TPPC3_HUMAN
ID TPPC3_HUMAN Reviewed; 180 AA.
AC O43617; A6NDN0; B2RDN2; D3DPS2;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Trafficking protein particle complex subunit 3;
DE AltName: Full=BET3 homolog;
GN Name=TRAPPC3 {ECO:0000303|PubMed:19416478, ECO:0000312|HGNC:HGNC:19942};
GN Synonyms=BET3 {ECO:0000303|PubMed:11805826}; ORFNames=CDABP0066;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 mediates
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Hoefert C.,
RA Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M.,
RA Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C.,
RA Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V.,
RA Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B.,
RA Neubauer G., Superti-Furga G.;
RT "Functional organization of the yeast proteome by systematic analysis of
RT 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., Buerckstuemmer T.,
RA 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 early
RT stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-180, SUBUNIT, MUTAGENESIS OF
RP 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., Jarosch E.,
RA Sommer T., Heinemann U.;
RT "Structure of palmitoylated BET3: insights into TRAPP complex assembly and
RT membrane localization.";
RL EMBO J. 24:875-884(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-175 IN COMPLEX WITH 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 interaction
RT between TRAPP subunits Trs33p and Bet3p.";
RL Traffic 6:1183-1195(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH TRAPPC6B, SUBUNIT,
RP INTERACTION WITH TRAPPC6B AND TRAPPC1, AND MUTAGENESIS OF 33-ASP--GLU-35.
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).
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 (PubMed:11805826,
CC PubMed:15692564, PubMed:16262728, PubMed:19416478, PubMed:21525244).
CC Heterodimer with TRAPPC6b. The heterodimer TRAPPC6B-TRAPPC3 interacts
CC with TRAPPC1 likely providing a core for TRAPP complex formation
CC (PubMed:16828797). {ECO:0000269|PubMed:11805826,
CC ECO:0000269|PubMed:15692564, ECO:0000269|PubMed:16262728,
CC ECO:0000269|PubMed:16828797, ECO:0000269|PubMed:19416478,
CC ECO:0000269|PubMed:21525244}.
CC -!- INTERACTION:
CC O43617; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-743566, EBI-742388;
CC O43617; Q9Y5R8: TRAPPC1; NbExp=6; IntAct=EBI-743566, EBI-6160554;
CC O43617; A5PLN9: TRAPPC13; NbExp=2; IntAct=EBI-743566, EBI-2857298;
CC O43617; P0DI81-3: TRAPPC2; NbExp=8; IntAct=EBI-743566, EBI-11961968;
CC O43617; Q9UL33: TRAPPC2L; NbExp=6; IntAct=EBI-743566, EBI-747601;
CC O43617; Q9UL33-2: TRAPPC2L; NbExp=7; IntAct=EBI-743566, EBI-11119202;
CC O43617; Q8IUR0: TRAPPC5; NbExp=7; IntAct=EBI-743566, EBI-3246160;
CC O43617; O75865: TRAPPC6A; NbExp=9; IntAct=EBI-743566, EBI-743573;
CC O43617; O75865-2: TRAPPC6A; NbExp=6; IntAct=EBI-743566, EBI-8451480;
CC O43617; Q86SZ2: TRAPPC6B; NbExp=3; IntAct=EBI-743566, EBI-6160531;
CC O43617; Q9Y2L5: TRAPPC8; NbExp=2; IntAct=EBI-743566, EBI-2820056;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily.
CC {ECO:0000305}.
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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 CCDS; CCDS404.1; -. [O43617-1]
DR CCDS; CCDS59194.1; -. [O43617-2]
DR RefSeq; NP_001257823.1; NM_001270894.1.
DR RefSeq; NP_001257824.1; NM_001270895.1. [O43617-2]
DR RefSeq; NP_001257825.1; NM_001270896.1. [O43617-2]
DR RefSeq; NP_001257826.1; NM_001270897.1.
DR RefSeq; NP_055223.1; NM_014408.4. [O43617-1]
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 AlphaFoldDB; O43617; -.
DR SMR; O43617; -.
DR BioGRID; 117997; 68.
DR ComplexPortal; CPX-4749; TRAPP II complex, TRAPPC2 variant.
DR ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant.
DR ComplexPortal; CPX-6902; TRAPP II complex, TRAPPC2B variant.
DR ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant.
DR CORUM; O43617; -.
DR DIP; DIP-47627N; -.
DR IntAct; O43617; 32.
DR MINT; O43617; -.
DR STRING; 9606.ENSP00000480332; -.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB03796; Palmitic Acid.
DR DrugBank; DB08342; S-palmitoyl-L-cysteine.
DR iPTMnet; O43617; -.
DR PhosphoSitePlus; O43617; -.
DR SwissPalm; O43617; -.
DR BioMuta; TRAPPC3; -.
DR EPD; O43617; -.
DR jPOST; O43617; -.
DR MassIVE; O43617; -.
DR MaxQB; O43617; -.
DR PaxDb; O43617; -.
DR PeptideAtlas; O43617; -.
DR PRIDE; O43617; -.
DR ProteomicsDB; 49084; -. [O43617-1]
DR ProteomicsDB; 918; -.
DR TopDownProteomics; O43617-1; -. [O43617-1]
DR Antibodypedia; 31641; 224 antibodies from 28 providers.
DR DNASU; 27095; -.
DR Ensembl; ENST00000373162.5; ENSP00000362256.1; ENSG00000054116.12. [O43617-2]
DR Ensembl; ENST00000373163.5; ENSP00000362257.1; ENSG00000054116.12. [O43617-2]
DR Ensembl; ENST00000373166.8; ENSP00000362261.3; ENSG00000054116.12. [O43617-1]
DR Ensembl; ENST00000617904.4; ENSP00000480648.1; ENSG00000054116.12. [O43617-2]
DR GeneID; 27095; -.
DR KEGG; hsa:27095; -.
DR MANE-Select; ENST00000373166.8; ENSP00000362261.3; NM_014408.5; NP_055223.1.
DR UCSC; uc001bzx.5; human. [O43617-1]
DR CTD; 27095; -.
DR DisGeNET; 27095; -.
DR GeneCards; TRAPPC3; -.
DR HGNC; HGNC:19942; TRAPPC3.
DR HPA; ENSG00000054116; Low tissue specificity.
DR MIM; 610955; gene.
DR neXtProt; NX_O43617; -.
DR OpenTargets; ENSG00000054116; -.
DR PharmGKB; PA134972272; -.
DR VEuPathDB; HostDB:ENSG00000054116; -.
DR eggNOG; KOG3330; Eukaryota.
DR GeneTree; ENSGT00390000003880; -.
DR HOGENOM; CLU_087110_2_0_1; -.
DR InParanoid; O43617; -.
DR OrthoDB; 1334804at2759; -.
DR PhylomeDB; O43617; -.
DR TreeFam; TF300091; -.
DR PathwayCommons; O43617; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; O43617; -.
DR BioGRID-ORCS; 27095; 781 hits in 1086 CRISPR screens.
DR ChiTaRS; TRAPPC3; human.
DR EvolutionaryTrace; O43617; -.
DR GeneWiki; TRAPPC3; -.
DR GenomeRNAi; 27095; -.
DR Pharos; O43617; Tbio.
DR PRO; PR:O43617; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43617; protein.
DR Bgee; ENSG00000054116; Expressed in right adrenal gland and 214 other tissues.
DR ExpressionAtlas; O43617; baseline and differential.
DR Genevisible; O43617; HS.
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:HPA.
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; IDA:UniProtKB.
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; IBA:GO_Central.
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; Alternative splicing; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Lipoprotein; Palmitate;
KW Reference proteome; Transport.
FT CHAIN 1..180
FT /note="Trafficking protein particle complex subunit 3"
FT /id="PRO_0000211572"
FT LIPID 68
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:15692564"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047015"
FT MUTAGEN 33..35
FT /note="DYE->KVR: Impairs interaction with TRAPPC1."
FT /evidence="ECO:0000269|PubMed:16828797"
FT MUTAGEN 68
FT /note="C->S: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:15692564"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:1SZ7"
FT HELIX 37..62
FT /evidence="ECO:0007829|PDB:1SZ7"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:1SZ7"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:1SZ7"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1SZ7"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1SZ7"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1SZ7"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1SZ7"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:1SZ7"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1SZ7"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:1SZ7"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1SZ7"
FT STRAND 159..170
FT /evidence="ECO:0007829|PDB:1SZ7"
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
