of the yeast proteome by systematic analysis
RT of protein complexes.";
RL Nature 415:141-147(2002).
RN [9]
RP IDENTIFICATION IN TRAPP COMPLEX, AND INTERACTION WITH TRAPPC2L.
RX PubMed=19416478; DOI=10.1111/j.1600-0854.2009.00906.x;
RA Scrivens P.J., Shahrzad N., Moores A., Morin A., Brunet S., Sacher M.;
RT "TRAPPC2L is a novel, highly conserved TRAPP-interacting protein.";
RL Traffic 10:724-736(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=21525244; DOI=10.1091/mbc.E10-11-0873;
RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
RT early stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-180, SUBUNIT, MUTAGENESIS
RP OF CYS-68, AND PALMITOYLATION AT CYS-68.
RX PubMed=15692564; DOI=10.1038/sj.emboj.7600565;
RA Turnbull A.P., Kummel D., Prinz B., Holz C., Schultchen J., Lang C.,
RA Niesen F.H., Hofmann K.P., Delbruck H., Behlke J., Muller E.C.,
RA Jarosch E., Sommer T., Heinemann U.;
RT "Structure of palmitoylated BET3: insights into TRAPP complex assembly
RT and membrane localization.";
RL EMBO J. 24:875-884(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-175 IN COMPLEX WITH
RP TRAPPC6A.
RX PubMed=16262728; DOI=10.1111/j.1600-0854.2005.00352.x;
RA Kim M.-S., Yi M.-J., Lee K.-H., Wagner J., Munger C., Kim Y.-G.,
RA Whiteway M., Cygler M., Oh B.-H., Sacher M.;
RT "Biochemical and crystallographic studies reveal a specific
RT interaction between TRAPP subunits Trs33p and Bet3p.";
RL Traffic 6:1183-1195(2005).
CC -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC reticulum to Golgi.
CC -!- SUBUNIT: Homodimer. Component of the multisubunit TRAPP (transport
CC protein particle) complex, which includes at least TRAPPC2,
CC TRAPPC2L, TRAPPC3, TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9,
CC TRAPPC10, TRAPPC11 and TRAPPC12. Heterodimer with TRAPPC6A. The
CC heterodimer TRAPPC3-TRAPPC6A interacts with TRAPPC2L.
CC -!- INTERACTION:
CC O75865:TRAPPC6A; NbExp=2; IntAct=EBI-743566, EBI-743573;
CC O75865-2:TRAPPC6A; NbExp=3; IntAct=EBI-743566, EBI-8451480;
CC Q86SZ2:TRAPPC6B; NbExp=2; IntAct=EBI-743566, EBI-6160531;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network (By
CC similarity). Endoplasmic reticulum (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43617-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43617-2; Sequence=VSP_047015;
CC Note=Gene prediction based on EST data;
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3
CC subfamily.
CC -----------------------------------------------------------------------
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DR EMBL; AJ224335; CAA11902.1; -; mRNA.
DR EMBL; AF041432; AAB96936.1; -; mRNA.
DR EMBL; AY007139; AAG02000.1; -; mRNA.
DR EMBL; AK315610; BAG37979.1; -; mRNA.
DR EMBL; AC114484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07385.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07386.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07387.1; -; Genomic_DNA.
DR EMBL; BC007662; AAH07662.1; -; mRNA.
DR RefSeq; NP_001257823.1; NM_001270894.1.
DR RefSeq; NP_001257824.1; NM_001270895.1.
DR RefSeq; NP_001257825.1; NM_001270896.1.
DR RefSeq; NP_001257826.1; NM_001270897.1.
DR RefSeq; NP_055223.1; NM_014408.4.
DR UniGene; Hs.523131; -.
DR PDB; 1SZ7; X-ray; 1.55 A; A=2-180.
DR PDB; 2C0J; X-ray; 2.20 A; A=15-175.
DR PDB; 2CFH; X-ray; 2.30 A; A/B=1-180.
DR PDB; 3KXC; X-ray; 2.00 A; A=1-180.
DR PDBsum; 1SZ7; -.
DR PDBsum; 2C0J; -.
DR PDBsum; 2CFH; -.
DR PDBsum; 3KXC; -.
DR ProteinModelPortal; O43617; -.
DR SMR; O43617; 13-171.
DR DIP; DIP-47627N; -.
DR IntAct; O43617; 10.
DR MINT; MINT-5002244; -.
DR STRING; 9606.ENSP00000362261; -.
DR PhosphoSite; O43617; -.
DR PaxDb; O43617; -.
DR PRIDE; O43617; -.
DR Ensembl; ENST00000373162; ENSP00000362256; ENSG00000054116.
DR Ensembl; ENST00000373163; ENSP00000362257; ENSG00000054116.
DR Ensembl; ENST00000373166; ENSP00000362261; ENSG00000054116.
DR GeneID; 27095; -.
DR KEGG; hsa:27095; -.
DR UCSC; uc031pls.1; human.
DR CTD; 27095; -.
DR GeneCards; GC01M036602; -.
DR HGNC; HGNC:19942; TRAPPC3.
DR HPA; HPA028408; -.
DR MIM; 610955; gene.
DR neXtProt; NX_O43617; -.
DR PharmGKB; PA134972272; -.
DR eggNOG; NOG286899; -.
DR HOGENOM; HOG000186184; -.
DR HOVERGEN; HBG055045; -.
DR InParanoid; O43617; -.
DR OMA; VGFKMFL; -.
DR OrthoDB; EOG73JKWX; -.
DR PhylomeDB; O43617; -.
DR ChiTaRS; TRAPPC3; human.
DR EvolutionaryTrace; O43617; -.
DR GeneWiki; TRAPPC3; -.
DR GenomeRNAi; 27095; -.
DR NextBio; 35462482; -.
DR PRO; PR:O43617; -.
DR ArrayExpress; O43617; -.
DR Bgee; O43617; -.
DR CleanEx; HS_TRAPPC3; -.
DR Genevestigator; O43617; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0030008; C:TRAPP complex; IEA:Ensembl.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:Ensembl.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR007194; TRAPP_component.
DR InterPro; IPR016721; TRAPP_I_complex_Bet3.
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; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Lipoprotein; Palmitate; Reference proteome; Transport.
FT CHAIN 1 180 Trafficking protein particle complex
FT subunit 3.
FT /FTId=PRO_0000211572.
FT LIPID 68 68 S-palmitoyl cysteine.
FT VAR_SEQ 1 46 Missing (in isoform 2).
FT /FTId=VSP_047015.
FT MUTAGEN 68 68 C->S: Loss of palmitoylation.
FT HELIX 17 34
FT HELIX 37 62
FT HELIX 71 80
FT HELIX 82 87
FT STRAND 92 94
FT STRAND 102 109
FT HELIX 120 122
FT TURN 127 129
FT HELIX 130 140
FT TURN 141 143
FT STRAND 144 152
FT HELIX 154 156
FT STRAND 159 170
SQ SEQUENCE 180 AA; 20274 MW; B5E2D92BE8A39599 CRC64;
MSRQANRGTE SKKMSSELFT LTYGALVTQL CKDYENDEDV NKQLDKMGFN IGVRLIEDFL
ARSNVGRCHD FRETADVIAK VAFKMYLGIT PSITNWSPAG DEFSLILENN PLVDFVELPD
NHSSLIYSNL LCGVLRGALE MVQMAVEAKF VQDTLKGDGV TEIRMRFIRR IEDNLPAGEE
//
MIM
610955
*RECORD*
*FIELD* NO
610955
*FIELD* TI
*610955 TRAFFICKING PROTEIN PARTICLE COMPLEX, SUBUNIT 3; TRAPPC3
;;BET3, YEAST, HOMOLOG OF; BET3
read more*FIELD* TX
DESCRIPTION
TRAPPC3 is a component of the TRAPP complex, which is involved in
tethering of transport vesicles to the cis-Golgi membrane (Turnbull et
al., 2005).
CLONING
Loh et al. (2005) reported that the human TRAPPC3 protein, which they
called BET3, contains 180 amino acids. Northern blot analysis detected
Bet3 expression in all mouse tissues examined. Western blot analysis of
fractionated rat liver showed that most Bet3 was present in the
cytosolic fraction, with a lesser amount in the Golgi-enriched membrane
fraction.
By immunohistochemical analysis, Yu et al. (2006) found that endogenous
BET3 showed perinuclear localization in several mammalian cell lines,
including HeLa cells.
GENE FUNCTION
Loh et al. (2005) found that antibodies against Bet3 inhibited in vitro
transport of the envelope glycoprotein of vesicular stomatitis virus
from the endoplasmic reticulum (ER) to the Golgi apparatus of
semi-intact rat kidney cells in a dose-dependent manner. Cytosol
depleted of Bet3 was also defective in this transport and could be
rescued by recombinant Bet3. Bet3 acted after coat protein II (COPII;
see 601924) but before Rab1 (179508), alpha-Snap (NAPA; 603215), and the
EGTA-sensitive stage during ER-Golgi transport.
Turnbull et al. (2005) found that both human and yeast BET3 were
palmitoylated in recombinant yeast cells, but palmitoylation of BET3 was
only partly responsible for the its membrane localization. Both wildtype
yeast Bet3 and mutant yeast Bet3 lacking palmitoylation rescued cell
viability in Bet3-deleted yeast, suggesting that palmitoylation is not
required for cell viability. Despite high sequence conservation, human
BET3 failed to rescue Bet3-deleted yeast.
In mammalian cells, COPII vesicles derived from the transitional ER do
not tether directly to the Golgi, but rather tether to each other to
form vesicular tubular clusters (VTCs). Using various mammalian cell
lines, including HeLa cells, Yu et al. (2006) showed that BET3 resided
in the transitional ER and adjacent to VTCs. Inactivation of BET3
resulted in accumulation of cargo in membranes that colocalized with the
COPII coat. Using an assay that reconstituted VTC biogenesis in vitro,
Yu et al. (2006) demonstrated that BET3 was required for the tethering
and fusion of COPII vesicles to each other. Depletion of BET3 by small
interfering RNA disrupted a VTC marker and Golgi architecture. Yu et al.
(2006) concluded that BET3 is essential for VTC biogenesis.
Cai et al. (2007) reported that in yeast and mammalian cells the
tethering complex TRAPP I binds to the coat subunit SEC23 (see 610511).
This event requires the BET3 subunit. In vitro studies demonstrated that
the interaction between SEC23 and BET3 targets TRAPP I to COPII vesicles
to mediate vesicle tethering. Cai et al. (2007) proposed that the
binding of TRAPP I to SEC23 marks a coated vesicle for fusion with
another COPII vesicle or the Golgi apparatus. An implication of these
findings is that the intracellular destination of a transport vesicle
may be determined in part by its coat and its associated cargo.
BIOCHEMICAL FEATURES
Turnbull et al. (2005) determined the crystal structure of human BET3 to
1.55-angstrom resolution. BET3 assumes an alpha/beta-plait topology
constructed by a twisted, antiparallel, 4-stranded beta sheet on one
side, with the 5 alpha helices forming the other side of the structural
motif. BET3 forms a dimer around the crystallographic 2-fold axis. A
hydrophobic pocket within the core of the alpha-helical face contains an
internal palmitate molecule covalently attached through a thioester
linkage to the conserved cys68.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TRAPPC3
gene to chromosome 1 (TMAP RH80455).
*FIELD* RF
1. Cai, H.; Yu, S.; Menon, S.; Cai, Y.; Lazarova, D.; Fu, C.; Reinisch,
K.; Hay, J. C.; Ferro-Novick, S.: TRAPPI tethers COPII vesicles by
binding the coat subunit Sec23. Nature 445: 941-944, 2007.
2. Loh, E.; Peter, F.; Subramaniam, V. N.; Hong, W.: Mammalian Bet3
functions as a cytosolic factor participating in transport from the
ER to the Golgi apparatus. J. Cell Sci. 118: 1209-1222, 2005.
3. Turnbull, A. P.; Kummel, D.; Prinz, B.; Holz, C.; Schultchen, J.;
Lang, C.; Niesen, F. H.; Hofmann, K.-P.; Delbruck, H.; Behlke, J.;
Muller, E.-C.; Jarosch, E.; Sommer, T.; Heinemann, U.: Structure
of palmitoylated BET3: insights into TRAPP complex assembly and membrane
localization. EMBO J. 24: 875-884, 2005.
4. Yu, S.; Satoh, A.; Pypaert, M.; Mullen, K.; Hay, J. C.; Ferro-Novick,
S.: mBet3p is required for homotypic COPII vesicle tethering in mammalian
cells. J. Cell Biol. 174: 359-368, 2006.
*FIELD* CN
Ada Hamosh - updated: 6/29/2007
*FIELD* CD
Patricia A. Hartz: 4/20/2007
*FIELD* ED
alopez: 07/03/2007
terry: 6/29/2007
mgross: 4/20/2007
*RECORD*
*FIELD* NO
610955
*FIELD* TI
*610955 TRAFFICKING PROTEIN PARTICLE COMPLEX, SUBUNIT 3; TRAPPC3
;;BET3, YEAST, HOMOLOG OF; BET3
read more*FIELD* TX
DESCRIPTION
TRAPPC3 is a component of the TRAPP complex, which is involved in
tethering of transport vesicles to the cis-Golgi membrane (Turnbull et
al., 2005).
CLONING
Loh et al. (2005) reported that the human TRAPPC3 protein, which they
called BET3, contains 180 amino acids. Northern blot analysis detected
Bet3 expression in all mouse tissues examined. Western blot analysis of
fractionated rat liver showed that most Bet3 was present in the
cytosolic fraction, with a lesser amount in the Golgi-enriched membrane
fraction.
By immunohistochemical analysis, Yu et al. (2006) found that endogenous
BET3 showed perinuclear localization in several mammalian cell lines,
including HeLa cells.
GENE FUNCTION
Loh et al. (2005) found that antibodies against Bet3 inhibited in vitro
transport of the envelope glycoprotein of vesicular stomatitis virus
from the endoplasmic reticulum (ER) to the Golgi apparatus of
semi-intact rat kidney cells in a dose-dependent manner. Cytosol
depleted of Bet3 was also defective in this transport and could be
rescued by recombinant Bet3. Bet3 acted after coat protein II (COPII;
see 601924) but before Rab1 (179508), alpha-Snap (NAPA; 603215), and the
EGTA-sensitive stage during ER-Golgi transport.
Turnbull et al. (2005) found that both human and yeast BET3 were
palmitoylated in recombinant yeast cells, but palmitoylation of BET3 was
only partly responsible for the its membrane localization. Both wildtype
yeast Bet3 and mutant yeast Bet3 lacking palmitoylation rescued cell
viability in Bet3-deleted yeast, suggesting that palmitoylation is not
required for cell viability. Despite high sequence conservation, human
BET3 failed to rescue Bet3-deleted yeast.
In mammalian cells, COPII vesicles derived from the transitional ER do
not tether directly to the Golgi, but rather tether to each other to
form vesicular tubular clusters (VTCs). Using various mammalian cell
lines, including HeLa cells, Yu et al. (2006) showed that BET3 resided
in the transitional ER and adjacent to VTCs. Inactivation of BET3
resulted in accumulation of cargo in membranes that colocalized with the
COPII coat. Using an assay that reconstituted VTC biogenesis in vitro,
Yu et al. (2006) demonstrated that BET3 was required for the tethering
and fusion of COPII vesicles to each other. Depletion of BET3 by small
interfering RNA disrupted a VTC marker and Golgi architecture. Yu et al.
(2006) concluded that BET3 is essential for VTC biogenesis.
Cai et al. (2007) reported that in yeast and mammalian cells the
tethering complex TRAPP I binds to the coat subunit SEC23 (see 610511).
This event requires the BET3 subunit. In vitro studies demonstrated that
the interaction between SEC23 and BET3 targets TRAPP I to COPII vesicles
to mediate vesicle tethering. Cai et al. (2007) proposed that the
binding of TRAPP I to SEC23 marks a coated vesicle for fusion with
another COPII vesicle or the Golgi apparatus. An implication of these
findings is that the intracellular destination of a transport vesicle
may be determined in part by its coat and its associated cargo.
BIOCHEMICAL FEATURES
Turnbull et al. (2005) determined the crystal structure of human BET3 to
1.55-angstrom resolution. BET3 assumes an alpha/beta-plait topology
constructed by a twisted, antiparallel, 4-stranded beta sheet on one
side, with the 5 alpha helices forming the other side of the structural
motif. BET3 forms a dimer around the crystallographic 2-fold axis. A
hydrophobic pocket within the core of the alpha-helical face contains an
internal palmitate molecule covalently attached through a thioester
linkage to the conserved cys68.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TRAPPC3
gene to chromosome 1 (TMAP RH80455).
*FIELD* RF
1. Cai, H.; Yu, S.; Menon, S.; Cai, Y.; Lazarova, D.; Fu, C.; Reinisch,
K.; Hay, J. C.; Ferro-Novick, S.: TRAPPI tethers COPII vesicles by
binding the coat subunit Sec23. Nature 445: 941-944, 2007.
2. Loh, E.; Peter, F.; Subramaniam, V. N.; Hong, W.: Mammalian Bet3
functions as a cytosolic factor participating in transport from the
ER to the Golgi apparatus. J. Cell Sci. 118: 1209-1222, 2005.
3. Turnbull, A. P.; Kummel, D.; Prinz, B.; Holz, C.; Schultchen, J.;
Lang, C.; Niesen, F. H.; Hofmann, K.-P.; Delbruck, H.; Behlke, J.;
Muller, E.-C.; Jarosch, E.; Sommer, T.; Heinemann, U.: Structure
of palmitoylated BET3: insights into TRAPP complex assembly and membrane
localization. EMBO J. 24: 875-884, 2005.
4. Yu, S.; Satoh, A.; Pypaert, M.; Mullen, K.; Hay, J. C.; Ferro-Novick,
S.: mBet3p is required for homotypic COPII vesicle tethering in mammalian
cells. J. Cell Biol. 174: 359-368, 2006.
*FIELD* CN
Ada Hamosh - updated: 6/29/2007
*FIELD* CD
Patricia A. Hartz: 4/20/2007
*FIELD* ED
alopez: 07/03/2007
terry: 6/29/2007
mgross: 4/20/2007