P40094
PR
Gene name |
COG3 (GRD20, SEC34, YER157W) |
Protein name |
Conserved oligomeric Golgi complex subunit 3 |
Names |
COG complex subunit 3, Component of oligomeric Golgi complex 3, Protein SEC34 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YER157W |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P40094
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P40094-F1 | Predicted | AlphaFoldDB |
18 variants for P40094
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s05-484846 | 22 | S>A | No | SGRP | |
| s05-484855 | 25 | I>V | No | SGRP | |
| s05-484930 | 50 | S>G | No | SGRP | |
| s05-484949 | 56 | V>A | No | SGRP | |
| s05-484997 | 72 | A>V | No | SGRP | |
| s05-485048 | 89 | Q>R | No | SGRP | |
| s05-485283 | 167 | N>K | No | SGRP | |
| s05-485375 | 198 | S>N | No | SGRP | |
| s05-485537 | 252 | T>I | No | SGRP | |
| s05-485594 | 271 | I>T | No | SGRP | |
| s05-485870 | 363 | R>H | No | SGRP | |
| s05-485923 | 381 | I>V | No | SGRP | |
| s05-486287 | 502 | S>N | No | SGRP | |
| s05-486325 | 515 | S>C | No | SGRP | |
| s05-486656 | 625 | V>A | No | SGRP | |
| s05-486877 | 699 | D>N | No | SGRP | |
| s05-486886 | 702 | L>M | No | SGRP | |
| s05-487179 | 799 | I>M | No | SGRP |
No associated diseases with P40094
No regional properties for P40094
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P40094 | |||
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cis-Golgi network | The network of interconnected tubular and cisternal structures located at the convex side of the Golgi apparatus, which abuts the endoplasmic reticulum. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| Golgi transport complex | A multisubunit tethering complex of the CATCHR family (complexes associated with tethering containing helical rods) that has a role in tethering vesicles to the Golgi prior to fusion. Composed of 8 subunits COG1-8. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| cargo adaptor activity | Binding directly to the structural scaffolding elements of a vesicle coat (such as clathrin or COPII), and bridging the membrane, cargo receptor, and membrane deformation machinery. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| autophagy | The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation. |
| autophagy of peroxisome | The process in which peroxisomes are delivered to a type of vacuole and degraded in response to changing nutrient conditions. |
| cytoplasm to vacuole transport by the Cvt pathway | A cytoplasm to vacuole targeting pathway that uses machinery common with autophagy. The Cvt vesicle is formed when the receptor protein, Atg19, binds to the complexes of the target protein (aminopeptidase or alpha-mannosidase homododecamers), forming the Cvt complex. Atg11 binds to Atg9 and transports the Cvt complex to the pre-autophagosome (PAS). The phagophore membrane expands around the Cvt complex (excluding bulk cytoplasm) forming the Cvt vesicle. This pathway is mostly observed in yeast. |
| endoplasmic reticulum to Golgi vesicle-mediated transport | The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi. |
| Golgi organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the Golgi apparatus. |
| intra-Golgi vesicle-mediated transport | The directed movement of substances within the Golgi, mediated by small transport vesicles. These either fuse with the cis-Golgi or with each other to form the membrane stacks known as the cis-Golgi reticulum (network). |
| macroautophagy | The major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane-bounded autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane-bounded structure. Autophagosomes then fuse with a lysosome (or vacuole) releasing single-membrane-bounded autophagic bodies that are then degraded within the lysosome (or vacuole). Some types of macroautophagy, e.g. pexophagy, mitophagy, involve selective targeting of the targets to be degraded. |
| retrograde transport, vesicle recycling within Golgi | The retrograde movement of substances within the Golgi, mediated by COP I vesicles. Cis-Golgi vesicles are constantly moving forward through the Golgi stack by cisternal progression, eventually becoming trans-Golgi vesicles. They then selectively transport membrane and luminal proteins from the trans- to the medial-Golgi while leaving others behind in the trans-Golgi cisternae; similarly, they selectively move proteins from the medial- to the cis-Golgi. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q96JB2 | COG3 | Conserved oligomeric Golgi complex subunit 3 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MARSRKNSLV | RDIASHPTIP | ESQTIVGLLD | DSYLFDKLKK | LSLAVENSDS | LQRTDVSEGC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SEVNGSEATT | SADVKKTNKY | LYYTTYLDQL | NIKIDEYKVV | LDQTRQVNDQ | LDSSIKKFRK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ISQDTGAFIE | ETKTIYEKQS | KLSNLTESIP | KALHYFEVLD | PIMRRLNHAT | SPAIVKKSSF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TTMLATIDES | LRFLDENSDL | KDAAAYRIKF | KQCLIRACEL | ISHFLTNLLK | QTNQEILDKT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KNKNSLTGLP | STTRDAFLYS | KFYTIADTFK | IQVSEIVKRS | NEKAYNKYHD | ELNSILYECF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NHYFQTRLRL | LTPVIWSHID | EIVVKDKDQG | LVKFIQDGKV | YFQQLCADEY | KLFVEFFPEK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ECRFKINQWF | LQLCEPLYDS | IRVRVLKETD | ICTLCDSVTL | FAPYYEFEEG | SEEYVKQFTD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IQYDKLFEPI | VQKVQARLIL | RVQIYVQQNI | LSYRPTRDVF | MISNRRRKSK | TSLQGGNEDA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TTSDDNPDPL | LESYLSSFKN | RSILPISPND | ADDKSIDSEE | STDKISQLQT | YYPPLLKTLA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LLSKIYEMIN | SVVFDDLAHH | VVHDCIVSLR | NAYDMVIKSS | AGKSDFNNLD | ISLAYLKNLL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MLRDSIQNFN | IQYTVNETYL | DFSGVEGFFK | SLKENGRNVL | KKTKSSSILT | LARELVPKVV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NNMVDARTEL | ISELRNVIKD | FTESTSLELI | DDTLDINSDE | DLLSKNVKLR | ENIKARLPRI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| YEQILNYIDD | QEIVTNLLDA | VQELITQSYS | KYYETITELA | ENGKFAKDQV | ADVMYLDVFT |
| 790 | 800 | ||||
| DFFAKEVADL | LRNGDIDTIT | K |