TPPC2_MOUSE
ID TPPC2_MOUSE Reviewed; 140 AA.
AC Q9CQP2; Q8BP61; Q9CQF5; Q9D0V3; Q9DCM3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Trafficking protein particle complex subunit 2;
DE AltName: Full=Sedlin;
GN Name=Trappc2; Synonyms=Sedl;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, Pancreas, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Mammary gland;
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 INTERACTION WITH TRAPPC3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ASP-47; SER-73; PHE-83 AND VAL-130.
RX PubMed=19650763; DOI=10.1042/bj20090541;
RA Choi M.Y., Chan C.C.Y., Chan D., Luk K.D.K., Cheah K.S.E., Tanner J.A.;
RT "Biochemical consequences of sedlin mutations that cause spondyloepiphyseal
RT dysplasia tarda.";
RL Biochem. J. 423:233-242(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=12361953; DOI=10.1074/jbc.m207436200;
RA Jang S.B., Kim Y.-G., Cho Y.-S., Suh P.-G., Kim K.-H., Oh B.-H.;
RT "Crystal structure of SEDL and its implications for a genetic disease
RT spondyloepiphyseal dysplasia tarda.";
RL J. Biol. Chem. 277:49863-49869(2002).
CC -!- FUNCTION: Prevents ENO1-mediated transcriptional repression and
CC antagonizes ENO1-mediated cell death. May play a role in vesicular
CC transport from endoplasmic reticulum to Golgi (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein particle)
CC complex. Interacts with ENO1, PITX1, SF1 and TRAPPC2L (By similarity).
CC Interacts with TRAPPC3. {ECO:0000250, ECO:0000269|PubMed:19650763}.
CC -!- INTERACTION:
CC Q9CQP2; Q8K3V1: Spata4; NbExp=3; IntAct=EBI-1172267, EBI-7067375;
CC Q9CQP2; Q96Q05: TRAPPC9; Xeno; NbExp=2; IntAct=EBI-1172267, EBI-6160596;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:19650763}. Nucleus {ECO:0000250|UniProtKB:P0DI81}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:P0DI81}. Cytoplasm
CC {ECO:0000269|PubMed:19650763}. Note=Localized in perinuclear granular
CC structures. {ECO:0000269|PubMed:19650763}.
CC -!- TISSUE SPECIFICITY: Expressed in chondrocytes at various stages of
CC differentiation, including proliferating, prehypertrophic and
CC hypertrophic chondrocytes in the distal femoral joint.
CC {ECO:0000269|PubMed:19650763}.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. Sedlin
CC subfamily. {ECO:0000305}.
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DR EMBL; AK008564; BAB25747.1; -; mRNA.
DR EMBL; AK007889; BAB25332.1; -; mRNA.
DR EMBL; AK002658; BAB22265.1; -; mRNA.
DR EMBL; AK004389; BAB23284.1; -; mRNA.
DR EMBL; AK007568; BAB25114.1; -; mRNA.
DR EMBL; AK002369; BAB22047.1; -; mRNA.
DR EMBL; AK004363; BAB23275.1; -; mRNA.
DR EMBL; AK077643; BAC36921.1; -; mRNA.
DR EMBL; BC034845; AAH34845.1; -; mRNA.
DR EMBL; BC061087; AAH61087.1; -; mRNA.
DR CCDS; CCDS41208.1; -.
DR RefSeq; NP_001300651.1; NM_001313722.1.
DR RefSeq; NP_079595.1; NM_025319.2.
DR RefSeq; NP_079708.2; NM_025432.4.
DR RefSeq; XP_006533980.1; XM_006533917.3.
DR RefSeq; XP_006533981.1; XM_006533918.2.
DR RefSeq; XP_006533982.1; XM_006533919.2.
DR PDB; 1H3Q; X-ray; 2.40 A; A=1-140.
DR PDB; 2J3W; X-ray; 2.10 A; A/C=1-140.
DR PDBsum; 1H3Q; -.
DR PDBsum; 2J3W; -.
DR AlphaFoldDB; Q9CQP2; -.
DR SMR; Q9CQP2; -.
DR BioGRID; 211310; 4.
DR ComplexPortal; CPX-4764; TRAPP II complex.
DR ComplexPortal; CPX-4766; TRAPP III complex.
DR IntAct; Q9CQP2; 10.
DR MINT; Q9CQP2; -.
DR STRING; 10090.ENSMUSP00000112195; -.
DR iPTMnet; Q9CQP2; -.
DR PhosphoSitePlus; Q9CQP2; -.
DR EPD; Q9CQP2; -.
DR MaxQB; Q9CQP2; -.
DR PaxDb; Q9CQP2; -.
DR PRIDE; Q9CQP2; -.
DR ProteomicsDB; 259170; -.
DR Antibodypedia; 52678; 3 antibodies from 1 providers.
DR DNASU; 66050; -.
DR DNASU; 66226; -.
DR Ensembl; ENSMUST00000112194; ENSMUSP00000107813; ENSMUSG00000079317.
DR Ensembl; ENSMUST00000116495; ENSMUSP00000112195; ENSMUSG00000079317.
DR GeneID; 66050; -.
DR GeneID; 66226; -.
DR KEGG; mmu:66050; -.
DR KEGG; mmu:66226; -.
DR UCSC; uc009uws.1; mouse.
DR CTD; 6399; -.
DR MGI; MGI:1913476; Trappc2.
DR VEuPathDB; HostDB:ENSMUSG00000079317; -.
DR eggNOG; KOG3487; Eukaryota.
DR GeneTree; ENSGT00510000047168; -.
DR HOGENOM; CLU_085828_0_2_1; -.
DR InParanoid; Q9CQP2; -.
DR OMA; VDKFNQW; -.
DR OrthoDB; 1426075at2759; -.
DR PhylomeDB; Q9CQP2; -.
DR TreeFam; TF314814; -.
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; 66050; 2 hits in 71 CRISPR screens.
DR BioGRID-ORCS; 66226; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Trappc2; mouse.
DR EvolutionaryTrace; Q9CQP2; -.
DR PRO; PR:Q9CQP2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CQP2; protein.
DR Bgee; ENSMUSG00000079317; Expressed in dentate gyrus of hippocampal formation granule cell and 68 other tissues.
DR ExpressionAtlas; Q9CQP2; baseline and differential.
DR Genevisible; Q9CQP2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO: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:0001222; F:transcription corepressor binding; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
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:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; ISO:MGI.
DR GO; GO:0006901; P:vesicle coating; IC:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR006722; Sedlin.
DR PANTHER; PTHR12403; PTHR12403; 1.
DR Pfam; PF04628; Sedlin_N; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; ER-Golgi transport; Nucleus; Reference proteome;
KW Transcription; Transport.
FT CHAIN 1..140
FT /note="Trafficking protein particle complex subunit 2"
FT /id="PRO_0000211567"
FT MUTAGEN 47
FT /note="D->Y: Increased interaction with TRAPPC3."
FT /evidence="ECO:0000269|PubMed:19650763"
FT MUTAGEN 73
FT /note="S->L: Aberrant protein folding and increased
FT proteasomal degradation."
FT /evidence="ECO:0000269|PubMed:19650763"
FT MUTAGEN 83
FT /note="F->S: Aberrant protein folding and increased
FT proteasomal degradation."
FT /evidence="ECO:0000269|PubMed:19650763"
FT MUTAGEN 130
FT /note="V->D: Aberrant protein folding and increased
FT proteasomal degradation."
FT /evidence="ECO:0000269|PubMed:19650763"
FT CONFLICT 7
FT /note="F -> I (in Ref. 1; BAB22265)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="P -> A (in Ref. 1; BAB25114/BAB22047/BAB23275)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="D -> E (in Ref. 1; BAB25114/BAB22047/BAB23275)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="F -> L (in Ref. 1; BAB25114/BAB22047/BAB23275)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="Q -> H (in Ref. 1; BAB25114/BAB22047/BAB23275)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="F -> L (in Ref. 1; BAB23284)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="R -> Q (in Ref. 1; BAC36921)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="D -> E (in Ref. 1; BAB25114/BAB22047/BAB23275)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="S -> N (in Ref. 1; BAB25114/BAB22047/BAB23275)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2J3W"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:2J3W"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2J3W"
FT HELIX 31..52
FT /evidence="ECO:0007829|PDB:2J3W"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2J3W"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:2J3W"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2J3W"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2J3W"
FT HELIX 92..111
FT /evidence="ECO:0007829|PDB:2J3W"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:2J3W"
SQ SEQUENCE 140 AA; 16441 MW; 6EE89427D223FCB0 CRC64;
MSGSFYFVIV GHHDNPVFEM EFLPPGKAES KDDHRHLNQF IAHAALDLVD ENMWLSNNMY
LKTVDKFNEW FVSAFVTAGH MRFIMLHDVR QEDGIKNFFT DVYDLYIKFA MNPFYEPNSP
IRSSAFDRKV QFLGKKHLLS
