Protein : Qrob_P0242820.2 Q. robur
Protein Identifier  ? Qrob_P0242820.2 Organism . Name  Quercus robur
Score  97.1 Score Type  egn
Protein Description  (M=2) PTHR10121 - COATOMER SUBUNIT DELTA Gene Prediction Quality  validated
Protein length 

Sequence

Length: 553  
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0 Synonyms

7 GO Terms

Identifier Name Description
GO:0005515 protein binding Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
GO:0006886 intracellular protein transport The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
GO:0006810 transport The directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter or pore.
GO:0016192 vesicle-mediated transport A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.
GO:0030131 clathrin adaptor complex A membrane coat adaptor complex that links clathrin to a membrane.
GO:0030126 COPI vesicle coat One of two multimeric complexes that forms a membrane vesicle coat. The mammalian COPI subunits are called alpha-, beta-, beta'-, gamma-, delta-, epsilon- and zeta-COP. Vesicles with COPI coats are found associated with Golgi membranes at steady state.
GO:0006890 retrograde vesicle-mediated transport, Golgi to ER The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.

24 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pmum:103327279 1 552 + 552 Gaps:21 100.00 531 88.70 0.0 coatomer subunit delta
blastp_kegg lcl|pper:PRUPE_ppa004065mg 1 552 + 552 Gaps:21 100.00 531 88.51 0.0 hypothetical protein
blastp_kegg lcl|csv:101222934 1 552 + 552 Gaps:22 100.00 530 89.06 0.0 coatomer subunit delta-like
blastp_kegg lcl|csv:101227874 1 552 + 552 Gaps:22 100.00 530 88.68 0.0 coatomer subunit delta-like
blastp_kegg lcl|cmo:103484537 1 552 + 552 Gaps:22 100.00 530 88.49 0.0 coatomer subunit delta-like
blastp_kegg lcl|cmo:103486369 1 552 + 552 Gaps:22 100.00 530 88.49 0.0 coatomer subunit delta-like
blastp_kegg lcl|csv:101208292 1 552 + 552 Gaps:22 100.00 530 88.11 0.0 coatomer subunit delta-like
blastp_kegg lcl|pxb:103956852 1 552 + 552 Gaps:22 100.00 530 85.28 0.0 coatomer subunit delta-like
blastp_kegg lcl|cit:102614683 1 552 + 552 Gaps:23 100.00 533 87.99 0.0 coatomer subunit delta-like
blastp_kegg lcl|mdm:103405942 1 552 + 552 Gaps:22 100.00 530 84.91 0.0 coatomer subunit delta-like
blastp_uniprot_sprot sp|Q93Y22|COPD_ARATH 1 552 + 552 Gaps:29 100.00 527 79.13 0.0 Coatomer subunit delta OS Arabidopsis thaliana GN At5g05010 PE 1 SV 2
blastp_uniprot_sprot sp|Q0DJ99|COPD2_ORYSJ 1 552 + 552 Gaps:29 100.00 523 74.76 0.0 Coatomer subunit delta-2 OS Oryza sativa subsp. japonica GN Os05g0311000 PE 2 SV 1
blastp_uniprot_sprot sp|Q0DJA0|COPD1_ORYSJ 1 552 + 552 Gaps:30 100.00 524 74.62 0.0 Coatomer subunit delta-1 OS Oryza sativa subsp. japonica GN Os05g0310800 PE 2 SV 1
blastp_uniprot_sprot sp|P49661|COPD3_ORYSJ 1 552 + 552 Gaps:44 100.00 518 73.55 0.0 Coatomer subunit delta-3 OS Oryza sativa subsp. japonica GN Os01g0833700 PE 2 SV 2
blastp_uniprot_sprot sp|Q5XJY5|COPD_MOUSE 1 552 + 552 Gaps:59 100.00 511 45.21 1e-145 Coatomer subunit delta OS Mus musculus GN Arcn1 PE 2 SV 2
blastp_uniprot_sprot sp|Q66H80|COPD_RAT 1 552 + 552 Gaps:59 100.00 511 45.21 2e-145 Coatomer subunit delta OS Rattus norvegicus GN Arcn1 PE 2 SV 1
blastp_uniprot_sprot sp|Q5RA77|COPD_PONAB 1 552 + 552 Gaps:59 100.00 511 45.21 5e-145 Coatomer subunit delta OS Pongo abelii GN ARCN1 PE 2 SV 1
blastp_uniprot_sprot sp|Q5ZL57|COPD_CHICK 1 552 + 552 Gaps:58 100.00 510 44.90 7e-145 Coatomer subunit delta OS Gallus gallus GN ARCN1 PE 2 SV 1
blastp_uniprot_sprot sp|P48444|COPD_HUMAN 1 552 + 552 Gaps:59 100.00 511 45.01 1e-144 Coatomer subunit delta OS Homo sapiens GN ARCN1 PE 1 SV 1
blastp_uniprot_sprot sp|Q0J649|COPD4_ORYSJ 170 552 + 383 Gaps:30 94.41 376 63.10 2e-144 Coatomer subunit delta-4 OS Oryza sativa subsp. japonica GN Os08g0368000 PE 2 SV 1
rpsblast_cdd gnl|CDD|211365 289 544 + 256 Gaps:26 100.00 232 50.00 1e-82 cd09254 AP_delta-COPI_MHD Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit. COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta- gamma- delta- and zeta-COP subunits where beta- and gamma-COP subunits are related to the large AP subunits and delta- and zeta-COP subunits are related to the medium and small AP subunits respectively. Due to the sequence similarity to the AP complexes the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha- beta- and epsilon-COP subunits which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP) which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.
rpsblast_cdd gnl|CDD|189773 288 505 + 218 Gaps:40 84.33 268 26.99 2e-27 pfam00928 Adap_comp_sub Adaptor complexes medium subunit family. This family also contains members which are coatomer subunits.
rpsblast_cdd gnl|CDD|211360 291 512 + 222 Gaps:26 92.05 239 24.09 8e-22 cd07954 AP_MHD_Cterm C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD). This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins delta-subunit of the heteroheptameric coat protein I (delta-COPI) a protein encoded by a pro-death gene referred as MuD (also known as MUDENG mu-2 related death-inducing gene) an endocytic adaptor syp1 the mammalian FCH domain only proteins (FCHo1/2) SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1) and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis promotes vesicle tabulation and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts FCHo1/2 which represent key initial proteins ultimately controlling cellular nutrient uptake receptor regulation and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin which subsequently engage the adaptor complex AP2 and clathrin leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.
rpsblast_kog gnl|CDD|37846 1 552 + 552 Gaps:54 100.00 512 50.78 1e-167 KOG2635 KOG2635 KOG2635 Medium subunit of clathrin adaptor complex [Intracellular trafficking secretion and vesicular transport].

9 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 2 505 504 PTHR10121 none none none
PANTHER 525 552 28 PTHR10121 none none none
Pfam 288 508 221 PF00928 none Adaptor complexes medium subunit family IPR008968
SUPERFAMILY 288 510 223 SSF49447 none none IPR028565
ProSiteProfiles 288 552 265 PS51072 none Mu homology domain (MHD) profile. IPR028565
SUPERFAMILY 5 142 138 SSF64356 none none IPR011012
PANTHER 2 505 504 PTHR10121:SF0 none none IPR027059
PANTHER 525 552 28 PTHR10121:SF0 none none IPR027059
Gene3D 8 141 134 G3DSA:3.30.450.60 none none none

0 Localization

0 Qtllist

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 86   Mitochondrion 4 0.197 0.578 NON-PLANT 86