The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
Functional site class:
ER export signals
Functional site description:
Signals found in the cytoplasmic tail of cargo receptors and facilitating their ER to Golgi anterograde transport by binding to COPII.
ELM Description:
The diPhe motif found in the cytoplasmic tail of all members of the p24/GP25 family of cargo receptors involved in vesicle trafficking. It is responsible for their binding to COPII, the coatomer driving the anterograde ER-to-Golgi transport. Importantly, the cytoplasmic domain of these proteins has been shown to mediate (1) the recruitment of ARF1 to Golgi membrane allowing subsequent coatomer recruitment (Gommel,2001) and (2) a conformational change and polymerisation of the coatomer, possibly driving the budding of vesicles at the CGN (Reinhard,1999).
Pattern: Q.{6,6}FF.{6,7}$
Pattern Probability: 6.801e-08
Present in taxons: Canis lupus familiaris Cricetulus griseus Homo sapiens Opisthokonta Oryctolagus cuniculus Rattus norvegicus Saccharomyces cerevisiae Xenopus laevis
Interaction Domain:
WD40 (PF00400) WD domain, G-beta repeat (Stochiometry: 1 : 1)
o See 11 Instances for TRG_Golgi_diPhe_1
o Abstract
In eukaryotic cells the secretory pathway consists of series of compartments that modify, transport and sort secretory cargo. Coat protein complexes are responsible for vesicle formation during the transport events and recognition of signals exposed to those complexes insure sorting and targeting of proteins between the various compartments. Cargo transport molecules bear at their C-terminus (cytoplasmic) short motifs used to direct them to and or retain them in specific compartments. For example DXE motif facilitates ER export of post-ER resident proteins and di-Phenylalanine (diPhe) motif drives anterograde ER to Golgi transport of cargo receptors.
In order to recycle some organellar components and cargo selecting molecules while the secretory cargo advances the transport within the secretory pathway has to be bidirectional. Anterograde transport is catalysed by COPII coat protein complex and retrograde transport involves COPI complex. Some proteins bear determinants allowing them to undergo transport in both directions. In many instances the diPhe motif of some cargo receptors cycling between the ER and the Golgi apparatus coexists with a diLys motif: it has been proposed that the diPhe motif triggers anterograde transport between ER and Golgi (binding to COPII), while the diLysine motif (TRG_ER_diLys_1) triggers return to the ER. The members of the p24 family are examples of diPhe bearing type I integral membrane proteins: they are involved in vesicle trafficking and reside at the cis Golgi network under steady state conditions. Their cytoplasmic tail mediates the recruitment of ARF1-GDP (ADP-ribosylation factor 1) to Golgi membranes (Gommel,2001), subsequently membrane bound ARF1-GTP triggers the recruitment of coatomer.
o 5 selected references:

o 13 GO-Terms:

o 11 Instances for TRG_Golgi_diPhe_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
P49020 TMED2
182 196 AMTLGQIYYLKRFFEVRRVV TP 1 Cricetulus griseus (Chinese hamster)
Q63524 Tmed2
187 201 AMTLGQIYYLKRFFEVRRVV TP 1 Rattus norvegicus (Norway rat)
P32803 EMP24
189 203 ANSLFQIYYLRRFFEVTSLV TP 1 Saccharomyces cerevisiae (Baker"s yeast)
Q28735 TMED10
204 219 LATWQVFYLRRFFKAKKLIE TP 1 Oryctolagus cuniculus (Rabbit)
P27869 TMED11
201 215 AIGIFQMKSLKNFFIAKKLV TP 1 Canis lupus familiaris (Dog)
P53198 ERP6
202 216 IICVWQMKSLRSFFVKQKVL TP 2 Saccharomyces cerevisiae (Baker"s yeast)
P38819 ERP5
198 212 GTCAFQLRYLKNFFVKQKVV TP 2 Saccharomyces cerevisiae (Baker"s yeast)
Q91841 Translocon-as
190 205 LATWQVCYLRHFFKAKKLIE TP 1 Xenopus laevis (African clawed frog)
Q15363 TMED2
187 201 AMTLGQIYYLKRFFEVRRVV TP 6 Homo sapiens (Human)
221 235 AIGVWQMRHLKSFFEAKKLV TP 6 Homo sapiens (Human)
P49755 TMED10
204 219 LATWQVFYLRRFFKAKKLIE TP 6 Homo sapiens (Human)
Please cite: The Eukaryotic Linear Motif resource: 2022 release. (PMID:34718738)

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