TPPC4_MOUSE
ID TPPC4_MOUSE Reviewed; 219 AA.
AC Q9ES56; Q9DB31;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Trafficking protein particle complex subunit 4 {ECO:0000305};
DE AltName: Full=Synbindin {ECO:0000303|PubMed:11018053};
DE AltName: Full=TRS23 homolog;
GN Name=Trappc4 {ECO:0000312|MGI:MGI:1926211};
GN Synonyms=Sbdn {ECO:0000303|PubMed:11018053};
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], AND INTERACTION WITH SDC2.
RC TISSUE=Brain;
RX PubMed=11018053; DOI=10.1083/jcb.151.1.53;
RA Ethell I.M., Hagihara K., Miura Y., Irie F., Yamaguchi Y.;
RT "Synbindin, a novel syndecan-2-binding protein in neuronal dendritic
RT spines.";
RL J. Cell Biol. 151:53-68(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-194.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and 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).
CC -!- FUNCTION: Core component of the TRAPP complexes which has a function of
CC guanine nucleotide exchange factor activity for Rab1 GTPase. Plays a
CC role in vesicular transport from endoplasmic reticulum to Golgi and
CC autophagy (By similarity). May play a role in dendrite postsynaptic
CC membrane trafficking (PubMed:11018053). {ECO:0000250|UniProtKB:Q9Y296,
CC ECO:0000269|PubMed:11018053}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3,
CC TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and
CC TRAPPC12 (By similarity). Interacts with SDC2 (PubMed:11018053).
CC {ECO:0000250|UniProtKB:Q9Y296, ECO:0000269|PubMed:11018053}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:11018053}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:11018053}. Endoplasmic reticulum {ECO:0000305}.
CC Vesicle {ECO:0000269|PubMed:11018053}. Note=Associated with
CC postsynaptic membranes and in intracellular cisterns and vesicles
CC (Golgi). {ECO:0000269|PubMed:11018053}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. TRAPPC4
CC subfamily. {ECO:0000305}.
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DR EMBL; AF233340; AAG24950.1; -; mRNA.
DR EMBL; BC038898; AAH38898.1; -; mRNA.
DR EMBL; AK005276; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS23109.1; -.
DR RefSeq; NP_068561.1; NM_021789.2.
DR AlphaFoldDB; Q9ES56; -.
DR SMR; Q9ES56; -.
DR BioGRID; 208560; 5.
DR ComplexPortal; CPX-4764; TRAPP II complex.
DR ComplexPortal; CPX-4766; TRAPP III complex.
DR IntAct; Q9ES56; 2.
DR MINT; Q9ES56; -.
DR STRING; 10090.ENSMUSP00000034623; -.
DR iPTMnet; Q9ES56; -.
DR PhosphoSitePlus; Q9ES56; -.
DR EPD; Q9ES56; -.
DR MaxQB; Q9ES56; -.
DR PaxDb; Q9ES56; -.
DR PRIDE; Q9ES56; -.
DR ProteomicsDB; 258832; -.
DR Antibodypedia; 32564; 306 antibodies from 26 providers.
DR DNASU; 60409; -.
DR Ensembl; ENSMUST00000034623; ENSMUSP00000034623; ENSMUSG00000032112.
DR GeneID; 60409; -.
DR KEGG; mmu:60409; -.
DR UCSC; uc009pdk.1; mouse.
DR CTD; 51399; -.
DR MGI; MGI:1926211; Trappc4.
DR VEuPathDB; HostDB:ENSMUSG00000032112; -.
DR eggNOG; KOG3369; Eukaryota.
DR GeneTree; ENSGT00940000153761; -.
DR HOGENOM; CLU_053380_1_0_1; -.
DR InParanoid; Q9ES56; -.
DR OMA; GQRDGIN; -.
DR OrthoDB; 1504863at2759; -.
DR PhylomeDB; Q9ES56; -.
DR TreeFam; TF314561; -.
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; 60409; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Trappc4; mouse.
DR PRO; PR:Q9ES56; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ES56; protein.
DR Bgee; ENSMUSG00000032112; Expressed in embryonic brain and 279 other tissues.
DR ExpressionAtlas; Q9ES56; baseline and differential.
DR Genevisible; Q9ES56; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
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:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; IC:ComplexPortal.
DR GO; GO:0016358; P:dendrite development; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0006901; P:vesicle coating; IC:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR007233; TRAPPC.
DR PANTHER; PTHR23249; PTHR23249; 1.
DR Pfam; PF04099; Sybindin; 1.
DR SMART; SM01399; Sybindin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Membrane; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transport.
FT CHAIN 1..219
FT /note="Trafficking protein particle complex subunit 4"
FT /id="PRO_0000211570"
SQ SEQUENCE 219 AA; 24385 MW; 7B03F1E772857E92 CRC64;
MAIFSVYVVN KAGGLIYQWD SYSPRAEAEK TFSYPLDLLL KLHDERVLVA FGQRDGIRVG
HAVLAINGMD VNGKYTADGK EVLEYLGNPA NYPVSIRFGR PRLTSNEKLM LASMFHSLFA
IGSQLSPEQG SSGIEMLETD TFKLHCFQTL TGIKFVVLAD PRQAGIDSLL RKIYEIYSDF
ALKNPFYSLE MPIRCELFDQ NLKLALEVAE KAGTFGPGS
